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  • Articles  (126)
  • Rats  (84)
  • Amino Acid Sequence  (43)
  • American Association for the Advancement of Science (AAAS)  (126)
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  • Articles  (126)
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  • American Association for the Advancement of Science (AAAS)  (126)
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  • 1
    Publication Date: 1986-10-17
    Description: The regulation of nerve growth factor (NGF) protein and NGF messenger RNA (mRNA) in the developing rat brain has been studied to assess the hypothesis that NGF supports the differentiation of cholinergic neurons in the basal forebrain. In the adult, the major targets of these neurons, the hippocampus and neocortex, contain the highest concentrations of NGF mRNA, but comparatively low ratios of NGF protein to its mRNA. In contrast, a high concentration of NGF protein and a low concentration of NGF mRNA were seen in the basal forebrain, consistent with retrograde transport of NGF protein into this region from the neocortex and hippocampus. In these two target regions NGF and NGF mRNA were barely detectable at birth, their concentrations increased to a peak at day 21, and then NGF mRNA, but not NGF protein, declined threefold by day 35. NGF accumulation in the basal forebrain paralleled that in the target regions and preceded an increase in choline acetyltransferase, suggesting that the differentiation of cholinergic projection neurons is indeed regulated by retrogradely transported NGF. In addition, high ratios of NGF protein to NGF mRNA, comparable to that in the basal forebrain, were seen in the olfactory bulb and cerebellum, suggesting that NGF may be transported into these regions by unidentified neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Large, T H -- Bodary, S C -- Clegg, D O -- Weskamp, G -- Otten, U -- Reichardt, L F -- NS21824/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 17;234(4774):352-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3764415" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*growth & development/metabolism ; Brain Chemistry ; Cerebellum/analysis ; Cerebral Cortex/analysis ; Hippocampus/analysis ; Nerve Growth Factors/analysis/*biosynthesis/genetics ; RNA, Messenger/analysis ; Rats ; Rats, Inbred Strains
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  • 2
    Publication Date: 1986-11-07
    Description: Binding of antibodies to effector cells by way of receptors to their constant regions (Fc receptors) is central to the pathway that leads to clearance of antigens by the immune system. The structure and function of this important class of receptors on immune cells is addressed through the molecular characterization of Fc receptors (FcR) specific for the murine immunoglobulin G isotype. Structural diversity is encoded by two genes that by alternative splicing result in expression of molecules with highly conserved extracellular domains and different transmembrane and intracytoplasmic domains. The proteins encoded by these genes are members of the immunoglobulin supergene family, most homologous to the major histocompatibility complex molecule E beta. Functional reconstitution of ligand binding by transfection of individual FcR genes demonstrates that the requirements for ligand binding are encoded in a single gene. These studies demonstrate the molecular basis for the functional heterogeneity of FcR's, accounting for the possible transduction of different signals in response to a single ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ravetch, J V -- Luster, A D -- Weinshank, R -- Kochan, J -- Pavlovec, A -- Portnoy, D A -- Hulmes, J -- Pan, Y C -- Unkeless, J C -- AI 24322/AI/NIAID NIH HHS/ -- GM 36306/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):718-25.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2946078" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/genetics ; Gene Expression Regulation ; Histocompatibility Antigens Class II/genetics ; Immunoglobulin G ; Lymphocytes/*physiology ; Macrophages/*physiology ; Membrane Proteins ; Mice ; Protein Conformation ; *Receptors, Fc/genetics ; Receptors, IgG ; Transcription, Genetic ; Transfection
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  • 3
    Publication Date: 1986-02-28
    Description: Transgenic mice expressing a metallothionein-somatostatin fusion gene contain high concentrations of somatostatin in the anterior pituitary gland, a tissue that does not normally produce somatostatin. Immunoreactive somatostatin within the anterior pituitaries was found exclusively within gonadotrophs. Similarly, a metallothionein-human growth-hormone fusion gene was also expressed selectively in gonadotrophs. It is proposed that sequences common to the two fusion genes are responsible for the gonadotroph-specific expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Low, M J -- Lechan, R M -- Hammer, R E -- Brinster, R L -- Habener, J F -- Mandel, G -- Goodman, R H -- AM 01313/AM/NIADDK NIH HHS/ -- AM 30457/AM/NIADDK NIH HHS/ -- AM 31400/AM/NIADDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Feb 28;231(4741):1002-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2868526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA, Recombinant/metabolism ; Genes ; Genetic Engineering ; Humans ; Immunoenzyme Techniques ; Luteinizing Hormone/metabolism ; Metallothionein/*genetics ; Mice ; Pituitary Gland, Anterior/*metabolism ; Rats ; Somatostatin/*genetics/metabolism
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  • 4
    Publication Date: 1986-02-21
    Description: Partial amino acid sequence analysis of a purified lymphocyte homing receptor demonstrates the presence of two amino termini, one of which corresponds precisely to the amino terminus of ubiquitin. This observation extends the province of this conserved polypeptide to the cell surface and leads to a proposed model of the receptor complex as a core polypeptide modified by glycosylation and ubiquitination. Independent antibodies to ubiquitin serve to identify additional cell surface species, an indication that ubiquitination of cell surface proteins may be more general. It is proposed that functional binding of lymphocytes to lymph node high endothelial venules might involve the ubiquitinated region of the receptor; if true, cell surface ubiquitin could play a more general role in cell-cell interaction and adhesion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siegelman, M -- Bond, M W -- Gallatin, W M -- St John, T -- Smith, H T -- Fried, V A -- Weissman, I L -- AI 19512/AI/NIAID NIH HHS/ -- CA 09151/CA/NCI NIH HHS/ -- GM 31461/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 21;231(4740):823-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003913" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cell Movement ; Endothelium/metabolism ; Glycoproteins/metabolism/*physiology ; Glycoside Hydrolases/metabolism ; High Mobility Group Proteins/*metabolism ; Lymphocytes/*physiology ; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase ; Membrane Proteins/metabolism/*physiology ; Mice ; Molecular Weight ; Protein Processing, Post-Translational ; Receptors, Cell Surface/metabolism/*physiology ; Ubiquitins/immunology/*metabolism
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  • 5
    Publication Date: 1986-05-23
    Description: Electrical stimulation of fibers in the stratum radiatum causes an excitatory postsynaptic potential in CA1 neurons of the hippocampus. Other excitatory inputs to or direct depolarization of these CA1 neurons during stimulation of the stratum radiatum caused a subsequent increase in the excitatory postsynaptic potential. This enhancement was characterized as a brief potentiation (2 to 3 minutes, similar to posttetanic potentiation) and a long-term potentiation (presumed to be involved in learning and memory). These potentiations are probably induced by an interaction of the postsynaptic cell or other presynaptic terminals with the test presynaptic terminals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sastry, B R -- Goh, J W -- Auyeung, A -- New York, N.Y. -- Science. 1986 May 23;232(4753):988-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3010459" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Mapping ; Calcium/physiology ; Conditioning (Psychology)/physiology ; Electric Stimulation ; Hippocampus/*physiology ; In Vitro Techniques ; Learning/physiology ; Membrane Potentials ; Rats ; Synapses/physiology ; Synaptic Transmission
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-18
    Description: The historical background of studies in Japan on chemical carcinogenesis from environmental sources is described from personal experience.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sugimura, T -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):312-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3088728" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Nitroquinoline-1-oxide/analysis ; Animals ; Biotransformation ; Carcinogens/*analysis ; Cyanobacteria/analysis ; Environmental Pollution/*analysis ; Food Additives ; Food Handling ; Furylfuramide/toxicity ; Health Policy ; Humans ; Indoles/metabolism ; Japan ; Lyngbya Toxins/toxicity ; Methods ; Methylnitronitrosoguanidine/toxicity ; Mutagenicity Tests ; Oncogenes ; Primary Prevention ; Rats ; Risk ; Stereoisomerism ; Stomach Neoplasms/chemically induced ; Streptomyces/analysis ; Structure-Activity Relationship ; Urinary Bladder Neoplasms/chemically induced
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-25
    Description: Electrophysiological recordings of inward currents from whole cells showed that vascular muscle cells have one type of sodium channel and two types of calcium channels. One of the calcium channels, the transient calcium channel, was activated by small depolarizations but then rapidly inactivated. It was equally permeable to calcium and barium and was blocked by cadmium, but not by tetrodotoxin. The other type, the sustained calcium channel, was activated by larger depolarizations, but inactivated very little; it was more permeable to barium than calcium. The sustained calcium channel was more sensitive to block by cadmium than the transient channel, but also was not blocked by tetrodotoxin. The sodium channel inactivated 15 times more rapidly than the transient calcium channel and at more negative voltages. This sodium channel, which is unusual because it is only blocked by a very high (60 microM) tetrodotoxin concentration but not by cadmium, is the first to be characterized in vascular muscle, and together with the two calcium channels, provides a basis for different patterns of excitation in vascular muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sturek, M -- Hermsmeyer, K -- HL 16328/HL/NHLBI NIH HHS/ -- HL 32295/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 25;233(4762):475-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2425434" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*physiology ; Ion Channels/*physiology ; Membrane Potentials ; *Muscle Contraction ; Muscle, Smooth, Vascular/*physiology ; Rats ; Rats, Inbred WKY ; Sodium/*physiology
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-01-31
    Description: Contrary to the orthodox view that optical image quality should "match" the photoreceptor grain, anatomical data from the eyes of various animals suggest that the image quality is significantly superior to the potential resolution of the cone mosaic in most retinal regions. A new theory is presented to explain the existence of this relation and to better appreciate eye design. It predicts that photoreceptors are potentially visible through the natural optics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Snyder, A W -- Bossomaier, T R -- Hughes, A -- New York, N.Y. -- Science. 1986 Jan 31;231(4737):499-501.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3941914" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; Humans ; Models, Neurological ; Photoreceptor Cells/*anatomy & histology ; Rats ; Snakes ; Species Specificity ; *Vision, Ocular ; *Visual Perception
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  • 9
    Publication Date: 1986-04-18
    Description: In situ hybridization of an oligonucleotide probe complementary to vasopressin messenger RNA (mRNA) in sections from normal or Brattleboro rat hypothalami revealed hybridization densities in each of three vasopressin-rich nuclei: the supraoptic, paraventricular, and suprachiasmatic. When entrained to a daily light-dark cycle, each rat strain displayed diurnal variation in hybridizable mRNA in the suprachiasmatic, but not in the supraoptic or paraventricular nuclei. The higher values for suprachiasmatic mRNA in the morning correlate well with previously elucidated morning increases in vasopressin immunoreactivity in the cerebrospinal fluid. These results support the utility of in situ hybridization techniques for elucidating physiological influences on regional peptidergic function, are consistent with a prominent role for vasopressinergic suprachiasmatic neurons in generating the cerebrospinal fluid vasopressin rhythm, and suggest that regulation of this mRNA rhythm is not dependent on release of intact peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Uhl, G R -- Reppert, S M -- New York, N.Y. -- Science. 1986 Apr 18;232(4748):390-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961487" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoradiography ; *Circadian Rhythm ; Nucleic Acid Hybridization ; Paraventricular Hypothalamic Nucleus/analysis/physiology ; RNA, Messenger/*analysis/isolation & purification ; Rats ; Rats, Brattleboro ; Rats, Inbred Strains ; Suprachiasmatic Nucleus/*analysis/physiology ; Supraoptic Nucleus/analysis/physiology ; Vasopressins/genetics/*physiology
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  • 10
    Publication Date: 1986-05-02
    Description: Two crystal structures of deamino-oxytocin have been determined at better than 1.1A resolution from isomorphous replacement and anomalous scattering x-ray measurements. In each of two crystal forms there are two closely related conformers with disulfide bridges of different chirality, which may be important in receptor recognition and activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wood, S P -- Tickle, I J -- Treharne, A M -- Pitts, J E -- Mascarenhas, Y -- Li, J Y -- Husain, J -- Cooper, S -- Blundell, T L -- Hruby, V J -- AM-10080/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 May 2;232(4750):633-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008332" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Dimethyl Sulfoxide ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Oxytocin/*analogs & derivatives/metabolism ; Protein Conformation ; Receptors, Angiotensin/*metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Oxytocin ; X-Ray Diffraction
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  • 11
    Publication Date: 1986-06-13
    Description: Administration of cholecystokinin (CCK) to rats caused a dose-dependent increase in plasma levels of the neurohypophyseal hormone oxytocin (OT). The OT secretion was comparable to that found in response to nausea-producing chemical agents that cause learned taste aversions. The effect of CCK on OT secretion was blunted after gastric vagotomy, as was the inhibition of food intake induced by CCK. Food ingestion also led to elevated plasma OT in rats, but CCK and aversive agents caused even greater OT stimulation. Thus, after administration of large doses of CCK, vagally mediated activation of central nausea pathways seems to be predominantly responsible for the subsequent decrease in food intake. Despite their dissimilar affective states, both nausea and satiety may activate a common hypothalamic oxytocinergic pathway that controls the inhibition of ingestion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verbalis, J G -- McCann, M J -- McHale, C M -- Stricker, E M -- AM-16166/AM/NIADDK NIH HHS/ -- MH-25140/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 13;232(4756):1417-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3715453" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning/physiology ; Cholecystokinin/*pharmacology ; Feeding Behavior/*physiology ; Nausea/*physiopathology ; Oxytocin/*secretion ; Paraventricular Hypothalamic Nucleus/physiology ; Rats ; Satiation/*physiology ; Vagotomy
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  • 12
    Publication Date: 1986-06-06
    Description: The Watanabe heritable hyperlipidemic (WHHL) rabbit, an animal with familial hypercholesterolemia, produces a mutant receptor for plasma low-density lipoprotein (LDL) that is not transported to the cell surface at a normal rate. Cloning and sequencing of complementary DNA's from normal and WHHL rabbits, shows that this defect arises from an in-frame deletion of 12 nucleotides that eliminates four amino acids from the cysteine-rich ligand binding domain of the LDL receptor. A similar mutation, detected by S1 nuclease mapping of LDL receptor messenger RNA, occurred in a patient with familial hypercholesterolemia whose receptor also fails to be transported to the cell surface. These findings suggest that animal cells may have fail-safe mechanisms that prevent the surface expression of improperly folded proteins with unpaired or improperly bonded cysteine residues.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451858/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451858/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamamoto, T -- Bishop, R W -- Brown, M S -- Goldstein, J L -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1230-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3010466" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport ; *Chromosome Deletion ; Cloning, Molecular ; Cysteine/genetics ; Dna ; DNA Restriction Enzymes ; Genes ; Humans ; Hyperlipoproteinemia Type II/*genetics ; Mutation ; RNA, Messenger ; Rabbits ; Receptors, LDL/*genetics
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  • 13
    Publication Date: 1986-05-09
    Description: Antigenic or mitogenic stimulation of T cells induces the secretion of an array of protein hormones that regulate immune responses. Molecular cloning has contributed strongly to our present understanding of the nature of this regulation. A complementary DNA (cDNA) library prepared from a cloned concanavalin A-activated mouse T-helper cell line was screened for abundant and induction-specific cDNA's. One such randomly chosen cDNA was found to encode mouse preproenkephalin messenger RNA (mRNA). Preproenkephalin mRNA represented about 0.4 percent of the mRNA in the activated cell line but was absent in resting cells of this line. Other induced T-helper cell lines have 0.1 to 0.5 percent of their mRNA as preproenkephalin mRNA. Induced T-helper cell culture supernatants have [Met]enkephalin-immunoreactive material. The production by activated T cells of a peptide neurotransmitter identifies a signal that can potentially permit T cells to modulate the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zurawski, G -- Benedik, M -- Kamb, B J -- Abrams, J S -- Zurawski, S M -- Lee, F D -- New York, N.Y. -- Science. 1986 May 9;232(4751):772-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2938259" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Enkephalins/*biosynthesis/genetics ; Humans ; *Lymphocyte Activation ; Mice ; Protein Precursors/*biosynthesis/genetics ; RNA, Messenger/*biosynthesis ; Rats ; T-Lymphocytes, Helper-Inducer/drug effects/metabolism/*physiology
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  • 14
    Publication Date: 1986-09-05
    Description: Expression of the ras oncogene is thought to be one of the contributing events in the initiation of certain types of human cancer. To determine the cellular activities that are directly triggered by ras proteins, the early consequences of microinjection of the human H-ras proteins into quiescent rat embryo fibroblasts were investigated. Within 30 minutes to 1 hour after injection, cells show a marked increase in surface ruffles and fluid-phase pinocytosis. The rapid enhancement of membrane ruffling and pinocytosis is induced by both the proto-oncogenic and the oncogenic forms of the H-ras protein. The effects produced by the oncogenic protein persist for more than 15 hours after injection, whereas the effects of the proto-oncogenic protein are short-lived, being restricted to a 3-hour interval after injection. The stimulatory effect of the ras oncogene protein on ruffling and pinocytosis is dependent on the amount of injected protein and is accompanied by an apparent stimulation of phospholipase A2 activity. These rapid changes in cell membrane activities induced by ras proteins may represent primary events in the mechanism of action of ras proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bar-Sagi, D -- Feramisco, J R -- CA07896/CA/NCI NIH HHS/ -- CA39811/CA/NCI NIH HHS/ -- GM28277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1061-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3090687" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle/drug effects ; Cell Membrane/*drug effects/ultrastructure ; Cells, Cultured ; Culture Media ; DNA/biosynthesis ; GTP-Binding Proteins/*pharmacology ; Humans ; Microinjections ; Oncogene Proteins, Viral/*pharmacology ; Phospholipases A/metabolism ; Phospholipases A2 ; Phospholipids/metabolism ; Pinocytosis/*drug effects ; Rats ; Time Factors
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, D M -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):155-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*anatomy & histology/growth & development ; Chickens ; Genes ; Humans ; Language Development ; Male ; Neurons/physiology ; Rats ; Synapses/physiology ; Visual Cortex/anatomy & histology/physiology
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  • 16
    Publication Date: 1986-08-08
    Description: The production and action of immunoregulatory cytokines, including interleukin-1 (IL-1), are inhibited by glucocorticoid hormones in vivo and in vitro. Conversely, glucocorticoid blood levels were increased by factors released by human leukocytes exposed to Newcastle disease virus preparations. This activity was neutralized by an antibody to IL-1. Therefore the capacity of IL-1 to stimulate the pituitary-adrenal axis was tested. Administration of subpyrogenic doses of homogeneous human monocyte-derived IL-1 or the pI 7 form of human recombinant IL-1 to mice and rats increased blood levels of adrenocorticotropic hormone (ACTH) and glucocorticoids. Another monokine, tumor necrosis factor, and the lymphokines IL-2 and gamma-interferon had no such effects when administered in doses equivalent to or higher than those of IL-1. The stimulatory effect of IL-1 on the pituitary-adrenal axis seemed not to be mediated by the secondary release of products from mature T lymphocytes since IL-1 was endocrinologically active when injected into athymic nude mice. These results strongly support the existence of an immunoregulatory feedback circuit in which IL-1 acts as an afferent and glucocorticoid as an efferent hormonal signal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Besedovsky, H -- del Rey, A -- Sorkin, E -- Dinarello, C A -- AI15614/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 8;233(4764):652-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014662" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/blood/physiology ; Animals ; Corticosterone/blood/physiology ; Female ; Glucocorticoids/blood/immunology/*physiology ; Humans ; Interleukin-1/immunology/pharmacology/*physiology ; Leukocytes/drug effects/physiology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Nude ; Newcastle disease virus/immunology ; Rats ; Rats, Inbred Strains
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  • 17
    Publication Date: 1986-06-27
    Description: Age-associated increases in collagen cross-linking and accumulation of advanced glycosylation products are both accelerated by diabetes, suggesting that glucose-derived cross-link formation may contribute to the development of chronic diabetic complications as well as certain physical changes of aging. Aminoguanidine, a nucleophilic hydrazine compound, prevented both the formation of fluorescent advanced nonenzymatic glycosylation products and the formation of glucose-derived collagen cross-links in vitro. Aminoguanidine administration to rats was equally effective in preventing diabetes-induced formation of fluorescent advanced nonenzymatic glycosylation products and cross-linking of arterial wall connective tissue protein in vivo. The identification of aminoguanidine as an inhibitor of advanced nonenzymatic glycosylation product formation now makes possible precise experimental definition of the pathogenetic significance of this process and suggests a potential clinical role for aminoguanidine in the future treatment of chronic diabetic complications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brownlee, M -- Vlassara, H -- Kooney, A -- Ulrich, P -- Cerami, A -- AM 19655/AM/NIADDK NIH HHS/ -- R01-AM 33861/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 27;232(4758):1629-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3487117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arteries/*drug effects/metabolism ; Collagen/metabolism ; Connective Tissue/drug effects/metabolism ; Diabetes Mellitus, Experimental/*drug therapy/metabolism ; Glucose/metabolism ; Guanidines/*pharmacology/therapeutic use ; Male ; Rats ; Rats, Inbred Lew ; Serum Albumin, Bovine/metabolism
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  • 18
    Publication Date: 1986-01-17
    Description: T lymphocytes recognize foreign antigen together with allele-specific determinants on membrane-bound class I and class II (Ia) gene products of the major histocompatibility complex. To identify amino acids of class II molecules critical to this recognition process, the genes encoding the beta chains of the I-Ak molecule were cloned from a wild-type B-cell hybridoma and from an immunoselected variant subline showing distinct serological and T-cell stimulatory properties. Nucleotide sequencing and DNA-mediated gene transfer established that a single base transition (G----A) encoding a change from glutamic acid to lysine at position 67 in the I-Ak beta molecule accounted for all the observed phenotypic changes of the variant cells. These results confirm the importance of residues 62 to 78 in the amino terminal domain of I-A beta for class II-restricted T-cell recognition of antigen and demonstrate the ability of a single substitution in this region to alter this recognition event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, M A -- Glimcher, L A -- Nielsen, E A -- Paul, W E -- Germain, R N -- New York, N.Y. -- Science. 1986 Jan 17;231(4735):255-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3484558" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/immunology ; Base Sequence ; Cloning, Molecular ; Histocompatibility Antigens Class II/*immunology ; Humans ; Hybridomas/immunology ; Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C ; T-Lymphocytes/*immunology
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  • 19
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-12
    Description: The SNF1 gene plays a central role in carbon catabolite repression in the yeast Saccharomyces cerevisiae, namely that SNF1 function is required for expression of glucose-repressible genes. The nucleotide sequence of the cloned SNF1 gene was determined, and the predicted amino acid sequence shows that SNF1 encodes a 72,040-dalton polypeptide that has significant homology to the conserved catalytic domain of mammalian protein kinases. Specific antisera were prepared and used to identify the SNF1 protein. The protein was shown to transfer phosphate from adenosine triphosphate to serine and threonine residues in an in vitro autophosphorylation reaction. These findings indicate that SNF1 encodes a protein kinase and suggest that protein phosphorylation plays a critical role in regulation by carbon catabolite repression in eukaryotic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celenza, J L -- Carlson, M -- GM34095/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 12;233(4769):1175-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526554" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Enzyme Repression ; Genes ; Glucose/*metabolism ; Phosphorylation ; Protein Kinases/biosynthesis/*genetics ; Saccharomyces cerevisiae/enzymology/*genetics
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  • 20
    Publication Date: 1986-04-25
    Description: Nerve growth factor (NGF) and its receptor are important in the development of cells derived from the neural crest. Mouse L cell transformants have been generated that stably express the human NGF receptor gene transfer with total human DNA. Affinity cross-linking, metabolic labeling and immunoprecipitation, and equilibrium binding with 125I-labeled NGF revealed that this NGF receptor had the same size and binding characteristics as the receptor from human melanoma cells and rat PC12 cells. The sequences encoding the NGF receptor were molecularly cloned using the human Alu repetitive sequence as a probe. A cosmid clone that contained the human NGF receptor gene allowed efficient transfection and expression of the receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chao, M V -- Bothwell, M A -- Ross, A H -- Koprowski, H -- Lanahan, A A -- Buck, C R -- Sehgal, A -- NS-17551/NS/NINDS NIH HHS/ -- NS-23343-01/NS/NINDS NIH HHS/ -- NS21072/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Apr 25;232(4749):518-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008331" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Transformation, Neoplastic/drug effects ; *Cloning, Molecular ; DNA, Recombinant ; Genes ; Humans ; Melanoma/metabolism ; Mice ; Oncogenes ; Rats ; Receptors, Cell Surface/*genetics ; Receptors, Nerve Growth Factor ; Repetitive Sequences, Nucleic Acid ; Tunicamycin/pharmacology
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  • 21
    Publication Date: 1986-07-25
    Description: Rat thyroid cells in culture, rendered quiescent by hormone deprivation, can be stimulated to undergo DNA synthesis in the absence of serum by the addition of purified thyrotropin. The primary effect in response to thyrotropin action in thyroid cells is the induction of the c-fos oncogene, followed by c-myc expression. This suggests that thyrotropin acts as a competence growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colletta, G -- Cirafici, A M -- Vecchio, G -- New York, N.Y. -- Science. 1986 Jul 25;233(4762):458-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cell Division/drug effects ; Cells, Cultured ; Cycloheximide/pharmacology ; DNA/biosynthesis ; Oncogenes/*drug effects ; Rats ; Thyroid Gland/*cytology/drug effects/metabolism ; Thyrotropin/*pharmacology
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  • 22
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Easton, T A -- New York, N.Y. -- Science. 1986 Mar 14;231(4743):1235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945820" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Homosexuality ; Humans ; Male ; *Perfume ; Rats ; *Sexual Behavior
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  • 23
    Publication Date: 1986-05-02
    Description: Cardiocytes in the atria contain a prohormone that gives rise to atrial natriuretic peptides (ANP's), which have intrinsic hemodynamic regulatory activity. The distribution of ANP's in the brain suggests the involvement of these peptides in central cardiovascular regulation. In conscious rats with chronic indwelling catheters, volume loading with isotonic saline or glucose increased the amount of circulating immunoreactive ANP's by a factor of 4 to 5, as determined by radioimmunoassay. Hyperosmotic challenge with a hypertonic NaCl solution or anesthesia with halothane caused similar increases in plasma ANP's. Results obtained with the denervated-heart preparation indicate that neuronal influences are important in the release of ANP's induced by volume loading. As judged from reversed-phase high-performance liquid chromatography of extracted plasma and radioimmunoassay of collected fractions, the circulating physiologically important ANP's in the conscious rodent appear to be alpha-rANP(5-28) (atriopeptin III) and either alpha-rANP(3-28) [ANF(8-33)] or alpha-rANP(1-28) (ANF).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eskay, R -- Zukowska-Grojec, Z -- Haass, M -- Dave, J R -- Zamir, N -- New York, N.Y. -- Science. 1986 May 2;232(4750):636-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2938258" target="_blank"〉PubMed〈/a〉
    Keywords: Anesthesia ; Animals ; Atrial Natriuretic Factor/blood/isolation & purification/physiology/*secretion ; Blood Volume ; Chromatography, High Pressure Liquid ; Consciousness/physiology ; Halothane/pharmacology ; Heart/innervation ; Heart Atria/drug effects/secretion ; Male ; Osmotic Pressure ; Pentobarbital/pharmacology ; Peptide Fragments/isolation & purification ; Radioimmunoassay ; Rats ; Rats, Inbred Strains
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  • 24
    Publication Date: 1986-05-23
    Description: The generally mild bleeding disorder of von Willebrand disease is associated with abnormalities of two distinct plasma proteins, the large multimeric von Willebrand factor (vWF), which mediates platelet adhesion, and von Willebrand antigen II (vW AgII), which is of unknown function. The two proteins were found to have a common biosynthetic origin in endothelial cells and megakaryocytes, which explains their simultaneous absence in the severe form of this hereditary disease. Shared amino acid sequences from a 100-kilodalton plasma glycoprotein and from vW AgII are identical to amino acid sequences predicted from a complementary DNA clone encoding the 5' end of vWF. In addition, these proteins have identical molecular weights and immunologic cross reactivities. Monoclonal antibodies prepared against both proteins recognize epitopes on the pro-vWF subunit and on a 100-kilodalton protein that are not present on the mature vWF subunit in endothelial cell lysates. In contrast, polyclonal antibodies against vWF recognize both pro-vWF and vWF subunits. Thus, the 100-kilodalton plasma glycoprotein and vW AgII are identical proteins and represent an extremely large propolypeptide that is first cleaved from pro-vWF during intracellular processing and then released into plasma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fay, P J -- Kawai, Y -- Wagner, D D -- Ginsburg, D -- Bonthron, D -- Ohlsson-Wilhelm, B M -- Chavin, S I -- Abraham, G N -- Handin, R I -- Orkin, S H -- HL-30616/HL/NHLBI NIH HHS/ -- HL-34050/HL/NHLBI NIH HHS/ -- HL-34787/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 May 23;232(4753):995-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3486471" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens/immunology/*metabolism ; Blood Proteins/immunology/metabolism ; Endothelium/metabolism ; Humans ; Molecular Weight ; Peptide Fragments/analysis ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; von Willebrand Factor/*metabolism
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  • 25
    Publication Date: 1986-11-07
    Description: Intracellular electrical recordings in an in vitro slice preparation of the brainstem medial pontine reticular formation, a region thought to be important in mediation of desynchronized sleep phenomena, demonstrate a population of neurons that have a calcium-dependent, low threshold spike. This low threshold spike was inactivated at relatively depolarized membrane potential levels and, when this spike was deinactivated, it induced a burst of action potentials. The membrane potential dependence of the spike may underlie changes in action potential firing patterns associated with behavioral state change because the baseline membrane potential in neurons of the medial pontine reticular population depolarizes during passage from waking and slow wave sleep to desynchronized sleep, which is characterized by the absence of burst firing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greene, R W -- Haas, H L -- McCarley, R W -- MH 39,683/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):738-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775364" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/physiology ; Electric Stimulation ; In Vitro Techniques ; Membrane Potentials ; Pons/cytology/*physiology ; Rats
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  • 26
    Publication Date: 1986-01-24
    Description: Steady-state cellular levels of phosphatidylinositol-4,5-bisphosphate (PIP2), 1,2-diacylglycerol (DAG), and inositol phosphates have been measured in two different fibroblast cell lines (NIH 3T3 and NRK cells) before and after transformation with three different ras genes. At high cell density the ratio of DAG to PIP2 was 2.5- to 3-fold higher in the ras-transformed cells than in their untransformed counterparts. The sum of the water-soluble breakdown products of the polyphosphoinositides, inositol-1,4-bisphosphate and inositol-1,4,5-trisphosphate, was also elevated in ras-transformed NRK cells compared with nontransformed NRK cells. These findings suggest that the ras (p21) protein may act by affecting these levels, possibly as a regulatory element in the PIP2 breakdown pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fleischman, L F -- Chahwala, S B -- Cantley, L -- GM 36133/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 24;231(4736):407-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3001936" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Transformation, Neoplastic/*analysis ; Diglycerides/analysis ; Humans ; Inositol 1,4,5-Trisphosphate ; Inositol Phosphates/analysis ; *Oncogenes ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/*analysis ; Rats
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  • 27
    Publication Date: 1986-09-05
    Description: Damage to the vessel wall is a signal for endothelial migration and replication and for platelet release at the site of injury. Addition of transforming growth factor-beta (TGF-beta) purified from platelets to growing aortic endothelial cells inhibited [3H]thymidine incorporation in a concentration-dependent manner. A transient inhibition of DNA synthesis was also observed in response to wounding; cell migration and replication are inhibited during the first 24 hours after wounding. By 48 hours after wounding both TGF-beta-treated and -untreated cultures showed similar responses. Flow microfluorimetric analysis of cell cycle distribution indicated that after 24 hours of exposure to TGF-beta the cells were blocked from entering S phase, and the fraction of cells in G1 was increased. The inhibition of the initiation of regeneration by TGF-beta could allow time for recruitment of smooth muscle cells into the site of injury by other platelet components.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heimark, R L -- Twardzik, D R -- Schwartz, S M -- HL-18645/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1078-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3461562" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Platelets/*physiology ; Cell Cycle/drug effects ; Cell Movement/drug effects ; Cells, Cultured ; Endothelium/cytology/*physiology ; Flow Cytometry ; *Growth Inhibitors ; Humans ; In Vitro Techniques ; Peptides/*pharmacology ; Rats ; Regeneration ; Transforming Growth Factors
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  • 28
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-12-19
    Description: Thyroid hormones stimulate the rate of cell division by poorly understood mechanisms. The possibility that thyroid hormones increase cell growth by stimulating secretion of a growth factor was investigated. Thyroid hormones are nearly an absolute requirement for the division of GH4C1 rat pituitary tumor cells plated at low density. Conditioned media from cells grown with or without L-triiodothyronine (T3) were treated with an ion exchange resin to remove T3 and were tested for ability to stimulate the division of GH4C1 cells. Conditioned medium from T3-treated cells was as active as thyroid hormone at promoting GH4C1 cell growth but did not elicit other thyroid hormone responses, induction of growth hormone, and down-regulation of thyrotropin-releasing hormone receptors, as effectively as T3 did. A substance or substances associated with T3-induced growth stimulatory activity migrated at high molecular weight at neutral pH and was different from known growth-promoting hormones induced by T3. The results demonstrate that thyroid hormones stimulate the division of GH4C1 pituitary cells by stimulating the secretion of an autocrine growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinkle, P M -- Kinsella, P A -- AM 32847/AM/NIADDK NIH HHS/ -- AM/NS 00827/AM/NIADDK NIH HHS/ -- CA 11198/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1549-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3097825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cell Line ; Epidermal Growth Factor/metabolism ; Growth Hormone/metabolism ; Growth Substances/*secretion ; Nerve Growth Factors/metabolism ; Pituitary Neoplasms/*metabolism/pathology ; Rats ; Thyrotropin-Releasing Hormone/metabolism ; Triiodothyronine/*pharmacology
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  • 29
    Publication Date: 1986-02-14
    Description: The yeast GAL4 protein (881 amino acids) binds to specific DNA sites upstream of target genes and activates transcription. Derivatives of this protein bearing as few as 74 amino terminal residues bind to these sites but fail to activate transcription. When appropriately positioned in front of a gene these derivatives act as repressors. These and related findings support the idea that GAL4 activates transcription by touching other DNA-bound proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keegan, L -- Gill, G -- Ptashne, M -- GM07598/GM/NIGMS NIH HHS/ -- GM32308/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 14;231(4739):699-704.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3080805" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Fungal/genetics/metabolism ; DNA, Recombinant ; DNA-Binding Proteins/*genetics/metabolism ; Fungal Proteins/genetics ; Galactose ; Gene Expression Regulation ; Repressor Proteins/genetics ; Saccharomyces cerevisiae/*genetics ; Transcription Factors/*genetics/metabolism ; *Transcription, Genetic ; beta-Galactosidase/genetics
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  • 30
    Publication Date: 1986-03-21
    Description: Structural data are now available for comparing a penicillin target enzyme, the D-alanyl-D-alanine-peptidase from Streptomyces R61, with a penicillin-hydrolyzing enzyme, the beta-lactamase from Bacillus licheniformis 749/C. Although the two enzymes have distinct catalytic properties and lack relatedness in their overall amino acid sequences except near the active-site serine, the significant similarity found by x-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that beta-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, J A -- Dideberg, O -- Charlier, P -- Wery, J P -- Libert, M -- Moews, P C -- Knox, J R -- Duez, C -- Fraipont, C -- Joris, B -- 10RRO1955-01/RR/NCRR NIH HHS/ -- AI-10925/AI/NIAID NIH HHS/ -- AI-16702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 21;231(4744):1429-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3082007" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillus cereus/enzymology ; Binding Sites ; Carboxypeptidases/genetics/*metabolism ; Molecular Weight ; *Penicillin Resistance ; Protein Conformation ; *Serine-Type D-Ala-D-Ala Carboxypeptidase ; Streptomyces/enzymology ; X-Ray Diffraction ; beta-Lactamases/genetics/*metabolism
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  • 31
    Publication Date: 1986-05-30
    Description: Glutamate decarboxylase (GAD; E.C. 4.1.1.15) converts glutamate to gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the vertebrate central nervous system. This report describes the isolation of a GAD complementary DNA clone by immunological screening of a lambda gt-11 brain complementary DNA expression library. The fusion protein produced by this clone catalyzes the conversion of glutamate to GABA and carbon dioxide, confirming its identity as GAD. Antibodies to beta-galactosidase remove GAD enzymatic activity from solution, showing that this activity is associated with the fusion protein. In immunoblotting experiments all three available antisera to GAD reacted with the fusion polypeptide and with two major polypeptides (molecular size, 60,000 and 66,000 daltons) in brain extracts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaufman, D L -- McGinnis, J F -- Krieger, N R -- Tobin, A J -- HD05615/HD/NICHD NIH HHS/ -- NS20356/NS/NINDS NIH HHS/ -- NS22256/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 May 30;232(4754):1138-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3518061" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*enzymology ; Cloning, Molecular ; DNA/genetics ; Escherichia coli/metabolism ; Glutamate Decarboxylase/biosynthesis/genetics/*metabolism ; Humans ; Mice ; Rats ; Recombinant Proteins/biosynthesis/metabolism ; gamma-Aminobutyric Acid/*biosynthesis
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  • 32
    Publication Date: 1986-01-10
    Description: To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic lambda gt11 library was screened with an antiserum directed against a synthetic peptide representing a portion of the rat TRH prohormone. The nucleotide sequence of the immunopositive complementary DNA encoded a protein with a molecular weight of 29,247. This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. In addition, potential cleavage sites in the TRH precursor could produce other non-TRH peptides, which may be secreted. In situ hybridization to rat brain sections demonstrated that the pre-proTRH complementary DNA detected neurons concentrated in the parvocellular division of the paraventricular nucleus, the same location as cells detected by immunohistochemistry. These findings indicate that mammalian TRH arises by posttranslational processing of a larger precursor protein. The ability of the TRH prohormone to generate multiple copies of the bioactive peptide may be an important mechanism in the amplification of hormone production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lechan, R M -- Wu, P -- Jackson, I M -- Wolf, H -- Cooperman, S -- Mandel, G -- Goodman, R H -- AM 34540/AM/NIADDK NIH HHS/ -- CA 37370/CA/NCI NIH HHS/ -- P30 AM 39428/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):159-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*physiology ; DNA/genetics ; Hypothalamus/physiology ; Molecular Weight ; Protein Precursors/genetics/*physiology ; Pyrrolidonecarboxylic Acid/analogs & derivatives ; Rats ; Rats, Inbred Strains ; Thyrotropin-Releasing Hormone/genetics/*physiology
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-04-25
    Description: The acoustic startle response in rats shows both short-term habituation, which recovers in seconds or minutes, and long-term habituation, which is effectively permanent. Lesions of the cerebellar vermis significantly attenuated long-term habituation without affecting the short-term process or altering initial response levels. In this response system the cerebellar vermis is part of an essential circuit for long-term habituation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leaton, R N -- Supple, W F Jr -- New York, N.Y. -- Science. 1986 Apr 25;232(4749):513-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961494" target="_blank"〉PubMed〈/a〉
    Keywords: Acoustic Stimulation ; Animals ; Auditory Pathways/anatomy & histology/physiology ; Cerebellum/anatomy & histology/*physiology ; Habituation, Psychophysiologic/*physiology ; Male ; Rats ; Reflex, Startle/*physiology ; Reticular Formation/analysis/physiology
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  • 34
    Publication Date: 1986-02-07
    Description: In mammals different isoforms of myosin heavy chain are encoded by the members of a multigene family. The expression of each gene of this family is regulated in a tissue- and developmental stage-specific manner as well as by hormonal and various pathological stimuli. In this study the molecular basis of isoform switches induced in myosin heavy chain by thyroid hormone was investigated. The expression of the myosin heavy chain gene family was analyzed in seven different muscles of adult rats subjected to hypo- or hyperthyroidism with complementary DNA probes specific for six different myosin heavy chain genes. The results demonstrate that all six genes are responsive to thyroid hormone. More interestingly, the same myosin heavy chain gene can be regulated by thyroid hormone in highly different modes, even in opposite directions, depending on the tissue in which it is expressed. Furthermore, the skeletal embryonic and neonatal myosin heavy chain genes, so far considered specific to these two developmental stages, can be reinduced by hypothyroidism in specific adult muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Izumo, S -- Nadal-Ginard, B -- Mahdavi, V -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):597-600.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945800" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Diaphragm/drug effects/growth & development/metabolism ; Genes/*drug effects ; Heart/drug effects/growth & development ; Hyperthyroidism/metabolism ; Hypothyroidism/metabolism ; Male ; Muscle Development ; Muscles/drug effects/metabolism ; Myocardium/metabolism ; Myosins/*genetics ; Rats ; Thyroid Hormones/*pharmacology
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  • 35
    Publication Date: 1986-01-10
    Description: In rat hippocampal pyramidal cells tested in situ by iontophoresis of several neurotransmitters, ethanol significantly enhanced excitatory responses to acetylcholine and inhibitory responses to somatostatin-14 but had no statistically significant effect on excitatory responses to glutamate or inhibitory responses to gamma-aminobutyric acid or, in preliminary tests, to norepinephrine or serotonin. The effects of ethanol on responses to acetylcholine and somatostatin-14 may provide insight into synaptic mechanisms underlying the behavioral consequences of ethanol intoxication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mancillas, J R -- Siggins, G R -- Bloom, F E -- AA-06420/AA/NIAAA NIH HHS/ -- AM-26741/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):161-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2867600" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/*pharmacology ; Action Potentials/drug effects ; Animals ; Ethanol/*pharmacology ; Goldfish ; Hippocampus/*drug effects ; Male ; Neurons/drug effects/physiology ; Norepinephrine/pharmacology ; Rats ; Rats, Inbred Strains ; Serotonin/pharmacology ; Somatostatin/*pharmacology ; Synaptic Membranes/drug effects ; gamma-Aminobutyric Acid/pharmacology
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  • 36
    Publication Date: 1986-08-15
    Description: Phosphoglycerate kinase (PGK) is a monomeric protein composed of two domains of approximately equal size, connected by a hinge. Substrate-induced conformational change results in the closure of the active site cleft, which is situated between these two domains. In a study of the relations between structure and function of this enzyme, two interspecies hybrids were constructed, each composed of one domain from the human enzyme and one domain from the yeast enzyme. Despite a 35% difference in the amino acid composition between human and yeast PGK, catalytic properties of the hybrid enzymes are very similar to those of the parental proteins. This result demonstrates that the evolutionary substitutions within these two distantly related molecules do not significantly affect formation of the active site cleft, mechanism of domain closure, or enzyme activity itself.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mas, M T -- Chen, C Y -- Hitzeman, R A -- Riggs, A D -- R01 GM31263/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):788-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526552" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; *Chimera ; *Genes ; *Genes, Fungal ; Genetic Engineering ; Humans ; Kinetics ; Models, Molecular ; Phosphoglycerate Kinase/*genetics/metabolism ; Plasmids ; Protein Conformation ; Protein Multimerization ; Saccharomyces cerevisiae/enzymology/*genetics
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-19
    Description: Prenatal exposure to alcohol produces many developmental defects of the central nervous system, such as microcephaly, mental retardation, motor dysfunction, and cognitive deficiencies. Therefore, the generation of neurons in the cerebral cortex was examined in the offspring of female rats fed a diet containing ethanol. Prenatal exposure to ethanol delayed and extended the period during which cortical neurons were generated, reduced the number of neurons in the nature cortex with the same time of origin, and altered the distribution of neurons generated on a particular day. Thus, the proliferation and migration of cortical neurons are profoundly affected by in utero exposure to ethanol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, M W -- AA 06916/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 19;233(4770):1308-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3749878" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cerebral Cortex/*drug effects/embryology ; Ethanol/*pharmacology ; Female ; Gestational Age ; Humans ; Motor Cortex/drug effects/embryology ; Neurons/*drug effects/embryology ; Pregnancy ; Rats
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  • 38
    Publication Date: 1986-07-11
    Description: The mechanism by which sex steroids rapidly modulate the excitability of neurons was investigated by intracellular recording of neurons in rat medial amygdala brain slices. Brief hyperpolarization and increased potassium conductance were produced by 17 beta-estradiol. This effect persisted after elimination of synaptic input and after suppression of protein synthesis. Thus, 17 beta-estradiol directly changes the ionic conductance of the postsynaptic membrane of medial amygdala neurons. In addition, a greater proportion of the neurons from females than from males responded to 17 beta-estradiol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nabekura, J -- Oomura, Y -- Minami, T -- Mizuno, Y -- Fukuda, A -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):226-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726531" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/cytology/*drug effects ; Animals ; Cycloheximide/pharmacology ; Dactinomycin/pharmacology ; Estradiol/*pharmacology ; Female ; Male ; Membrane Potentials/drug effects ; Neurons/drug effects/physiology ; Rats ; Rats, Inbred Strains
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  • 39
    Publication Date: 1986-10-03
    Description: A sulfated, myotropic neuropeptide termed leucosulfakinin (Glu-Gln-Phe-Glu-Asp-Tyr(SO3H)-Gly-His-Met-Arg-Phe-NH2) was isolated from head extracts of the cockroach Leucophaea maderae. The peptide exhibits sequence homology with the hormonally active portion of the vertebrate hormones human gastrin II and cholecystokinin, suggesting that these peptides are evolutionarily related. Six of the 11 amino acid residues (55 percent) are identical to those in gastrin II. In addition, the intestinal myotropic action of leucosulfakinin is analogous to that of gastrin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nachman, R J -- Holman, G M -- Haddon, W F -- Ling, N -- New York, N.Y. -- Science. 1986 Oct 3;234(4772):71-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3749893" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aplysia ; Brachyura ; Cholecystokinin/genetics ; Cockroaches ; Gastrins/genetics ; Humans ; Insect Hormones/genetics/*isolation & purification/physiology ; Muscle Contraction/drug effects ; Nerve Tissue Proteins/genetics/*isolation & purification/physiology ; *Neuropeptides ; Sequence Homology, Nucleic Acid
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-05-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelson, T -- Lucignani, G -- Sokoloff, L -- New York, N.Y. -- Science. 1986 May 9;232(4751):776-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008340" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; Brain Chemistry ; Deoxy Sugars/*metabolism ; Deoxyglucose/*metabolism ; Glucose-6-Phosphatase/metabolism ; *Glucose-6-Phosphate/*analogs & derivatives ; Glucosephosphates/analysis ; *Magnetic Resonance Spectroscopy ; Rats
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  • 41
    Publication Date: 1986-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, S M -- Schwartz, R D -- Creveling, C R -- Hollingsworth, E B -- Daly, J W -- Skolnick, P -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):228-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014649" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Brain/*metabolism ; Cell Membrane/metabolism/*physiology ; Chick Embryo ; Chlorides/*metabolism ; Guinea Pigs ; Mice ; Rats ; Receptors, GABA-A/metabolism/*physiology ; Synaptosomes/metabolism
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  • 42
    Publication Date: 1986-03-28
    Description: Simian acquired immune deficiency syndrome (SAIDS) in the macaque genus of monkeys at the California Primate Research Center is apparently caused by infection by a type D retrovirus. The complete nucleotide sequence (8173 base pairs) of a molecular clone of the prototype SAIDS virus isolate, SRV-1, reveals a typical retrovirus structure with long terminal repeats (346 base pairs) and open reading frames for the gag (663 codons), pol (867 codons), and env (605 codons) genes. SRV-1 also has a separate open reading frame of 314 codons between the gag and pol genes that defines the viral protease gene (prt) and a short open reading frame of unknown significance downstream from the env gene. The SRV-1 protease region shows a high degree of homology to its counterpart in the hamster intracisternal A-type particle genome; both these protease genes are about twice as long as the analogous region of other retroviruses. SRV-1 has no notable similarity in either genetic organization or sequence to the human AIDS retroviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Power, M D -- Marx, P A -- Bryant, M L -- Gardner, M B -- Barr, P J -- Luciw, P A -- AI20573/AI/NIAID NIH HHS/ -- CA37467/CA/NCI NIH HHS/ -- RR00169/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1567-72.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3006247" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology/*veterinary ; Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA Restriction Enzymes/metabolism ; Genes, Viral ; Macaca/*microbiology ; Peptide Hydrolases/genetics ; Retroviridae/*genetics ; Retroviridae Proteins/genetics ; Sequence Homology, Nucleic Acid
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1037-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3738524" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Collagen/genetics ; *Genetic Code ; Humans ; *Protein Conformation ; Protein Denaturation ; Protein Processing, Post-Translational ; Structure-Activity Relationship ; X-Ray Diffraction
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  • 44
    Publication Date: 1986-04-11
    Description: Human color vision is based on three light-sensitive pigments. The isolation and sequencing of genomic and complementary DNA clones that encode the apoproteins of these three pigments are described. The deduced amino acid sequences show 41 +/- 1 percent identity with rhodopsin. The red and green pigments show 96 percent mutual identity but only 43 percent identity with the blue pigment. Green pigment genes vary in number among color-normal individuals and, together with a single red pigment gene, are proposed to reside in a head-to-tail tandem array within the X chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nathans, J -- Thomas, D -- Hogness, D S -- New York, N.Y. -- Science. 1986 Apr 11;232(4747):193-202.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2937147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; Cattle ; Cebidae ; Cercopithecidae ; Color ; Color Perception/*physiology ; DNA/metabolism ; Drosophila melanogaster ; Eye Proteins/genetics/physiology ; *Genes ; Humans ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Photoreceptor Cells/physiology ; RNA, Messenger/genetics ; Retinal Pigments/*genetics ; Retinaldehyde/physiology ; Rhodopsin/genetics ; Rod Opsins ; X Chromosome
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  • 45
    Publication Date: 1986-03-14
    Description: Human malignant melanoma cells express specific chondroitin sulfate proteoglycans (mel-CSPG) on the surface, both in vivo and in vitro. Melanocytes in normal skin show no detectable mel-CSPG but can be induced to express the antigen when cultured in the presence of cholera toxin and the tumor promoter 12-O-tetradecanoylphorbol-13-acetate. Most other cell types do not express mel-CSPG either in vivo or in vitro. A study was designed to examine regulatory signals controlling mel-CSPG expression. The gene encoding mel-CSPG was mapped to human chromosome 15, and this chromosome was introduced into rodent cells derived from distinct differentiation lineages. Three types of mel-CSPG--expressing hybrids were found: (i) hybrids derived from human melanomas; (ii) hybrids derived from human cells that do not express mel-CSPG; and (iii) hybrids derived from human cells expressing mel-CSPG that are antigen-negative but that are induced to express mel-CSPG when cultured on extracellular matrix instead of plastic surfaces. Thus, mel-CSPG expression can be controlled both through intrinsic signals, provided by the differentiation program of the rodent fusion partner, and through extrinsic signals, provided by specific cell-matrix interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rettig, W J -- Real, F X -- Spengler, B A -- Biedler, J L -- Old, L J -- CA-08748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 14;231(4743):1281-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3633135" target="_blank"〉PubMed〈/a〉
    Keywords: Aggrecans ; Animals ; Antibodies, Monoclonal ; Cell Line ; Cholera Toxin/pharmacology ; Chromosome Mapping ; Chromosomes, Human, 13-15 ; Cricetinae ; Cricetulus ; *Extracellular Matrix Proteins ; Gene Expression Regulation/drug effects ; Glycoproteins/*biosynthesis/genetics ; Humans ; Hybrid Cells/drug effects/*metabolism ; Lectins, C-Type ; Lymphocytes/metabolism ; Melanocytes/drug effects/metabolism ; Melanoma/*metabolism ; Mice ; Neoplasm Proteins/*biosynthesis/genetics ; Neuroblastoma/metabolism ; *Proteoglycans ; Rats ; Tetradecanoylphorbol Acetate/pharmacology
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  • 46
    Publication Date: 1986-06-13
    Description: Tissue welding is a potentially important biomedical application of laser technology. The structural alterations basic to this phenomenon were studied in experimental repair of lesions of the rat carotid artery and sciatic nerve. A modified neodymiumdoped yttrium-aluminum-garnet laser operating at a wavelength of 1.319 micrometers was used in conjunction with conventional suture techniques. Histological and fine-structural analysis revealed a homogenizing change in collagen with interdigitation of altered individual fibrils that appeared to be the structural basis of the welding effect.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schober, R -- Ulrich, F -- Sander, T -- Durselen, H -- Hessel, S -- New York, N.Y. -- Science. 1986 Jun 13;232(4756):1421-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3715454" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carotid Arteries/*radiation effects ; *Collagen ; Dose-Response Relationship, Radiation ; Extracellular Matrix/radiation effects ; *Lasers ; Rats ; Sciatic Nerve/*radiation effects
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  • 47
    Publication Date: 1986-02-07
    Description: In the adult castrated male rat, exposure to inescapable, intermittent electroshocks inhibited the pulsatile pattern of luteinizing hormone release and markedly lowered its plasma concentrations. The central administration of the corticotropin-releasing factor (CRF) antagonist alpha-helical ovine CRF residues 9 to 41 reversed the inhibitory action of stress. Neither its peripheral injection, nor the intraventricular injection of the inactive CRF analog des-Glu to Arg ovine CRF was effective. These results suggest that endogenous CRF may mediate some deleterious effects of noxious stimuli on reproduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rivier, C -- Rivier, J -- Vale, W -- AA03504/AA/NIAAA NIH HHS/ -- AM26741/AM/NIADDK NIH HHS/ -- HD13527/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):607-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003907" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/physiology ; Animals ; Corticotropin-Releasing Hormone/pharmacology/*physiology ; Electroshock ; Female ; Humans ; Luteinizing Hormone/blood ; Male ; Orchiectomy ; Rats ; *Reproduction/drug effects ; Stress, Psychological/*physiopathology
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  • 48
    Publication Date: 1986-02-21
    Description: A 4-week assay for screening tumor promoters of bladder cancer has been developed in which increased agglutinability of isolated rat bladder cells with concanavalin A is used as an indicator. On the basis of this assay system, L-isoleucine and L-leucine were suspected of being possible tumor promoters. Results of 40- to 60-week carcinogenesis experiments in which N-butyl-N-(4-hydroxybutyl)nitrosamine was used as an initiator demonstrate that L-isoleucine and L-leucine promote bladder cancer in rats. This finding may be relevant to the high incidence of human bladder cancer in Western countries, where the diet is rich in protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishio, Y -- Kakizoe, T -- Ohtani, M -- Sato, S -- Sugimura, T -- Fukushima, S -- New York, N.Y. -- Science. 1986 Feb 21;231(4740):843-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945812" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carcinogens ; Carcinoma/*chemically induced ; *Isoleucine ; *Leucine ; Papilloma/*chemically induced ; Precancerous Conditions/*chemically induced ; Rats ; Rats, Inbred F344 ; Urinary Bladder Neoplasms/*chemically induced
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-18
    Description: Protein kinase C, an enzyme that is activated by the receptor-mediated hydrolysis of inositol phospholipids, relays information in the form of a variety of extracellular signals across the membrane to regulate many Ca2+-dependent processes. At an early phase of cellular responses, the enzyme appears to have a dual effect, providing positive forward as well as negative feedback controls over various steps of its own and other signaling pathways, such as the receptors that are coupled to inositol phospholipid hydrolysis and those of some growth factors. In biological systems, a positive signal is frequently followed by immediate negative feedback regulation. Such a novel role of this protein kinase system seems to give a logical basis for clarifying the biochemical mechanism of signal transduction, and to add a new dimension essential to our understanding of cell-to-cell communication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishizuka, Y -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):305-12.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014651" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Animals ; Blood Platelets/metabolism ; Calcimycin/pharmacology ; Calcium-Transporting ATPases/metabolism ; Carrier Proteins/metabolism ; *Cation Transport Proteins ; Cell Membrane/physiology ; Cyclic AMP/metabolism ; Diglycerides/metabolism ; Electric Conductivity ; Enzyme Activation ; Fluorescent Antibody Technique ; Isoenzymes/metabolism ; Models, Biological ; Phosphatidylinositols/*metabolism ; Potassium/metabolism ; Protein Kinase C/*metabolism ; Purkinje Cells/enzymology ; Rats ; Serotonin/blood ; Sodium/metabolism ; Sodium-Hydrogen Antiporter ; Tetradecanoylphorbol Acetate/pharmacology ; Time Factors
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  • 50
    Publication Date: 1986-09-05
    Description: The oral administration of peptide drugs is well known to be precluded by their digestion in the stomach and small intestine. As a new approach to oral delivery, peptide drugs were coated with polymers cross-linked with azoaromatic groups to form an impervious film to protect orally administered drugs from digestion in the stomach and small intestine. When the azopolymer-coated drug reached the large intestine, the indigenous microflora reduced the azo bonds, broke the cross-links, and degraded the polymer film, thereby releasing the drug into the lumen of the colon for local action or for absorption. The ability of the azopolymer coating to protect and deliver orally administered peptide drugs was demonstrated in rats with the peptide hormones vasopressin and insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saffran, M -- Kumar, G S -- Savariar, C -- Burnham, J C -- Williams, F -- Neckers, D C -- AI 18710/AI/NIAID NIH HHS/ -- SO-7-RR05700-15/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1081-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526553" target="_blank"〉PubMed〈/a〉
    Keywords: Administration, Oral ; Animals ; Azo Compounds ; Blood Glucose/metabolism ; Diabetes Mellitus, Experimental/drug therapy ; Enterobacteriaceae/metabolism ; Insulin/*administration & dosage ; Lypressin/administration & dosage ; Peptides/*administration & dosage ; Polymers ; Rats ; *Tablets, Enteric-Coated
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  • 51
    Publication Date: 1986-08-01
    Description: Transforming growth factor-beta (TGF-beta) is a multifunctional peptide that controls proliferation, differentiation, and other functions in many cell types. Many cells synthesize TGF-beta and essentially all of them have specific receptors for this peptide. TGF-beta regulates the actions of many other peptide growth factors and determines a positive or negative direction of their effects. Its marked ability to enhance formation of connective tissue in vivo suggests several therapeutic applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sporn, M B -- Roberts, A B -- Wakefield, L M -- Assoian, R K -- New York, N.Y. -- Science. 1986 Aug 1;233(4763):532-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3487831" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/drug effects ; Epidermal Growth Factor/metabolism ; Genes ; Humans ; Peptides/genetics/metabolism/pharmacology/*physiology ; Platelet-Derived Growth Factor/pharmacology ; Rats ; Transforming Growth Factors
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-05-16
    Description: The adrenergic control of glucose homeostasis is mediated in part through variations in the release of pancreatic hormones. In this study, purified pancreatic A and B cells were used to identify the recognition and messenger units involved in the adrenergic regulation of glucagon and insulin release. Catecholamines induced beta-adrenergic receptor activity in A cells and alpha 2-adrenergic receptor activity in B cells. The two recognition units provoked opposite variations in the production of cellular cyclic adenosine monophosphate, the beta-adrenergic unit enhancing the nucleotide's permissive effect on amino acid-induced glucagon release and the alpha 2-adrenergic unit inhibiting that upon glucose-induced insulin release. In both cell types, catecholamines interact powerfully with the synergistic control of hormone release by nutrient- and (neuro)hormone-driven messenger systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schuit, F C -- Pipeleers, D G -- New York, N.Y. -- Science. 1986 May 16;232(4752):875-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2871625" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Agonists/pharmacology ; Adrenergic beta-Antagonists/pharmacology ; Animals ; Cyclic AMP/analysis ; Epinephrine/pharmacology ; Glucagon/secretion ; Insulin/secretion ; Islets of Langerhans/analysis/drug effects/*physiology ; Male ; Rats ; Rats, Inbred Strains ; Receptors, Adrenergic, beta/drug effects/*physiology
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  • 53
    Publication Date: 1986-03-28
    Description: Adhesive interactions of the platelet surface with plasma proteins such as fibrinogen and fibronectin play an important role in thrombosis and hemostasis. The binding of both of these proteins to platelets is inhibited by synthetic peptides containing the sequence Arg-Gly-Asp, which corresponds to the cell adhesion site in fibronectin and is also present in the alpha chain of fibrinogen. An affinity matrix made of an insolubilized heptapeptide containing the Arg-Gly-Asp sequence selectively binds the platelet membrane glycoprotein IIb/IIIa from detergent extracts of platelets. When incorporated into liposome membranes, the isolated protein confers to the liposomes the ability to bind to surfaces coated with fibrinogen, fibronectin, and vitronectin but not to surfaces coated with thrombospondin or albumin. This platelet receptor is related to the previously identified fibronectin and vitronectin receptors in that it recognizes an Arg-Gly-Asp sequence but differs from the other receptors in its wider specificity toward various adhesive proteins. These results establish the existence of a family of adhesion receptors that recognize the sequence Arg-Gly-Asp.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pytela, R -- Pierschbacher, M D -- Ginsberg, M H -- Plow, E F -- Ruoslahti, E -- CA38352/CA/NCI NIH HHS/ -- HL26838/HL/NHLBI NIH HHS/ -- HL28235/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1559-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2420006" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blood Platelets/*physiology ; *Cell Adhesion ; Fibrinogen/metabolism ; Fibronectins/metabolism ; Glycoproteins/*metabolism ; Humans ; Membrane Proteins/*metabolism ; Oligopeptides/*metabolism ; Platelet Membrane Glycoproteins ; Receptors, Cell Surface/*metabolism ; Structure-Activity Relationship ; Thrombospondins ; Vitronectin
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  • 54
    Publication Date: 1986-12-05
    Description: Ethanol, at pharmacologically relevant concentrations of 20 to 100 mM, stimulates gamma-aminobutyric (GABA) receptor-mediated uptake of 36Cl-labeled chlorine into isolated brain vesicles. One drug that acts at GABA-benzodiazepine receptors, the imidazobenzodiazepine Ro15-4513, has been found to be a potent antagonist of ethanol-stimulated 36Cl- uptake into brain vesicles, but it fails to antagonize either pentobarbital- or muscimol-stimulated 36Cl- uptake. Pretreatment of rats with Ro15-4513 blocks the anticonflict activity of low doses of ethanol (but not pentobarbital) as well as the behavioral intoxication observed with higher doses of ethanol. The effects of Ro15-4513 in antagonizing ethanol-stimulated 36Cl- uptake and behavior are completely blocked by benzodiazepine receptor antagonists. However, other benzodiazepine receptor inverse agonists fail to antagonize the actions of ethanol in vitro or in vivo, suggesting a novel interaction of Ro15-4513 with the GABA receptor-coupled chloride ion channel complex. The identification of a selective benzodiazepine antagonist of ethanol-stimulated 36Cl- uptake in vitro that blocks the anxiolytic and intoxicating actions of ethanol suggests that many of the neuropharmacologic actions of ethanol may be mediated via central GABA receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suzdak, P D -- Glowa, J R -- Crawley, J N -- Schwartz, R D -- Skolnick, P -- Paul, S M -- New York, N.Y. -- Science. 1986 Dec 5;234(4781):1243-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3022383" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anxiety/drug effects ; Azides/*pharmacology ; Benzodiazepines/*pharmacology ; Chlorides/metabolism ; Ethanol/*antagonists & inhibitors ; Flumazenil/pharmacology ; Male ; Pyrazoles/pharmacology ; Rats ; Rats, Inbred Strains ; Receptors, GABA-A/drug effects ; Synaptosomes/drug effects
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  • 55
    Publication Date: 1986-06-27
    Description: The posttranslational maturation of a complex precursor polyprotein, human proenkephalin, was assessed by infection of a wide spectrum of cell types with a recombinant vaccinia virus that expressed human proenkephalin. The infected cells rapidly produced both cellular and secreted Met-enkephalin immunoreactivity. Although each cell line could secrete intact proenkephalin, only a mouse pituitary line was capable of processing proenkephalin to mature enkephalin peptides. The quantity of intact proenkephalin secreted from BSC-40 cells (derived from African Green monkey kidney) was sufficient to establish the value of vaccinia virus as a mammalian cell expression vector.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, G -- Herbert, E -- Hruby, D E -- 7 RO1 DA04154-01/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 27;232(4758):1641-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3754979" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cercopithecus aethiops ; Enkephalin, Methionine/biosynthesis ; Enkephalins/*biosynthesis/genetics ; Genetic Vectors ; Humans ; Mice ; Protein Precursors/*biosynthesis/genetics ; Rats ; Recombinant Proteins/*biosynthesis ; Vaccinia virus/*genetics
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  • 56
    Publication Date: 1986-10-24
    Description: Cachectin (tumor necrosis factor), a protein produced in large quantities by endotoxin-activated macrophages, has been implicated as an important mediator of the lethal effect of endotoxin. Recombinant human cachectin was infused into rats in an effort to determine whether cachectin, by itself, can elicit the derangements of host physiology caused by administration of endotoxin. When administered in quantities similar to those produced endogenously in response to endotoxin, cachectin causes hypotension, metabolic acidosis, hemoconcentration, and death within minutes to hours, as a result of respiratory arrest. Hyperglycemia and hyperkalemia were also observed after infusion. At necropsy, diffuse pulmonary inflammation and hemorrhage were apparent on gross and histopathologic examination, along with ischemic and hemorrhagic lesions of the gastrointestinal tract, and acute renal tubular necrosis. Thus, it appears that a single protein mediator (cachectin) is capable of inducing many of the deleterious effects of endotoxin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tracey, K J -- Beutler, B -- Lowry, S F -- Merryweather, J -- Wolpe, S -- Milsark, I W -- Hariri, R J -- Fahey, T J 3rd -- Zentella, A -- Albert, J D -- New York, N.Y. -- Science. 1986 Oct 24;234(4775):470-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3764421" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Glucose/metabolism ; Endotoxins/toxicity ; Female ; Glycoproteins/*toxicity ; Humans ; Potassium/blood ; Rats ; Recombinant Proteins ; Shock/*chemically induced/pathology/physiopathology ; Sodium/blood ; Tumor Necrosis Factor-alpha
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, M -- New York, N.Y. -- Science. 1986 Sep 12;233(4769):1143-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3738527" target="_blank"〉PubMed〈/a〉
    Keywords: Acetamides/*adverse effects ; Animals ; *Government Agencies ; Herbicides/*adverse effects ; Humans ; Neoplasms/chemically induced ; Rats ; United States ; *United States Environmental Protection Agency
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-06-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wehrenberg, W B -- Ehlers, C L -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1271-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3085220" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arousal/drug effects ; Brain/*drug effects ; Electroencephalography ; Growth Hormone/blood ; Growth Hormone-Releasing Hormone/administration & dosage/*pharmacology ; Injections, Intraventricular ; Motor Activity/drug effects ; Rats
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  • 59
    Publication Date: 1986-10-31
    Description: T lymphocytes express on their surface not only a specific receptor for antigen and major histocompatibility complex proteins, but also a number of additional glycoproteins that are thought to play accessory roles in the processes of recognition and signal transduction. L3T4 is one such T-cell surface protein that is expressed on most mouse thymocytes and on mature mouse T cells that recognize class II (Ia) major histocompatibility complex proteins. Such cells are predominantly of the helper/inducer phenotype. In this study, complementary DNA clones encoding L3T4 were isolated and sequenced. The predicted protein sequence shows that L3T4 is a member of the immunoglobulin gene superfamily. It is encoded by a single gene that does not require rearrangement prior to expression. Although the protein has not previously been demonstrated on nonhematopoietic cells, two messenger RNA species specific for L3T4 are found in brain. The minor species comigrates with the L3T4 transcript in T cells, whereas the major species is 1 kilobase smaller.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tourvieille, B -- Gorman, S D -- Field, E H -- Hunkapiller, T -- Parnes, J R -- 1 F32 CA07877-01/CA/NCI NIH HHS/ -- AI11313/AI/NIAID NIH HHS/ -- GM34991/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):610-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3094146" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Differentiation, T-Lymphocyte ; Antigens, Surface/genetics/*isolation & purification ; Base Sequence ; Brain/*metabolism ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Humans ; Mice ; Mice, Inbred C57BL ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Sequence Homology, Nucleic Acid ; T-Lymphocytes/*immunology/metabolism
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  • 60
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-04-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merrifield, B -- New York, N.Y. -- Science. 1986 Apr 18;232(4748):341-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961484" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; In Vitro Techniques ; Methods ; Nucleotides/*chemical synthesis ; Peptide Fragments/metabolism ; Peptides/*chemical synthesis ; Ribonuclease, Pancreatic/chemical synthesis/metabolism ; Structure-Activity Relationship
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  • 61
    Publication Date: 1986-07-18
    Description: A human complementary DNA whose protein product is considered to be the major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, and Gerstmann-Straussler syndrome has been identified and characterized. The extensive homology of this gene sequence to the hamster PrP 27- to 30-kilodalton prion protein complementary DNA clone, and its existence as a single copy in the human genome, leads to the conclusion that this is the human prion gene. This human prion gene has been mapped to human chromosome 20, negating a direct link between the prion protein and Down's syndrome or the amyloid of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liao, Y C -- Lebo, R V -- Clawson, G A -- Smuckler, E A -- CA 21141/CA/NCI NIH HHS/ -- CA 40145/CA/NCI NIH HHS/ -- KO4 CA 01003/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):364-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014653" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, 19-20 ; Chromosomes, Human, 21-22 and Y ; *Cloning, Molecular ; Creutzfeldt-Jakob Syndrome/genetics/microbiology ; Cricetinae ; DNA/*analysis ; DNA Restriction Enzymes/metabolism ; Humans ; Prions/*genetics ; Viral Proteins/analysis
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  • 62
    Publication Date: 1986-05-30
    Description: The three-dimensional crystal structure of the adenovirus major coat protein is presented. Adenovirus type 2 hexon, at 967 residues, is now the longest polypeptide whose structure has been determined crystallographically. Taken with our model for hexon packing, which positions the 240 trimeric hexons in the capsid, the structure defines 60% of the protein within the 150 X 10(6) dalton virion. The assembly provides the first details of a DNA-containing animal virus that is 20 times larger than the spherical RNA viruses previously described. Unexpectedly, the hexon subunit contains two similar beta-barrels whose topology is identical to those of the spherical RNA viruses, but whose architectural role in adenovirus is very different. The hexon structure reveals several distinctive features related to its function as a stable protective coat, and shows that the type-specific immunological determinants are restricted to the virion surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, M M -- White, J L -- Grutter, M G -- Burnett, R M -- AI 17270/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 May 30;232(4754):1148-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3704642" target="_blank"〉PubMed〈/a〉
    Keywords: *Adenoviridae/genetics/ultrastructure ; Amino Acid Sequence ; *Capsid/genetics/ultrastructure ; *Capsid Proteins ; Protein Conformation ; RNA Viruses/ultrastructure ; X-Ray Diffraction
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  • 63
    Publication Date: 1986-01-24
    Description: Parathyroid hormone-like factors have been found in extracts of tumors associated with humoral hypercalcemia of malignancy, many of which are of squamous epithelial origin. Cultured, nonmalignant human keratinocytes were examined for the production of similar factors. Keratinocyte-conditioned medium from ten cultures stimulated the production of cyclic adenosine monophosphate in clonally derived rat osteosarcoma cells sensitive to parathyroid hormone. Bovine [Nle8,18, Tyr34]PTH-(3-34)NH2, a competitive inhibitor of parathyroid hormone, stopped the adenylate cyclase production stimulated by keratinocyte-conditioned medium, but antisera to parathyroid hormone had no effect on such adenylate cyclase activity. The active component of keratinocyte-conditioned medium has a molecular weight exceeding that of native parathyroid hormone. These characteristics are shared by the parathyroid hormone receptor agonists associated with humoral hypercalcemia of malignancy, which suggests that normal human keratinocytes may produce a factor related to that produced by malignant tumors associated with humoral hypercalcemia of malignancy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merendino, J J Jr -- Insogna, K L -- Milstone, L M -- Broadus, A E -- Stewart, A F -- AM 30102/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 24;231(4736):388-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2417317" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Animals ; Cattle ; Cells, Cultured ; Cyclic AMP/metabolism ; Epidermis/*cytology/metabolism/physiology ; Humans ; Isoproterenol/pharmacology ; Keratins/*metabolism ; Mice ; Osteosarcoma/metabolism ; Parathyroid Hormone/pharmacology/*physiology ; Peptide Fragments/pharmacology ; Rats ; Teriparatide
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  • 64
    Publication Date: 1986-02-21
    Description: The lymphocyte cell surface receptor for the high endothelial venules (HEV's) of peripheral lymph nodes is specifically recognized by the monoclonal antibody MEL-14. Three independent complementary DNA (cDNA) clones, each of which encodes the protein ubiquitin, were detected by virtue of the expression of the MEL-14 antigenic determinant on cDNA-beta-galactosidase bacterial fusion proteins. The antigenic determinant defined by MEL-14 resides in the carboxyl terminal 13-amino-acid proteolytic peptide of ubiquitin, but is undetected in intact undenatured ubiquitin and other cellular ubiquitinated proteins. Antisera and monoclonal antibodies to ubiquitin determinants bind to the surface of both HEV-receptor positive and negative cell lines. The MEL-14-identified cDNA clones hydridize to RNA transcripts that encode tandemly repeated ubiquitins. Sequence analysis of these polyubiquitin cDNA's does not identify a leader sequence for export to the cell surface. The expression of the MEL-14 epitope of ubiquitin depends upon its local environment. The steady-state levels of expression of the ubiquitin messenger RNA's do not correlate with either the tissue derivation of the RNA or the expression of the lymphocyte HEV receptor. Regulation of the expression of the HEV receptor is not likely to reflect the transcriptional control of ubiquitin genes, but rather to reflect control of the expression of the HEV core polypeptide or its level or form of ubiquitination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St John, T -- Gallatin, W M -- Siegelman, M -- Smith, H T -- Fried, V A -- Weissman, I L -- AI19512/AI/NIAID NIH HHS/ -- CA 09151/CA/NCI NIH HHS/ -- GM 31461/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 21;231(4740):845-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003914" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*immunology ; Antibody Specificity ; Base Sequence ; Cloning, Molecular ; Endothelium/metabolism ; Gene Expression Regulation ; High Mobility Group Proteins/*genetics ; Lymphatic System/metabolism ; Lymphocytes/*physiology ; Mice ; Receptors, Cell Surface/*genetics/immunology/metabolism ; Ubiquitins/*genetics/immunology/metabolism
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  • 65
    Publication Date: 1986-10-31
    Description: The mechanism by which Trypanosoma cruzi, the protozoan parasite that causes Chagas' disease, becomes attached to mammalian cells is not well understood. Fibronectin is thought to participate in the attachment, and in this study the region of fibronectin that interacts with the surface receptors of T. cruzi trypomastigotes was investigated by testing the binding of the amino acid sequence Arg-Gly-Asp-Ser, corresponding to the cell attachment site of fibronectin to T. cruzi trypomastigotes. Peptides with the sequence Arg-Gly-Asp-Ser, but not Arg-Phe-Asp-Ser, Arg-Phe-Asp-Ser-Ala-Ala-Arg-Phe-Asp, Ser-Lys-Pro, Glu-Ser-Gly, or Ala-Lys-Thr-Lys-Pro, bound to the parasite surface and inhibited cell invasion by the pathogen. Monoclonal antibodies to the cell attachment domain of fibronectin also inhibited cell infection by the parasite. The immunization of BALB/c mice with tetanus toxoid-conjugated peptide induced a significant protection against T. cruzi. The data support the notion that the sequence Arg-Gly-Asp-Ser of cell surface fibronectin acts as a recognition site for attachment of the parasites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ouaissi, M A -- Cornette, J -- Afchain, D -- Capron, A -- Gras-Masse, H -- Tartar, A -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):603-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3094145" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Chagas Disease/parasitology/*prevention & control ; Fibronectins/immunology/*physiology ; Mice ; Mice, Inbred BALB C ; Peptides/*therapeutic use ; Trypanocidal Agents/*therapeutic use ; Trypanosoma cruzi/drug effects
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  • 66
    Publication Date: 1986-02-07
    Description: Rat optic and sciatic nerves were crushed, and 10 minutes to 3 days later nerve segments between the crushed site and the cell body were removed and assayed for posttranslational protein modification by amino acid addition. Protein modification was comparable in intact optic and sciatic nerves, but in sciatic nerves increased to 1.6 times control levels 10 minutes after crushing and reached a maximum of ten times control levels by 2 hours. In optic nerves activity was decreased throughout the time course studied. The results indicate that, in a nerve which is capable of regeneration (sciatic), protein modification by the addition of amino acids increases immediately after injury, but a nerve incapable of regeneration (optic) is incapable of activating the modification reaction. These findings may be important in understanding the reasons for the lack of a regenerative response after injury to central mammalian nerves.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shyne-Athwal, S -- Riccio, R V -- Chakraborty, G -- Ingoglia, N A -- NS19148/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):603-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3080804" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*metabolism ; Animals ; Arginine/metabolism ; Decapodiformes ; Goldfish ; Leucine/metabolism ; Lysine/metabolism ; Nerve Regeneration ; Nerve Tissue Proteins/*metabolism ; Optic Nerve/*metabolism/physiology ; Optic Nerve Injuries ; Rats ; Sciatic Nerve/injuries/*metabolism/physiology ; Time Factors
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  • 67
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-08-08
    Description: Single amino acid changes were introduced into normal (non-oncogenic) and activated forms of the human H-ras protein at a position (residue 116) proposed on structural grounds to represent a contact site with guanine nucleotides. Substitutions at this site could significantly reduce the ability of both forms to bind and hydrolyze guanosine 5'-triphosphate; these substitutions, however, did not necessarily diminish the transforming capacity of activated derivatives. One substitution that severely impairs these functions activated the transforming potential of the otherwise normal polypeptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walter, M -- Clark, S G -- Levinson, A D -- New York, N.Y. -- Science. 1986 Aug 8;233(4764):649-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3487832" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Transformation, Neoplastic/metabolism ; DNA/genetics ; Guanosine Triphosphate/metabolism ; Humans ; Neoplasm Proteins/*genetics/metabolism ; Oncogene Protein p21(ras) ; *Oncogenes
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-18
    Description: Excitability is generated in developing skeletal muscle by the incorporation of sodium-selective ion channels into the surface membrane. Whole-cell and patch voltage-clamp recording from myotubes and their embryologic precursors, myoblasts, indicated that voltage-activated sodium current in myoblasts was more resistant to block by tetrodotoxin (TTX) than that in myotubes. Single-channel recording from both cell types showed two classes of sodium channels. One class had a lower single-channel conductance, activated at more hyperpolarized voltages, and was more resistant to TTX than the other. The proportion of TTX-resistant to TTX-sensitive sodium channels was higher in myoblasts than in myotubes. Thus, the difference in TTX sensitivity between myoblasts and myotubes can be explained by a difference in the proportion of the two classes of sodium channels. In addition, the lower conductance of TTX-resistant channels provides insight into the relationship between the TTX binding site and the external mouth of the sodium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiss, R E -- Horn, R -- NS 00703/NS/NINDS NIH HHS/ -- NS 18608/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):361-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2425432" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dose-Response Relationship, Drug ; Drug Resistance ; Electric Conductivity ; Electric Stimulation ; Ion Channels/drug effects/*physiology ; *Muscle Development ; Muscles/metabolism ; Rats ; Sodium/*metabolism ; Tetrodotoxin/pharmacology
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  • 69
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-08-29
    Description: Cardiac gap junctions consist of arrays of integral membrane proteins joined across the intercellular cleft at points of cell-to-cell contact. These junctional proteins are thought to form pores through which ions can diffuse from cytosol to cytosol. By monitoring whole-cell currents in pairs of embryonic heart cells with two independent patch-clamp circuits, the properties of single gap junction channels have been investigated. These channels had a conductance of about 165 picosiemens and underwent spontaneous openings and closings that were independent of voltage. Channel activity and macroscopic junctional conductance were both decreased by the uncoupling agent 1-octanol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veenstra, R D -- DeHaan, R L -- HL-06909/HL/NHLBI NIH HHS/ -- HL-27385/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 29;233(4767):972-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2426781" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chick Embryo ; Electric Conductivity ; Guinea Pigs ; Heart/embryology ; Intercellular Junctions/*physiology ; Ion Channels/*cytology ; Myocardium/*cytology ; Rats
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-06-06
    Description: The current pertussis vaccines, although efficacious, in some instances produce undesirable side effects. Molecular engineering of pertussis toxin, the major protective antigen, could provide a safer, new generation of vaccines against whooping cough. As a first critical step in the development of such a vaccine, the complete nucleotide sequence of the pertussis toxin gene was determined and the amino acid sequences of the individual subunits were deduced. All five subunits are coded by closely linked cistrons. A promoter-like structure was found in the 5'-flanking region, suggesting that the toxin is expressed through a polycistronic messenger RNA. The order of the cistrons is S1, S2, S4, S5, and S3. All subunits contain signal peptides of variable length. The calculated molecular weights of the mature subunits are 26,024 for S1, 21,924 for S2, 21,873 for S3, 12,058 for S4, and 11,013 for S5. Subunits S2 and S3 share 70% amino acid homology and 75% nucleotide homology. Subunit S1 contains two regions of eight amino acids homologous to analogous regions in the A subunit of both cholera and Escherichia coli heat labile toxins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Locht, C -- Keith, J M -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1258-64.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3704651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Genes ; Molecular Weight ; *Pertussis Toxin ; Virulence Factors, Bordetella/*genetics
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  • 71
    Publication Date: 1986-04-18
    Description: Suppressor cells specific for acetylcholine receptor (AChR) were induced in a population of lymphocytes previously sensitized to AChR, obtained from rats with experimental autoimmune myasthenia gravis (EAMG). The lymphocytes were cultured with the immunosuppressive drug cyclosporin A plus purified AChR for 7 days. These cells, when mixed with lymphocytes from rats with EAMG in vitro, strongly suppressed the antibody response to AChR. They did not inhibit antibody responses to an unrelated antigen, an indication that suppression was specific for AChR. This approach should be a useful way to induce specific suppressor cells from sensitized populations of lymphocytes and may be applicable in the treatment of autoimmune diseases such as myasthenia gravis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McIntosh, K R -- Drachman, D B -- 5RO1 HD04817-16/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 18;232(4748):401-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2938256" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cyclosporins/pharmacology ; Female ; Lymph Nodes/cytology ; Lymphocytes/drug effects ; Myasthenia Gravis/*immunology ; Rats ; Rats, Inbred Lew ; Receptors, Cholinergic/*immunology ; Spleen/cytology ; T-Lymphocytes, Regulatory/*immunology
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  • 72
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-05-16
    Description: The activities of both chymotrypsin and amylase in individual zymogen granules of rat pancreas were measured by means of micromanipulation and microfluorometric methods. The enzyme content and the ratio of amylase to chymotrypsin varied widely among granules taken from the same animal. These results are compatible with short-term nonparallel bulk secretion of the two enzymes through exocytosis. The distribution of each enzyme activity in a population of granules suggests quantal packaging of amylase and chymotrypsinogen into the granules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mroz, E A -- Lechene, C -- AM26488/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 May 16;232(4752):871-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2422756" target="_blank"〉PubMed〈/a〉
    Keywords: Amylases/*analysis ; Animals ; Chymotrypsin/*analysis ; Cytoplasmic Granules/*analysis ; Exocytosis ; Female ; Pancreas/*secretion ; Rats ; Rats, Inbred Strains
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  • 73
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-10-10
    Description: The secretion of follicle-stimulating hormone (FSH) by the anterior pituitary gland is regulated by the interaction of hypothalamic and gonadal hormones. Recently, proteins termed inhibins that selectively suppress FSH secretion have been purified and characterized from the gonadal fluids of several species. Antibodies to a synthetic peptide encompassing the amino terminal 25 residues of the recently characterized porcine inhibin were used to develop a specific radioimmunoassay (RIA) for inhibin and to neutralize endogenous inhibin during the estrous cycle of the rat. The administration of 20 international units of pregnant mare serum gonadotropin (PMSG) stimulated the secretion of inhibin in intact immature female rats, whereas ovariectomy caused an abrupt decrease in plasma inhibin concentrations that were not prevented by the injection of PMSG. The infusion of a polyclonal antiserum to inhibin, from 12 noon on proestrus to 1 a.m. on the morning of estrus, as well as its acute intravenous injection during diestrus I or II, caused an increase in plasma FSH (but not luteinizing hormone) concentrations. These results support the hypothesis of a feedback loop between the release of ovarian inhibin and FSH in the female rat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rivier, C -- Rivier, J -- Vale, W -- HD13527/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 10;234(4773):205-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3092356" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Estrus ; Female ; Follicle Stimulating Hormone/blood/*secretion ; Gonadotropins, Equine/pharmacology ; Immune Sera ; Inhibins/blood/immunology/*secretion ; Luteinizing Hormone/blood ; Ovariectomy ; Proestrus ; Rats ; Rats, Inbred Strains
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  • 74
    Publication Date: 1986-05-23
    Description: Two metabolites of the steroid hormones progesterone and deoxycorticosterone, 3 alpha-hydroxy-5 alpha-dihydroprogesterone and 3 alpha, 5 alpha-tetrahydrodeoxycorticosterone, are potent barbiturate-like ligands of the gamma-aminobutyric acid (GABA) receptor-chloride ion channel complex. At concentrations between 10(-7) and 10(-5)M both steroids inhibited binding of the convulsant t-butylbicyclophosphorothionate to the GABA-receptor complex and increased the binding of the benzodiazepine flunitrazepam; they also stimulated chloride uptake (as measured by uptake of 36Cl-) into isolated brain vesicles, and potentiated the inhibitory actions of GABA in cultured rat hippocampal and spinal cord neurons. These data may explain the ability of certain steroid hormones to rapidly alter neuronal excitability and may provide a mechanism for the anesthetic and hypnotic actions of naturally occurring and synthetic anesthetic steroids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Majewska, M D -- Harrison, N L -- Schwartz, R D -- Barker, J L -- Paul, S M -- New York, N.Y. -- Science. 1986 May 23;232(4753):1004-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2422758" target="_blank"〉PubMed〈/a〉
    Keywords: 20-alpha-Dihydroprogesterone/*analogs & derivatives/metabolism/pharmacology ; Animals ; Bicyclo Compounds/metabolism ; *Bicyclo Compounds, Heterocyclic ; Binding, Competitive ; Brain/metabolism ; Cells, Cultured ; Chlorides/metabolism ; Desoxycorticosterone/*analogs & derivatives/metabolism/pharmacology ; Drug Synergism ; Flunitrazepam/metabolism ; Hippocampus/metabolism ; In Vitro Techniques ; Ion Channels/metabolism ; Progesterone/*analogs & derivatives/metabolism/pharmacology ; Rats ; Receptors, GABA-A/*drug effects/metabolism ; Spinal Cord/metabolism
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  • 75
    Publication Date: 1986-08-15
    Description: Growth cones are specialized structures that form the distal tips of growing axons. During both normal development of the nervous system and regeneration of injured nerves, growth cones are essential for elongation and guidance of growing axons. Developmental and regenerative axon growth is frequently accompanied by elevated synthesis of a protein designated GAP-43. GAP-43 has now been found to be a major component of growth-cone membranes in developing rat brains. Relative to total protein, GAP-43 is approximately 12 times as abundant in growth-cone membranes as in synaptic membranes from adult brains. Immunohistochemical localization of GAP-43 in frozen sections of developing brain indicates that the protein is specifically associated with neuropil areas containing growth cones and immature synaptic terminals. The results support the proposal that GAP-43 plays a role in axon growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skene, J H -- Jacobson, R D -- Snipes, G J -- McGuire, C B -- Norden, J J -- Freeman, J A -- EY01117/EY/NEI NIH HHS/ -- EY03718/EY/NEI NIH HHS/ -- NS18103/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):783-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3738509" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Animals, Newborn ; Anura ; Axons/physiology ; Brain/growth & development/*physiology ; Cell Membrane/metabolism ; Fetus ; GAP-43 Protein ; Growth Substances/*biosynthesis/isolation & purification ; Membrane Proteins/*biosynthesis/isolation & purification ; *Nerve Regeneration ; Nerve Tissue Proteins/*biosynthesis/isolation & purification ; Optic Nerve/cytology/*physiology ; Rats ; Synaptic Membranes/metabolism
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  • 76
    Publication Date: 1986-08-22
    Description: Protein kinase C, the major phorbol ester receptor, was purified from bovine brain and through the use of oligonucleotide probes based on partial amino acid sequence, complementary DNA clones were derived from bovine brain complementary DNA libraries. Thus, the complete amino acid sequence of bovine protein kinase C was determined, revealing a domain structure. At the amino terminal is a cysteine-rich domain with an internal duplication; a putative calcium-binding domain follows, and there is at the carboxyl terminal a domain that shows substantial homology, but not identity, to sequences of other protein kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parker, P J -- Coussens, L -- Totty, N -- Rhee, L -- Young, S -- Chen, E -- Stabel, S -- Waterfield, M D -- Ullrich, A -- New York, N.Y. -- Science. 1986 Aug 22;233(4766):853-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3755547" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/metabolism ; *Caenorhabditis elegans Proteins ; Carrier Proteins ; Cattle ; Dna ; Models, Chemical ; Protein Biosynthesis ; *Protein Kinase C/isolation & purification ; RNA, Messenger/metabolism ; *Receptors, Drug ; *Receptors, Immunologic
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  • 77
    Publication Date: 1986-08-01
    Description: Whether growth hormone stimulates longitudinal bone growth by a direct effect at the site of the growth plate or indirectly by increasing the concentration of circulating somatomedins (insulin-like growth factors) has been the subject of controversy. Immunohistochemical methods were used to explore the localization and distribution of insulin-like growth factor I (IGF-I) immunoreactivity in the epiphyseal growth plate of the proximal tibia of male rats. Cells in the proliferative zone of the growth plate of normal rats exhibited a bright immunofluorescence, whereas cells in the germinal and hypertrophic zones stained only weakly. In rats subjected to hypophysectomy, the number of fluorescent cells was markedly reduced. When the hypophysectomized rats were treated with growth hormone, either systemically or at the site of the growth plate, the number of IGF-I-immunoreactive cells in the proliferative zone was increased. The results show that IGF-I is produced in proliferative chondrocytes in the growth plate and that the number of IGF-I-containing cells is directly regulated by growth hormone. These findings suggest that IGF-I has a specific role in the clonal expansion of differentiated chondrocytes and exerts its function locally through autocrine or paracrine mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nilsson, A -- Isgaard, J -- Lindahl, A -- Dahlstrom, A -- Skottner, A -- Isaksson, O G -- New York, N.Y. -- Science. 1986 Aug 1;233(4763):571-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3523759" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Fluorescent Antibody Technique ; Growth Hormone/pharmacology/*physiology ; Growth Plate/*cytology/drug effects/growth & development ; Hypophysectomy ; Insulin-Like Growth Factor I/pharmacology/*physiology ; Male ; Rats ; Rats, Inbred Strains ; Somatomedins/*physiology ; Tibia
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  • 78
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-08-29
    Description: Study of the neurobiology of learning and memory is in a most exciting phase. Behavioral studies in animals are characterizing the categories and properties of learning and memory; essential memory trace circuits in the brain are being defined and localized in mammalian models; work on human memory and the brain is identifying neuronal systems involved in memory; the neuronal, neurochemical, molecular, and biophysical substrates of memory are beginning to be understood in both invertebrate and vertebrate systems; and theoretical and mathematical analysis of basic associative learning and of neuronal networks in proceeding apace. Likely applications of this new understanding of the neural bases of learning and memory range from education to the treatment of learning disabilities to the design of new artificial intelligence systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, R F -- New York, N.Y. -- Science. 1986 Aug 29;233(4767):941-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3738519" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia/physiology ; Brain/physiology ; Cerebellum/physiology ; Cerebral Cortex/physiology ; Conditioning, Classical/physiology ; Hippocampus/physiology ; Humans ; Learning/*physiology ; Memory/*physiology ; Neural Pathways/physiology ; Neurons/physiology ; Primates ; Rats ; Synapses/physiology
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  • 79
    Publication Date: 1986-08-22
    Description: In order to characterize the variability of the expressed human T-cell receptor (TCR) beta-chain repertoire and contrast this variability to the known murine beta-chain repertoire, 15 independent complementary DNA (cDNA) clones containing TCR beta-chain variable region (V beta) genes were isolated from a human tonsil cDNA library. The nucleotide and derived amino acid sequences of these 15 V beta genes were analyzed together with 7 previously defined sequences. Fifteen different human V beta genes could be identified from 22 independent sequences. By means of DNA hybridization and sequence homology comparisons, it was possible to group these 15 genes into ten distinct V beta subfamilies, each containing from one to seven members. Minimal polymorphism was noted between individuals, except in multimember subfamilies. The amino acid sequences of these genes contain conserved amino acids that are also shared by murine TCR V beta genes and immunoglobulins; no features were found that distinguish human V beta genes from their murine counterparts. Evaluation of secondary structure showed that maximum variability coincides with generally hydrophilic portions of the amino acid sequence, while specific hydrophobic regions were conserved in all V beta genes examined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tillinghast, J P -- Behlke, M A -- Loh, D Y -- 2-T32-AI00112/AI/NIAID NIH HHS/ -- GM 07200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 22;233(4766):879-83.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3755549" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Dna ; Genes ; Humans ; Nucleic Acid Hybridization ; Polymorphism, Genetic ; Receptors, Antigen, T-Cell/*genetics
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  • 80
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-11-21
    Description: Long-term potentiation (LTP), a long-lasting enhancement of synaptic efficacy, is considered a model for learning and memory. In anesthetized rats, activation of dentate granule cells by stimulating either the medial or lateral perforant pathway at frequencies of 100 to 400 Hz produced LTP of the stimulated pathway preferentially at 400 Hz. However, hippocampal pathways do not normally fire at this high rate. Stimuli at 200 Hz were then applied to either the medial or lateral pathway separately, to both pathways simultaneously, or to the two pathways asynchronously so that the composite stimulus applied to the granule cell dendrite was 400 Hz. LTP was produced preferentially in the asynchronous condition. Thus, lower frequency, physiological input volleys arriving asynchronously at medial and lateral synapses can induce LTP by activating a 400-Hz sensitive mechanism capable of integrating spatially separated granule cell inputs. This may reflect how LTP is normally produced in the dentate gyrus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Winson, J -- Dahl, D -- 5-K02-MH00232/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 21;234(4779):985-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775372" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electric Stimulation ; Evoked Potentials ; Hippocampus/*physiology ; Neurons, Afferent/physiology ; Rats
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 81
    Publication Date: 1986-06-27
    Description: Antibodies were raised against a synthetic peptide corresponding to 14 amino acid residues at the COOH-terminus of a protein deduced from the human c-erbB-2 nucleotide sequence. These antibodies immunoprecipitated a 185-kilodalton glycoprotein from MKN-7 adenocarcinoma cells. Incubation of the immunoprecipitates with (gamma-32P)ATP resulted in the phosphorylation of this protein on tyrosine residues. These results indicate that the human c-erbB-2 gene product is the 185-kilodalton glycoprotein that is associated with tyrosine kinase activity. Although the c-erbB-2 protein was predicted to encode a protein very similar to epidermal growth factor (EGF) receptor, EGF did not stimulate this kinase activity either in vivo or in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akiyama, T -- Sudo, C -- Ogawara, H -- Toyoshima, K -- Yamamoto, T -- New York, N.Y. -- Science. 1986 Jun 27;232(4758):1644-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3012781" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Epidermal Growth Factor/metabolism ; *Genes ; Glycoproteins/genetics/isolation & purification/*metabolism ; HeLa Cells/metabolism ; Humans ; Molecular Weight ; Oncogenes ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/metabolism
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  • 82
    Publication Date: 1986-02-07
    Description: Protein kinase C activity in rat hippocampal membranes and cytosol was determined 1 minute and 1 hour after induction of the synaptic plasticity of long-term potentiation. At 1 hour after long-term potentiation, but not at 1 minute, protein kinase C activity was increased twofold in membranes and decreased proportionately in cytosol, suggesting translocation of the activity. This time-dependent redistribution of enzyme activity was directly related to the persistence of synaptic plasticity, suggesting a novel mechanism regulating the strength of synaptic transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akers, R F -- Lovinger, D M -- Colley, P A -- Linden, D J -- Routtenberg, A -- MH25281/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):587-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003904" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/enzymology ; Cytosol/enzymology ; Enzyme Activation ; Hippocampus/*enzymology/physiology ; Male ; Neuronal Plasticity ; Protein Kinase C/metabolism/*physiology ; Rats ; Synaptic Membranes/enzymology ; Synaptic Transmission
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  • 83
    Publication Date: 1986-11-07
    Description: Dense, focal injections of wheat germ agglutinin conjugated-horseradish peroxidase in the locus coeruleus of rats labeled afferent neurons in unexpectedly few brain regions. Major inputs emanate from only two nuclei--the paragigantocellularis and the prepositus hypoglossi, both in the rostral medulla. The dorsal cap of the paraventricular hypothalamic nucleus and the spinal intermediate gray are possible minor afferents to locus coeruleus. Other areas reported to project to locus coeruleus (for example, amygdala, nucleus tractus solitarius, and spinal dorsal horn) did not exhibit consistent retrograde labeling. Anterograde tracing and electrophysiologic experiments confirmed the absence of input to locus coeruleus from these areas, which instead terminate in targets adjacent to locus coeruleus. These findings redefine the anatomic organization of the locus coeruleus, and have implications for hypotheses concerning the functions of this noradrenergic brain nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aston-Jones, G -- Ennis, M -- Pieribone, V A -- Nickell, W T -- Shipley, M T -- NS20643/NS/NINDS NIH HHS/ -- NS22320/NS/NINDS NIH HHS/ -- NS23348/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):734-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775363" target="_blank"〉PubMed〈/a〉
    Keywords: Afferent Pathways ; Animals ; Efferent Pathways ; Electric Stimulation ; Locus Coeruleus/anatomy & histology/*physiology ; Male ; Medulla Oblongata/cytology ; Paraventricular Hypothalamic Nucleus/cytology ; Rats ; Spinal Cord/cytology ; Wheat Germ Agglutinins
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  • 84
    Publication Date: 1986-02-28
    Description: Differentiation of lymphoid precursor cells in a variety of species is induced by polypeptide hormones such as thymopoietin for T cells and bursin for B cells. In the present experiments, bursin isolated from the bursa of Fabricius of chicken was found to induce the phenotypic differentiation of mammalian and avian B precursor cells but not of T precursor cells in vitro. Similarly, bursin increased cyclic guanosine monophosphate in cells of the human B-cell line Daudi but not in cells of the human T-cell line CEM. These inducing properties of bursin are the reverse of the inducing properties of thymopoietin produced by the thymus and are appropriate to a physiological B-cell-inducing hormone. A tripeptide sequence (lysyl-histidyl-glycyl-amide) was determined for bursin and confirmed by synthesizing this proposed structure and demonstrating chemical identity of the natural and synthetic peptides. Similarity of biological action was indicated in induction assays by elevation of cyclic adenosine monophosphate and guanosine monophosphate in Daudi B cells but not in CEM T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Audhya, T -- Kroon, D -- Heavner, G -- Viamontes, G -- Goldstein, G -- New York, N.Y. -- Science. 1986 Feb 28;231(4741):997-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3484838" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*physiology ; Bursa of Fabricius/*physiology ; Cell Line ; Chickens ; Chromatography, High Pressure Liquid ; Chromatography, Thin Layer ; Humans ; Mass Spectrometry ; Oligopeptides/*isolation & purification/pharmacology/physiology ; Rats ; T-Lymphocytes/drug effects
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-03-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, B M -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1505.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3952493" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Brain/cytology/*embryology ; Cell Differentiation ; Nerve Tissue/transplantation ; Peripheral Nerves/*cytology ; Rats
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-11-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, D M -- New York, N.Y. -- Science. 1986 Nov 21;234(4779):938-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3022378" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/physiopathology ; Disease Models, Animal ; Epilepsy/*physiopathology ; Humans ; Kindling, Neurologic ; Neural Inhibition ; Rats ; *Synaptic Transmission
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  • 87
    Publication Date: 1986-01-10
    Description: In rats infected with the parasite Schistosoma mansoni, the concentration of C-reactive protein in the serum increases after the lung stage of infection and is at its highest at the time of terminal worm rejection. The peak of platelet-mediated cytotoxicity induced by infected serum that has been heated (and is free of immunoglobulin E) as well as the time course for the development of platelet cytotoxic activity in infected rats was found to be correlated with the concentration of C-reactive protein. Rat and human platelets treated with homologous serum obtained during an acute phase of inflammation or with purified C-reactive protein were able to kill the immature forms of the worm in vitro. Platelets treated with C-reactive protein were furthermore capable of conferring significant protection against schistosomiasis in transfer experiments. Collectively these data indicate that a system that includes C-reactive protein and platelets participates in the natural resistance of the rat to schistosomal infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bout, D -- Joseph, M -- Pontet, M -- Vorng, H -- Deslee, D -- Capron, A -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):153-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079916" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Platelets/*drug effects/immunology ; C-Reactive Protein/blood/immunology/*pharmacology ; Cytotoxicity, Immunologic/*drug effects ; Dose-Response Relationship, Drug ; Immunity, Innate/drug effects ; Rats ; Schistosomiasis mansoni/*immunology ; Turpentine/pharmacology
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  • 88
    Publication Date: 1986-10-31
    Description: The polypeptide encoded in URF6, the last unassigned reading frame of human mitochondrial DNA, has been identified with antibodies to peptides predicted from the DNA sequence. Antibodies prepared against highly purified respiratory chain NADH dehydrogenase from beef heart or against the cytoplasmically synthesized 49-kilodalton iron-sulfur subunit isolated from this enzyme complex, when added to a deoxycholate or a Triton X-100 mitochondrial lysate of HeLa cells, specifically precipitated the URF6 product together with the six other URF products previously identified as subunits of NADH dehydrogenase. These results strongly point to the URF6 product as being another subunit of this enzyme complex. Thus, almost 60% of the protein coding capacity of mammalian mitochondrial DNA is utilized for the assembly of the first enzyme complex of the respiratory chain. The absence of such information in yeast mitochondrial DNA dramatizes the variability in gene content of different mitochondrial genomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chomyn, A -- Cleeter, M W -- Ragan, C I -- Riley, M -- Doolittle, R F -- Attardi, G -- GM-11726/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):614-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3764430" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cytochrome Reductases/*genetics ; DNA/*genetics/isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Eukaryota/genetics ; Fungi/genetics ; HeLa Cells/metabolism ; Humans ; Mitochondria/enzymology ; NADH Dehydrogenase/*genetics ; Sequence Homology, Nucleic Acid
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  • 89
    Publication Date: 1986-08-15
    Description: Predictions of the structures of the antigen-binding domains of an antibody, recorded before its experimental structure determination and tested subsequently, were based on comparative analysis of known antibody structures or on conformational energy calculations. The framework, the relative positions of the hypervariable regions, and the folds of four of the hypervariable loops were predicted correctly. This portion includes all residues in contact with the antigen, in this case hen egg white lysozyme, implying that the main chain conformation of the antibody combining site does not change upon ligation. The conformations of three residues in each of the other two hypervariable loops are different in the predicted models and the experimental structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chothia, C -- Lesk, A M -- Levitt, M -- Amit, A G -- Mariuzza, R A -- Phillips, S E -- Poljak, R J -- GM25435/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):755-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3090684" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; *Antigen-Antibody Complex ; Chickens ; Egg White ; Female ; Immunoglobulin Fab Fragments ; *Immunoglobulin G ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; Immunoglobulin Variable Region ; Models, Molecular ; Muramidase/immunology ; Protein Conformation
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-02-28
    Description: gamma-Aminobutyric acid (GABA) is one of the major inhibitory neurotransmitters in the central nervous system. In the cerebral cortex, GABA-containing cells represent a subpopulation of interneurons. With semithin frozen sections, it is possible to demonstrate that most GABA neurons in the rat somatosensory cortex contain the calcium-binding protein parvalbumin and that parvalbumin is found virtually only in GABA neurons. Parvalbumin seems to influence the electrical properties and enzymatic machinery to modulate neuronal excitability and activity. The specific role of parvalbumin in GABA-containing cortical cells may be related to controlling the effectiveness of their inhibitory action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celio, M R -- New York, N.Y. -- Science. 1986 Feb 28;231(4741):995-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945815" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cerebral Cortex/analysis/*cytology ; Electrophysiology ; Male ; Muscle Proteins/*analysis ; Neurons/*analysis/physiology ; Parvalbumins/*analysis ; Rats ; gamma-Aminobutyric Acid/*physiology
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  • 91
    Publication Date: 1986-08-15
    Description: To define the functional domains of the progesterone receptor required for gene regulation, complementary DNA (cDNA) clones encoding the chicken progesterone receptor have been isolated from a chicken oviduct lambda gt11 cDNA expression library. Positive clones expressed antigenic determinants that cross-reacted with six monospecific antibodies derived from two independent sources. A 36-amino acid peptide sequence obtained by microsequencing of purified progesterone receptor was encoded by nucleotide sequences in the longest cDNA clone. Analysis of the amino acid sequence of the progesterone receptor deduced from the cDNA clones revealed a cysteine-rich region that was homologous to a region found in the estrogen and glucocorticoid receptors and to the avian erythroblastosis virus gag-erb-A fusion protein. Northern blot analysis with chicken progesterone receptor cDNA's indicated the existence of at least three messenger RNA species. These messages were found only in oviduct and could be induced by estrogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conneely, O M -- Sullivan, W P -- Toft, D O -- Birnbaumer, M -- Cook, R G -- Maxwell, B L -- Zarucki-Schulz, T -- Greene, G L -- Schrader, W T -- O'Malley, B W -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):767-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2426779" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Base Sequence ; Chickens ; *Cloning, Molecular ; Cross Reactions ; DNA/*metabolism ; Epitopes/analysis ; Female ; *Genes ; Humans ; Nucleic Acid Hybridization ; Oviducts/metabolism ; RNA, Messenger/genetics ; Receptors, Progesterone/*genetics ; Species Specificity
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  • 92
    Publication Date: 1986-08-22
    Description: A new family of protein kinase C-related genes has been identified in bovine, human, and rat genomes. The alpha-, beta-, and gamma-type protein kinase sequences are highly homologous, include a kinase domain, and potential calcium-binding sites, and they contain interspersed variable regions. The corresponding genes are located on distinct human chromosomes; the possibility of even greater genetic complexity of this gene family is suggested by Northern and Southern hybridization analyses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coussens, L -- Parker, P J -- Rhee, L -- Yang-Feng, T L -- Chen, E -- Waterfield, M D -- Francke, U -- Ullrich, A -- New York, N.Y. -- Science. 1986 Aug 22;233(4766):859-66.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3755548" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; Chromosome Mapping ; Chromosomes, Human, 16-18 ; Dna ; Genes ; Humans ; Nucleic Acid Hybridization ; Protein Kinase C/*genetics ; Rats
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-02-07
    Description: Measurements confirm the quantitative theoretical prediction that the autonomic nonendocrine abnormality of rapid daytime gastric emptying is the major primary cause of the obesity resulting from ventromedial hypothalamic lesions in rats. Therapy for obesity could include slowing of stomach emptying.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duggan, J P -- Booth, D A -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):609-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3511527" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Feeding and Eating Disorders/*physiopathology ; *Gastric Emptying/drug effects ; Humans ; Hyperphagia/etiology/*physiopathology ; Insulin/pharmacology ; Obesity/etiology/*physiopathology ; Rats ; Rats, Inbred Strains ; Time Factors ; Ventromedial Hypothalamic Nucleus/*physiology
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  • 94
    Publication Date: 1986-01-10
    Description: The catalytically essential amino acid in the active site of bacterial alkaline phosphatase (Ser-102) has been replaced with a cysteine by site-directed mutagenesis. The resulting thiol enzyme catalyzes the hydrolysis of a variety of phosphate monoesters. The rate-determining step of hydrolysis, however, is no longer the same for catalysis when the active protein nucleophile is changed from the hydroxyl of serine to the thiol of cysteine. Unlike the steady-state kinetics of native alkaline phosphatase, those of the mutant show sensitivity to the leaving group of the phosphate ester.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, S S -- Bock, S C -- Rokita, S E -- Kaiser, E T -- AM 07122-02/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):145-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3510454" target="_blank"〉PubMed〈/a〉
    Keywords: *2,4-Dinitrophenol/*analogs & derivatives ; Alkaline Phosphatase/*genetics/metabolism ; Amino Acid Sequence ; Binding Sites ; DNA/genetics ; Dinitrophenols/metabolism ; Escherichia coli/enzymology/genetics ; Kinetics ; Mutation ; Nitrophenols/metabolism ; Organophosphates/metabolism ; Organophosphorus Compounds/metabolism ; Plasmids
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-10-03
    Description: Cholinergic agonists rapidly and transiently induced transcription of the c-fos protooncogene and one or more actin genes in neuronally differentiated PC12 cells. Transcription was activated within minutes after stimulation of the nicotinic acetylcholine receptor and required an influx of extracellular Ca2+ ions through voltage-sensitive calcium channels. Nicotine activation proceeded by a different pathway from activation by nerve growth factor, whose stimulation of these genes is independent of extracellular Ca2+ ions. These findings suggest that neurotransmitters may rapidly activate specific gene transcription in nondividing neuronally differentiated cells. They also suggest a functional role for neurotransmitter induction of c-fos and actin expression in the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greenberg, M E -- Ziff, E B -- Greene, L A -- GM 30760/GM/NIGMS NIH HHS/ -- NS16036/NS/NINDS NIH HHS/ -- P30 CA 16087/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Oct 3;234(4772):80-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3749894" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Adrenal Gland Neoplasms/metabolism ; Animals ; Calcium/metabolism ; Cell Line ; Dose-Response Relationship, Drug ; Nerve Growth Factors/pharmacology ; Nicotine/pharmacology ; Pheochromocytoma/metabolism ; Rats ; Receptors, Cholinergic/*drug effects ; Transcription, Genetic/*drug effects
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  • 96
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1986 Dec 5;234(4781):1198-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775379" target="_blank"〉PubMed〈/a〉
    Keywords: Alcoholic Intoxication/*drug therapy ; Animals ; Azides/*pharmacology/therapeutic use ; Benzodiazepines/*pharmacology/therapeutic use ; Ethanol/*antagonists & inhibitors ; Humans ; Rats
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  • 97
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, C -- New York, N.Y. -- Science. 1986 Apr 11;232(4747):147-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3952503" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Care Committees ; *Animal Experimentation ; Animal Testing Alternatives ; *Animal Welfare ; Animals ; *Animals, Laboratory ; Aplysia ; Birds ; Chick Embryo ; Decapodiformes ; Federal Government ; Government Regulation ; Horseshoe Crabs ; Macaca ; Mice ; National Institutes of Health (U.S.) ; Rabbits ; Rats ; United States ; are discussed. The enactment of amendments to the Animal Welfare Act of 1966 and ; revisions to the Public Health Service's animal care guidelines are described as ; major federal moves to tighten standards and to locate responsibility for proper ; animal care at the institutional level. These regulatory changes will have a ; significant economic impact on the cost of doing research, but are generally ; accepted by the scientific community as necessary. Although moderate animal ; welfare groups see signs of progress, there is a growing number of activists who ; see recent policy developments as only a step toward the real goal of total ; elimination of the use of animals in research. It is apparent that the ; combination of political pressure, financial stringency, and better experimental ; methodologies will result in a continued reduction in laboratory animal use.
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  • 98
    Publication Date: 1986-12-12
    Description: While much information exists about the structure and function of the clonally distributed T cell receptor (TCR) alpha beta heterodimer, little is known about the gamma protein, the product of a third rearranging TCR gene. An antiserum to a carboxyl-terminal peptide common to several of the murine gamma chain constant regions and a monoclonal antibody to the murine T3 complex were used to identify products of this TCR gene family in a subpopulation of Lyt2-, L3T4- thymocytes. This subpopulation does not express TCR alpha or full-length TCR beta messenger RNA. The gamma chain is a 35-kilodalton (kD) protein that is disulfide-bonded to a 45-kD partner and is associated with the T3 complex. Analysis of the glycosylation pattern of this thymic gamma chain revealed that the major variable region gamma (V gamma) gene transcribed in activated peripheral T cells is absent from this subpopulation. The cells that bear this second T cell receptor may therefore represent a distinct lineage differentiating within the thymus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lew, A M -- Pardoll, D M -- Maloy, W L -- Fowlkes, B J -- Kruisbeek, A -- Cheng, S F -- Germain, R N -- Bluestone, J A -- Schwartz, R H -- Coligan, J E -- New York, N.Y. -- Science. 1986 Dec 12;234(4782):1401-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3787252" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Disulfides/analysis ; Electrophoresis, Polyacrylamide Gel ; Glycosylation ; Macromolecular Substances ; Mice ; Molecular Weight ; RNA, Messenger/metabolism ; Receptors, Antigen, T-Cell/*biosynthesis/genetics ; Structure-Activity Relationship ; Thymus Gland/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-04-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alpher, V S -- New York, N.Y. -- Science. 1986 Apr 18;232(4748):307.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961482" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Humans ; Male ; *Psychosexual Development ; Rats ; Sexual Behavior
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 1986-07-18
    Description: Determination of the molecular structure and properties of allergens that elicit severe immediate-type hypersensitivity diseases in humans and a knowledge of the structure of their antibody-binding sites should provide new insight into the pathogenetic mechanisms of allergic diseases. Monomeric and homodimeric hemoglobins (CTT I to X) have been identified as potent allergenic components of Chironomidae, a family of Diptera. Immunologic investigations of peptides of three of these hemoglobins (CTT IV, CTT VI, and CTT VIII) showed that human antibodies of the E and G classes recognize at least two different sites within each molecule. Individual hemoglobin peptides were aligned with homologous regions of chironomid hemoglobin CTT III, whose tertiary structure has been determined by x-ray analysis at a resolution of 1.4 angstroms. The antigenic site CTT IV(91 to 101) showed the following characteristics: (i) seven polar or hydroxylated amino acids, from a total of eleven, occupying predominantly superficial regions; (ii) the property of linkage to other molecules by hydrogen bonds or solvent clusters; and (iii) high thermal mobility factors. In contrast, peptide CTT IV(102 to 108), which does not bind human antibodies, contained no polar amino acids and had low thermal mobility factors. These results support the idea that the antigenicity of clinically relevant proteins is related to regions with a predominance of polar amino acids and with low energy barriers between different conformations, which allow high flexibility, including site-specific adaptation in antibody binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baur, X -- Aschauer, H -- Mazur, G -- Dewair, M -- Prelicz, H -- Steigemann, W -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):351-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2425431" target="_blank"〉PubMed〈/a〉
    Keywords: Allergens/*immunology ; Amino Acid Sequence ; Animals ; Chironomidae/*immunology ; Diptera/*immunology ; Epitopes/*analysis ; Hemoglobins/analysis/*immunology ; Larva/analysis ; Molecular Conformation ; Peptide Fragments/analysis ; Temperature
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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