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  • 1
    Publication Date: 1989-12-22
    Description: T cell clones obtained from a human volunteer immunized with Plasmodium falciparum sporozoites specifically recognized the native circumsporozoite (CS) antigen expressed on P. falciparum sporozoites, as well as bacteria- and yeast-derived recombinant falciparum CS proteins. The response of these CD4+ CD8- cells was species-specific, since the clones did not proliferate or secrete gamma interferon when challenged with sporozoites or recombinant CS proteins of other human, simian, or rodent malarias. The epitope recognized by the sporozoite-specific human T cell clones mapped to the 5' repeat region of the CS protein and was contained in the NANPNVDPNANP sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nardin, E H -- Herrington, D A -- Davis, J -- Levine, M -- Stuber, D -- Takacs, B -- Caspers, P -- Barr, P -- Altszuler, R -- Clavijo, P -- AI25085/AI/NIAID NIH HHS/ -- AI62533/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1603-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical and Molecular Parasitology, New York University, NY 10010.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2480642" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*immunology ; Antigens, Protozoan/*immunology ; Cells, Cultured ; Clone Cells ; Epitopes/*analysis ; Humans ; Interferon-gamma/biosynthesis ; Lymphocyte Activation ; Malaria/*immunology ; Molecular Sequence Data ; Plasmodium falciparum/*immunology ; *Protozoan Proteins ; Recombinant Proteins/immunology ; T-Lymphocytes/*immunology
    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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  • 2
    Publication Date: 1988-12-16
    Description: Human T cell leukemia viruses (HTLV-I and HTLV-II) can infect many cell types in vitro. HTLV-I and HTLV-II use the same cell surface receptor, as shown by interference with syncytium formation and with infection by vesicular stomatitis virus (VSV) pseudotypes bearing the HTLV envelope glycoproteins. Human-mouse somatic cell hybrids were used to determine which human chromosome was required to confer susceptibility to VSV(HTLV) infection. The only human chromosome common to all susceptible cell hybrids was chromosome 17, and the receptor gene was localized to 17cen-qter. Antibodies to surface antigens known to be determined by genes on 17q did not block the HTLV receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sommerfelt, M A -- Williams, B P -- Clapham, P R -- Solomon, E -- Goodfellow, P N -- Weiss, R A -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1557-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chester Beatty Laboratories, Institute of Cancer Research, London, U.K.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201246" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cell Line ; Chromosome Mapping ; *Chromosomes, Human, Pair 17 ; Cricetinae ; *Genes ; Human T-lymphotropic virus 1/*physiology ; Human T-lymphotropic virus 2/*physiology ; Humans ; Hybrid Cells/cytology/microbiology ; Mice ; Rats ; Receptors, Virus/*genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1988-02-05
    Description: An expression vector for the epidermal growth factor (EGF) receptor was introduced into the 32D myeloid cell line, which is devoid of EGF receptors and absolutely dependent on interleukin-3 (IL-3) for its proliferation and survival. Expression of the EGF receptor conferred the ability to utilize EGF for transduction of a mitogenic signal. When the transfected cells were propagated in EGF, they exhibited a more mature myeloid phenotype than was observed under conditions of IL-3-directed growth. Moreover, exposure to EGF led to a rapid stimulation of phosphoinositide metabolism, while IL-3 had no detectable effect on phosphoinositide turnover either in control or EGF receptor-transfected 32D cells. Although the transfected cells exhibited high levels of functional EGF receptors, they remained nontumorigenic. In contrast, transfection of v-erbB, an amino-terminal truncated form of the EGF receptor with constitutive tyrosine kinase activity, not only abrogated the IL-3 growth factor requirement of 32D cells, but caused them to become tumorigenic in nude mice. These results show that a naive hematopoietic cell expresses all of the intracellular components of the EGF-signaling pathway necessary to evoke a mitogenic response and sustain continuous proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pierce, J H -- Ruggiero, M -- Fleming, T P -- Di Fiore, P P -- Greenberger, J S -- Varticovski, L -- Schlessinger, J -- Rovera, G -- Aaronson, S A -- New York, N.Y. -- Science. 1988 Feb 5;239(4840):628-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3257584" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cell Line ; *Cloning, Molecular ; DNA Replication/drug effects ; Epidermal Growth Factor/metabolism/pharmacology ; Genetic Vectors ; Hematopoietic Stem Cells/cytology/drug effects/*metabolism ; Interleukin-3/*pharmacology ; Receptor, Epidermal Growth Factor/*genetics/metabolism ; *Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1987-07-24
    Description: Removal of the representation of a specific body part in the postcentral cortex of the macaque resulted in the somatic deactivation of the corresponding body part in the second somatosensory area. In contrast, removal of the entire second somatosensory area had no grossly detectable effect on the somatic responsivity of neurons in the postcentral cortex. This direct electrophysiological evidence for serial cortical processing in somesthesia is similar to that found earlier for vision and, taken together with recent anatomical evidence, suggests that there is a common cortical plan for the processing of sensory information in the various sensory modalities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pons, T P -- Garraghty, P E -- Friedman, D P -- Mishkin, M -- NS07497/NS/NINDS NIH HHS/ -- NS07704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):417-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603028" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Functional Laterality ; Hand/innervation ; Macaca fascicularis ; Macaca mulatta ; Models, Neurological ; Neurons/physiology ; Somatosensory Cortex/*physiology
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  • 5
    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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  • 6
    Publication Date: 1987-09-04
    Description: Tumor necrosis factor, or cachectin (TNF-alpha), a protein with a wide range of biological activities, is produced mainly by macrophages and may be important in inflammatory processes. The role of TNF-alpha in the pathogenesis of cerebral malaria was investigated in a murine model. Most CBA mice infected with Plasmodium berghei anka die between days 6 and 14 with acute neurological manifestations unrelated to the level of parasitemia, whereas mice of some other strains have malaria of the same severity that ends in death after 3 to 4 weeks without neurological manifestations. The activity of serum TNF-alpha was considerably increased in CBA/Ca mice with cerebral malaria but not in Plasmodium berghei-infected mice that did not develop this complication. One injection of rabbit antibody to TNF-alpha on day 4 or 7 fully protected infected mice from cerebral malaria without modifying the parasitemia, whereas immunoglobulins from normal rabbit had no effect. In mice with cerebral malaria, the cerebral vessels showed focal accumulations of packed macrophages often containing infected erythrocytes; this lesion was not seen in mice treated with antibody to TNF-alpha or in untreated mice without cerebral malaria. These findings indicate that TNF-alpha has an important role in the pathogenesis of cerebral malaria in this murine model and suggest that local accumulation and activation of macrophages may lead to the predominance of lesions in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grau, G E -- Fajardo, L F -- Piguet, P F -- Allet, B -- Lambert, P H -- Vassalli, P -- New York, N.Y. -- Science. 1987 Sep 4;237(4819):1210-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3306918" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Diseases/etiology/pathology/*physiopathology ; Cerebral Cortex/pathology ; Glycoproteins/*physiology ; *Macrophage Activation ; Macrophages/cytology ; Malaria/complications/pathology/*physiopathology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred CBA ; Plasmodium berghei ; Tumor Necrosis Factor-alpha
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1986-04-11
    Description: Synapses develop concurrently and at identical rates in different layers of the visual, somatosensory, motor, and prefrontal areas of the primate cerebral cortex. This isochronic course of synaptogenesis in anatomically and functionally diverse regions indicates that the entire cerebral cortex develops as a whole and that the establishment of cell-to-cell communication in this structure may be orchestrated by a single genetic or humoral signal. This is in contrast to the traditional view of hierarchical development of the cortical regions and provides new insight into the maturation of cortical functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rakic, P -- Bourgeois, J P -- Eckenhoff, M F -- Zecevic, N -- Goldman-Rakic, P S -- EY02593/EY/NEI NIH HHS/ -- MH38546/MH/NIMH NIH HHS/ -- NS22807/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 11;232(4747):232-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3952506" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cerebral Cortex/growth & development/*physiology ; Macaca mulatta ; Motor Cortex/growth & development/physiology ; Somatosensory Cortex/growth & development/physiology ; Synapses/*physiology ; Visual Cortex/growth & development/physiology
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  • 8
    Publication Date: 1987-12-11
    Description: Peptides corresponding to the amino-terminal region of the parathyroid hormone-related protein (PTHrP) of humoral hypercalcemia of malignancy were synthesized. A 34-amino acid peptide, PTHrP(1-34), was two to four times more potent than bovine or human PTH(1-34) in bioassays promoting the formation of adenosine 3',5'-monophosphate (cAMP) and plasminogen activator activity in osteogenic sarcoma cells and adenylate cyclase activity in chick kidney membranes. Like parathyroid hormone itself, in which the activity resides in the first 34 residues, PTHrP peptides of less than 30 residues from the amino terminus showed substantially reduced activity. PTHrP(1-34) had only 6% of the potency of bovine PTH(1-34) in promoting bone resorption in vitro. PTHrP(1-34) strongly promoted the excretion of cAMP and phosphorus and reduced the excretion of calcium in the isolated, perfused rat kidney consistent with the symptoms seen in malignant hypercalcemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kemp, B E -- Moseley, J M -- Rodda, C P -- Ebeling, P R -- Wettenhall, R E -- Stapleton, D -- Diefenbach-Jagger, H -- Ure, F -- Michelangeli, V P -- Simmons, H A -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1568-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Melbourne, Department of Medicine, Repatriation General Hospital, Heidelberg, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Resorption/*drug effects ; Bone and Bones/metabolism ; Calcium/metabolism ; Cattle ; Cells, Cultured ; Humans ; Hypercalcemia/etiology ; Neoplasms/*physiopathology ; Parathyroid Hormone/*pharmacology/physiology ; Peptide Fragments/*pharmacology/physiology ; Structure-Activity Relationship ; Teriparatide
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  • 9
    Publication Date: 1987-10-23
    Description: The p21 products of ras proto-oncogenes are thought to be important components in pathways regulating normal cell proliferation and differentiation. These proteins acquire transforming properties as a result of activating lesions that convert ras genes to oncogenes in a wide array of malignancies. In Xenopus laevis oocytes, microinjection of transforming ras p21 is a potent inducer of maturation, whereas microinjection of a monoclonal antibody to ras p21 inhibits normal maturation induced by hormones. The phosphoinositide pathway is a ubiquitous system that appears to play a key role in diverse cellular functions. By use of the Xenopus oocyte system, it was possible to quantitate the effects of ras p21 microinjection on individual components of the phosphoinositide pathway. Within 20 minutes of microinjection, levels of phosphatidylinositol 4,5-bisphosphate, inositol 1-phosphate, and inositol bisphosphate increased 1.5- to 2-fold. The most striking effects were on diacylglycerol, which increased 5-fold under the same conditions. In contrast, the normal ras p21 protein induced no detectable alteration in any of the metabolites analyzed. The earliest effects of the transforming p21 on phosphoinositol turnover were observable within 2 minutes, implying a very rapid effect of ras p21 on the enzymes involved in phospholipid metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lacal, J C -- de la Pena, P -- Moscat, J -- Garcia-Barreno, P -- Anderson, P S -- Aaronson, S A -- New York, N.Y. -- Science. 1987 Oct 23;238(4826):533-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2821623" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Diglycerides/*biosynthesis ; Female ; Glycerides/*biosynthesis ; Glycerol/metabolism ; Inositol/metabolism ; Inositol Phosphates/biosynthesis ; Kinetics ; Microinjections ; Oocytes/drug effects/*metabolism ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/biosynthesis/*metabolism ; Proto-Oncogene Proteins/*pharmacology ; Proto-Oncogene Proteins p21(ras) ; Xenopus laevis
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  • 10
    Publication Date: 1988-09-09
    Description: Human platelet-derived growth factor (PDGF) consists of two distinct but related polypeptide chains designated PDGF-A and PDGF-B. The gene encoding PDGF-B has given rise to the v-sis oncogene. In the present study the transforming activities of PDGF-A and PDGF-B genes are compared. The PDGF-A chain gene is markedly less efficient in inducing transformation than the PDGF-B gene under the influence of the same promoter. There are significant differences in the secretory and growth stimulating properties of the two chains. These properties appear to account for the much more potent transforming ability of the PDGF-B gene. These findings provide insights into biologic properties of a growth factor responsible for potent autocrine stimulation of abnormal cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beckmann, M P -- Betsholtz, C -- Heldin, C H -- Westermark, B -- Di Marco, E -- Di Fiore, P P -- Robbins, K C -- Aaronson, S A -- New York, N.Y. -- Science. 1988 Sep 9;241(4871):1346-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842868" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Compartmentation ; Cell Line ; *Cell Transformation, Neoplastic ; Gene Expression Regulation ; Immunologic Techniques ; Mice ; Molecular Weight ; Platelet-Derived Growth Factor/*physiology ; Proto-Oncogene Proteins/*physiology ; Receptors, Cell Surface/*physiology ; Receptors, Platelet-Derived Growth Factor ; Solubility
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