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  • Cells, Cultured  (49)
  • American Association for the Advancement of Science (AAAS)  (49)
  • American Meteorological Society
  • 2000-2004  (49)
  • 1995-1999
  • 1990-1994
  • 2000  (49)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (49)
  • American Meteorological Society
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  • 2000-2004  (49)
  • 1995-1999
  • 1990-1994
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-06
    Description: A human cytomegalovirus gene array was used to identify a previously unidentified class of viral transcripts. These transcripts, termed virion RNAs, were packaged within infectious virions and were delivered to the host cell on infection. This mechanism of herpesvirus gene expression allows for viral genes to be expressed within an infected cell immediately after virus entry and in the absence of transcription from the viral genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bresnahan, W A -- Shenk, T -- CA85786/CA/NCI NIH HHS/ -- F32 AI010448/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2373-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875924" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/metabolism ; Cells, Cultured ; Cytomegalovirus/*genetics/*physiology ; Dactinomycin/pharmacology ; Gene Expression ; Genes, Viral ; Genome, Viral ; Golgi Apparatus/metabolism ; Humans ; Nucleic Acid Hybridization ; Nucleic Acid Synthesis Inhibitors/pharmacology ; Oligonucleotide Array Sequence Analysis ; RNA, Messenger/*genetics/isolation & purification/metabolism ; RNA, Viral/*genetics/isolation & purification/metabolism ; Recombinant Fusion Proteins/metabolism ; Transcription, Genetic ; Viral Proteins/genetics/metabolism ; Virion/*genetics/physiology ; Virus Assembly
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    Electronic ISSN: 1095-9203
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  • 2
    Publication Date: 2000-09-01
    Description: Activation of the transcription factor nuclear factor (NF)-kappaB by proinflammatory stimuli leads to increased expression of genes involved in inflammation. Activation of NF-kappaB requires the activity of an inhibitor of kappaB (IkappaB)-kinase (IKK) complex containing two kinases (IKKalpha and IKKbeta) and the regulatory protein NEMO (NF-kappaB essential modifier). An amino-terminal alpha-helical region of NEMO associated with a carboxyl-terminal segment of IKKalpha and IKKbeta that we term the NEMO-binding domain (NBD). A cell-permeable NBD peptide blocked association of NEMO with the IKK complex and inhibited cytokine-induced NF-kappaB activation and NF-kappaB-dependent gene expression. The peptide also ameliorated inflammatory responses in two experimental mouse models of acute inflammation. The NBD provides a target for the development of drugs that would block proinflammatory activation of the IKK complex without inhibiting basal NF-kappaB activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉May, M J -- D'Acquisto, F -- Madge, L A -- Glockner, J -- Pober, J S -- Ghosh, S -- AI 33443/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 1;289(5484):1550-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology and Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10968790" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/chemistry/pharmacology ; COS Cells ; Cells, Cultured ; E-Selectin/biosynthesis/genetics ; Endothelium, Vascular/metabolism ; Gene Expression Regulation ; HeLa Cells ; Humans ; I-kappa B Kinase ; Inflammation/drug therapy ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; NF-kappa B/*metabolism ; Peptides/chemistry/*pharmacology ; Point Mutation ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism
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  • 3
    Publication Date: 2000-05-29
    Description: Pathogenic mycobacteria, including the agent of tuberculosis, Mycobacterium tuberculosis, must replicate in macrophages for long-term persistence within their niche during chronic infection: organized collections of macrophages and lymphocytes called granulomas. We identified several genes preferentially expressed when Mycobacterium marinum, the cause of fish and amphibian tuberculosis, resides in host granulomas and/or macrophages. Two were homologs of M. tuberculosis PE/PE-PGRS genes, a family encoding numerous repetitive glycine-rich proteins of unknown function. Mutation of two PE-PGRS genes produced M. marinum strains incapable of replication in macrophages and with decreased persistence in granulomas. Our results establish a direct role in virulence for some PE-PGRS proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ramakrishnan, L -- Federspiel, N A -- Falkow, S -- AI 32396/AI/NIAID NIH HHS/ -- K08 AI 01400/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 May 26;288(5470):1436-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. lalitar@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827956" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/chemistry/*genetics ; Cells, Cultured ; Disease Models, Animal ; Gene Expression Profiling ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Glycine/analysis ; Granuloma/*microbiology/pathology ; Humans ; Macrophages/*microbiology ; Mutation ; Mycobacterium Infections, Nontuberculous/*microbiology/pathology ; Mycobacterium marinum/*genetics/growth & development/*pathogenicity ; Mycobacterium tuberculosis/genetics/pathogenicity ; Promoter Regions, Genetic ; Rana pipiens ; Tuberculosis/microbiology ; Virulence
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  • 4
    Publication Date: 2000-07-15
    Description: Bone morphogenetic proteins (BMPs) have multiple functions in the developing nervous system. A member of this family, BMP-9, was found to be highly expressed in the embryonic mouse septum and spinal cord, indicating a possible role in regulating the cholinergic phenotype. In cultured neurons, BMP-9 directly induced the expression of the cholinergic gene locus encoding choline acetyltransferase and the vesicular acetylcholine transporter and up-regulated acetylcholine synthesis. The effect was reversed upon withdrawal of BMP-9. Intracerebroventricular injection of BMP-9 increased acetylcholine levels in vivo. Although certain other BMPs also up-regulated the cholinergic phenotype in vitro, they were less effective than BMP-9. These data indicate that BMP-9 is a differentiating factor for cholinergic central nervous system neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lopez-Coviella, I -- Berse, B -- Krauss, R -- Thies, R S -- Blusztajn, J K -- P01 AG09525/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 14;289(5477):313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry and Department of Pathology and Laboratory Medicine, Boston University School of Medicine, Boston, MA 02118, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10894782" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/biosynthesis ; Animals ; Bone Morphogenetic Proteins/*physiology ; Carrier Proteins/genetics ; Cells, Cultured ; Central Nervous System ; Choline O-Acetyltransferase/genetics ; Embryo, Mammalian/metabolism ; Fibroblast Growth Factor 2/physiology ; Gene Expression Regulation, Developmental ; Gene Expression Regulation, Enzymologic ; Growth Differentiation Factor 2 ; *Membrane Transport Proteins ; Mice ; Neurons/metabolism ; Phenotype ; RNA, Messenger/metabolism ; Septum of Brain/embryology/metabolism ; Spinal Cord/embryology/metabolism ; Up-Regulation ; Vesicular Acetylcholine Transport Proteins ; *Vesicular Transport Proteins
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  • 5
    Publication Date: 2000-02-11
    Description: The nonclassical major histocompatibility complex (MHC) class I molecule HLA-E inhibits natural killer (NK) cell-mediated lysis by interacting with CD94/NKG2A receptors. Surface expression of HLA-E depends on binding of conserved peptides derived from MHC class I molecules. The same peptide is present in the leader sequence of the human cytomegalovirus (HCMV) glycoprotein UL40 (gpUL40). It is shown that, independently of the transporter associated with antigen processing, gpUL40 can up-regulate expression of HLA-E, which protects targets from NK cell lysis. While classical MHC class I molecules are down-regulated, HLA-E is up-regulated by HCMV. Induction of HLA-E surface expression by gpUL40 may represent an escape route for HCMV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomasec, P -- Braud, V M -- Rickards, C -- Powell, M B -- McSharry, B P -- Gadola, S -- Cerundolo, V -- Borysiewicz, L K -- McMichael, A J -- Wilkinson, G W -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1031.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Wales College of Medicine, Cardiff CF14 4XN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669413" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; *Antigens, CD ; Cell Line ; Cell Membrane/immunology ; Cells, Cultured ; Conserved Sequence ; Cytomegalovirus/genetics/immunology/*metabolism ; Cytotoxicity, Immunologic ; Down-Regulation ; HLA Antigens/immunology/*metabolism ; Histocompatibility Antigens Class I/immunology/*metabolism ; Humans ; Killer Cells, Natural/*immunology ; Molecular Sequence Data ; Open Reading Frames ; Protein Sorting Signals/chemistry/*metabolism ; Receptors, Immunologic/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transfection ; Up-Regulation ; Viral Proteins/chemistry/genetics/*metabolism
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  • 6
    Publication Date: 2000-05-08
    Description: The c-Jun NH2-terminal kinase (JNK) is activated when cells are exposed to ultraviolet (UV) radiation. However, the functional consequence of JNK activation in UV-irradiated cells has not been established. It is shown here that JNK is required for UV-induced apoptosis in primary murine embryonic fibroblasts. Fibroblasts with simultaneous targeted disruptions of all the functional Jnk genes were protected against UV-stimulated apoptosis. The absence of JNK caused a defect in the mitochondrial death signaling pathway, including the failure to release cytochrome c. These data indicate that mitochondria are influenced by proapoptotic signal transduction through the JNK pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tournier, C -- Hess, P -- Yang, D D -- Xu, J -- Turner, T K -- Nimnual, A -- Bar-Sagi, D -- Jones, S N -- Flavell, R A -- Davis, R J -- New York, N.Y. -- Science. 2000 May 5;288(5467):870-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular Medicine, Department of Biochemistry & Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10797012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptotic Protease-Activating Factor 1 ; Caspase 3 ; Caspase 9 ; Caspases/metabolism ; Cell Count ; Cell Division ; Cells, Cultured ; Cytochrome c Group/*metabolism ; DNA Fragmentation ; Enzyme Activation ; Fibroblasts ; Gene Targeting ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Signaling System ; Methyl Methanesulfonate/pharmacology ; Mice ; Mitochondria/metabolism ; Mitogen-Activated Protein Kinases/genetics/*metabolism ; NF-kappa B/metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Tumor Suppressor Protein p53/metabolism ; Ultraviolet Rays
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  • 7
    Publication Date: 2000-04-25
    Description: Major histocompatibility complex class II (MHC II) molecules capture peptides within the endocytic pathway to generate T cell receptor (TCR) ligands. Immature dendritic cells (DCs) sequester intact antigens in lysosomes, processing and converting antigens into peptide-MHC II complexes upon induction of DC maturation. The complexes then accumulate in distinctive, nonlysosomal MHC II+ vesicles that appear to migrate to the cell surface. Although the vesicles exclude soluble lysosomal contents and antigen-processing machinery, many contain MHC I and B7 costimulatory molecules. After arrival at the cell surface, the MHC and costimulatory molecules remain clustered. Thus, transport of peptide-MHC II complexes by DCs not only accomplishes transfer from late endocytic compartments to the plasma membrane, but does so in a manner that selectively concentrates TCR ligands and costimulatory molecules for T cell contact.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turley, S J -- Inaba, K -- Garrett, W S -- Ebersold, M -- Unternaehrer, J -- Steinman, R M -- Mellman, I -- AI-13013/AI/NIAID NIH HHS/ -- AI-34098/AI/NIAID NIH HHS/ -- AI-39672/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):522-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Section of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520-8002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10775112" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; *Antigen Presentation ; Antigens, CD/immunology/metabolism ; Antigens, CD86 ; B-Lymphocytes/immunology/metabolism ; Bicyclo Compounds, Heterocyclic/pharmacology ; Biological Transport ; Cell Membrane/immunology/metabolism ; Cells, Cultured ; Dendritic Cells/*immunology/*metabolism ; Endocytosis ; Endosomes/immunology/metabolism ; Histocompatibility Antigens Class I/immunology/metabolism ; Histocompatibility Antigens Class II/immunology/*metabolism ; Kinetics ; Ligands ; Lipopolysaccharides/immunology ; Lysosomes/immunology/metabolism ; Membrane Glycoproteins/immunology/metabolism ; Mice ; Mice, Inbred C3H ; Muramidase/immunology/*metabolism ; Peptide Fragments/immunology/*metabolism ; Receptors, Antigen, T-Cell/metabolism ; Thiazoles/pharmacology ; Thiazolidines
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-04-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2133-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10744529" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Chemoreceptor Cells/*physiology ; Humans ; Mice ; Multigene Family ; Receptors, Cell Surface/genetics/*physiology ; *Taste ; Taste Buds/*physiology ; Transducin/biosynthesis
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  • 9
    Publication Date: 2000-08-19
    Description: Pig cloning will have a marked impact on the optimization of meat production and xenotransplantation. To clone pigs from differentiated cells, we microinjected the nuclei of porcine (Sus scrofa) fetal fibroblasts into enucleated oocytes, and development was induced by electroactivation. The transfer of 110 cloned embryos to four surrogate mothers produced an apparently normal female piglet. The clonal provenance of the piglet was indicated by her coat color and confirmed by DNA microsatellite analysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Onishi, A -- Iwamoto, M -- Akita, T -- Mikawa, S -- Takeda, K -- Awata, T -- Hanada, H -- Perry, A C -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1188-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Breeding and Genetics, National Institute of Animal Industry, Tsukuba Norin Danchi, Ibaraki-ken 305-0901, Japan. onishi@niai.affrc.go.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10947985" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Cloning, Organism/*methods ; Electric Stimulation ; Embryo Transfer ; Embryonic and Fetal Development ; Female ; Fetus/cytology ; Fibroblasts/ultrastructure ; Microinjections ; Microsatellite Repeats ; *Nuclear Transfer Techniques ; Oocytes ; Pregnancy ; *Swine/embryology/genetics
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  • 10
    Publication Date: 2000-01-05
    Description: Mutations in copper, zinc superoxide dismutase (SOD) have been implicated in the selective death of motor neurons in 2 percent of amyotrophic lateral sclerosis (ALS) patients. The loss of zinc from either wild-type or ALS-mutant SODs was sufficient to induce apoptosis in cultured motor neurons. Toxicity required that copper be bound to SOD and depended on endogenous production of nitric oxide. When replete with zinc, neither ALS-mutant nor wild-type copper, zinc SODs were toxic, and both protected motor neurons from trophic factor withdrawal. Thus, zinc-deficient SOD may participate in both sporadic and familial ALS by an oxidative mechanism involving nitric oxide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Estevez, A G -- Crow, J P -- Sampson, J B -- Reiter, C -- Zhuang, Y -- Richardson, G J -- Tarpey, M M -- Barbeito, L -- Beckman, J S -- R01 HL58209/HL/NHLBI NIH HHS/ -- R01 NS33291/NS/NINDS NIH HHS/ -- R01 NS36761/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2498-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anesthesiology, University of Alabama at Birmingham, Birmingham, AL 35233, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617463" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/drug therapy/*enzymology/genetics/pathology ; Animals ; *Apoptosis ; Brain-Derived Neurotrophic Factor/pharmacology ; Cells, Cultured ; Chelating Agents/pharmacology ; Copper/metabolism ; Fluoresceins/metabolism ; Liposomes ; Motor Neurons/*cytology/metabolism ; Mutation ; Nitrates/metabolism ; Nitric Oxide/*metabolism ; Nitric Oxide Synthase/antagonists & inhibitors/metabolism ; Nitric Oxide Synthase Type I ; Oxidation-Reduction ; Rats ; Superoxide Dismutase/chemistry/genetics/*metabolism/toxicity ; Superoxides/metabolism ; Zinc/*metabolism
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-01-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Plotkin, S A -- Koprowski, H -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2450.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10636806" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Democratic Republic of the Congo ; History, 20th Century ; Humans ; Immunization Programs/history ; Pan troglodytes ; Poliovirus/growth & development ; Poliovirus Vaccine, Oral/*history ; Virus Cultivation
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 2000 Apr 28;288(5466):586-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10798984" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics ; Animals ; Bioethics ; Cattle/*genetics ; *Cell Aging/genetics ; Cell Division ; Cells, Cultured ; *Cloning, Organism ; Female ; Nuclear Transfer Techniques ; Oocytes/physiology ; Stem Cells ; Telomere/*ultrastructure
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-03-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 2000 Feb 25;287(5457):1418-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10722390" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animal Experimentation ; Animals ; Bioethics ; *Biomedical Research ; Bone Marrow Cells/cytology/physiology ; Cell Differentiation ; Cell Separation ; Cell Transplantation ; Cells, Cultured ; Child ; *Embryo Research ; Embryo, Mammalian/*cytology ; Federal Government ; Humans ; Mice ; Middle Aged ; Stem Cells/*cytology/physiology
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  • 14
    Publication Date: 2000-04-28
    Description: The potential of cloning depends in part on whether the procedure can reverse cellular aging and restore somatic cells to a phenotypically youthful state. Here, we report the birth of six healthy cloned calves derived from populations of senescent donor somatic cells. Nuclear transfer extended the replicative life-span of senescent cells (zero to four population doublings remaining) to greater than 90 population doublings. Early population doubling level complementary DNA-1 (EPC-1, an age-dependent gene) expression in cells from the cloned animals was 3.5- to 5-fold higher than that in cells from age-matched (5 to 10 months old) controls. Southern blot and flow cytometric analyses indicated that the telomeres were also extended beyond those of newborn (〈2 weeks old) and age-matched control animals. The ability to regenerate animals and cells may have important implications for medicine and the study of mammalian aging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanza, R P -- Cibelli, J B -- Blackwell, C -- Cristofalo, V J -- Francis, M K -- Baerlocher, G M -- Mak, J -- Schertzer, M -- Chavez, E A -- Sawyer, N -- Lansdorp, P M -- West, M D -- AG00378/AG/NIA NIH HHS/ -- AI29524/AI/NIAID NIH HHS/ -- GM56162/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 28;288(5466):665-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Advanced Cell Technology, One Innovation Drive, Worcester, MA 01605, USA. rlanza@advancedcell.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10784448" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blotting, Southern ; Cattle/*genetics ; *Cell Aging ; Cell Division ; Cells, Cultured ; Clone Cells ; *Cloning, Organism ; DNA, Complementary ; Embryo Transfer ; *Eye Proteins ; Female ; Fibroblasts ; Flow Cytometry ; In Situ Hybridization, Fluorescence ; Longevity ; Matched-Pair Analysis ; *Nerve Growth Factors ; *Nuclear Transfer Techniques ; Proteins/genetics ; RNA, Messenger/genetics/metabolism ; Serpins/genetics ; Telomere/*ultrastructure
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  • 15
    Publication Date: 2000-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williamson, T L -- Corson, L B -- Huang, L -- Burlingame, A -- Liu, J -- Bruijn, L I -- Cleveland, D W -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):399.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, University of California at San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10798964" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*enzymology/genetics/pathology ; Animals ; Apoptosis ; Cells, Cultured ; Copper/metabolism ; Humans ; Mice ; Motor Neurons/metabolism/*pathology ; Mutation ; Neurofilament Proteins/metabolism ; Nitrates/metabolism ; Superoxide Dismutase/*genetics/*metabolism ; Yeasts/cytology/metabolism ; Zinc/*metabolism/toxicity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-03-24
    Description: Sensory axons become functional late in development when Schwann cells (SC) stop proliferating and differentiate into distinct phenotypes. We report that impulse activity in premyelinated axons can inhibit proliferation and differentiation of SCs. This neuron-glial signaling is mediated by adenosine triphosphate acting through P2 receptors on SCs and intracellular signaling pathways involving Ca2+, Ca2+/calmodulin kinase, mitogen-activated protein kinase, cyclic adenosine 3',5'-monophosphate response element binding protein, and expression of c-fos and Krox-24. Adenosine triphosphate arrests maturation of SCs in an immature morphological stage and prevents expression of O4, myelin basic protein, and the formation of myelin. Through this mechanism, functional activity in the developing nervous system could delay terminal differentiation of SCs until exposure to appropriate axon-derived signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, B -- Fields, R D -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2267-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Neurobiology, National Institutes of Health, National Institute of Child Health and Human Development, Building 49, Room 5A38, 49 Convent Drive, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10731149" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Adenosine Triphosphate/metabolism ; Animals ; Axons/*physiology ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Differentiation ; Cell Division ; Cells, Cultured ; Coculture Techniques ; Cyclic AMP Response Element-Binding Protein/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Early Growth Response Protein 1 ; Electric Stimulation ; Ganglia, Spinal/physiology ; Gene Expression Regulation, Developmental ; Genes, fos ; *Immediate-Early Proteins ; Mice ; Microscopy, Confocal ; Myelin Sheath/metabolism ; Neurons, Afferent/*physiology ; Phosphorylation ; Proto-Oncogene Proteins c-fos/metabolism ; Receptors, Purinergic P2/metabolism ; Schwann Cells/*cytology/*physiology ; Signal Transduction ; Transcription Factors/genetics/metabolism
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  • 17
    Publication Date: 2000-08-19
    Description: To gain a molecular understanding of tumor angiogenesis, we compared gene expression patterns of endothelial cells derived from blood vessels of normal and malignant colorectal tissues. Of over 170 transcripts predominantly expressed in the endothelium, 79 were differentially expressed, including 46 that were specifically elevated in tumor-associated endothelium. Several of these genes encode extracellular matrix proteins, but most are of unknown function. Most of these tumor endothelial markers were expressed in a wide range of tumor types, as well as in normal vessels associated with wound healing and corpus luteum formation. These studies demonstrate that tumor and normal endothelium are distinct at the molecular level, a finding that may have significant implications for the development of anti-angiogenic therapies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St Croix, B -- Rago, C -- Velculescu, V -- Traverso, G -- Romans, K E -- Montgomery, E -- Lal, A -- Riggins, G J -- Lengauer, C -- Vogelstein, B -- Kinzler, K W -- CA57345/CA/NCI NIH HHS/ -- CA62924/CA/NCI NIH HHS/ -- CGAP S98-146A/PHS HHS/ -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1197-202.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Oncology Center, Howard Hughes Medical Institute, Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10947988" target="_blank"〉PubMed〈/a〉
    Keywords: Biomarkers, Tumor ; Cell Separation ; Cells, Cultured ; Colon/*blood supply/metabolism ; Colorectal Neoplasms/*blood supply/genetics/metabolism/pathology ; Corpus Luteum/blood supply/metabolism ; Endothelium, Vascular/cytology/*metabolism/pathology ; Extracellular Matrix Proteins/genetics ; Female ; Gene Expression ; *Gene Expression Profiling ; Humans ; Intestinal Mucosa/blood supply/cytology/pathology ; Neoplasms/blood supply/genetics/metabolism ; Neovascularization, Pathologic/*genetics ; Neovascularization, Physiologic/genetics ; RNA, Messenger/genetics/metabolism ; Rectum/*blood supply/metabolism ; Tumor Cells, Cultured
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  • 18
    Publication Date: 2000-04-15
    Description: The capsaicin (vanilloid) receptor VR1 is a cation channel expressed by primary sensory neurons of the "pain" pathway. Heterologously expressed VR1 can be activated by vanilloid compounds, protons, or heat (〉43 degrees C), but whether this channel contributes to chemical or thermal sensitivity in vivo is not known. Here, we demonstrate that sensory neurons from mice lacking VR1 are severely deficient in their responses to each of these noxious stimuli. VR1-/- mice showed normal responses to noxious mechanical stimuli but exhibited no vanilloid-evoked pain behavior, were impaired in the detection of painful heat, and showed little thermal hypersensitivity in the setting of inflammation. Thus, VR1 is essential for selective modalities of pain sensation and for tissue injury-induced thermal hyperalgesia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caterina, M J -- Leffler, A -- Malmberg, A B -- Martin, W J -- Trafton, J -- Petersen-Zeitz, K R -- Koltzenburg, M -- Basbaum, A I -- Julius, D -- NS07265/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 14;288(5464):306-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94143-0450, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10764638" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Temperature/drug effects ; Calcium/metabolism ; Capsaicin/metabolism/*pharmacology ; Cells, Cultured ; Diterpenes/pharmacology ; Ganglia, Spinal/cytology ; Gene Targeting ; Hot Temperature ; Hydrogen-Ion Concentration ; Inflammation/physiopathology ; Mice ; Mice, Knockout ; Nerve Fibers/physiology ; Neurons/physiology ; Neurons, Afferent/*physiology ; Nociceptors/*physiology ; Pain/*physiopathology ; Pain Threshold ; Receptors, Drug/*physiology ; Spinal Cord/cytology/physiology ; TRPV Cation Channels
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-02-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 2000 Jan 14;287(5451):202-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10660414" target="_blank"〉PubMed〈/a〉
    Keywords: *Aborted Fetus ; *Abortion, Induced ; Academic Medical Centers ; Cells, Cultured ; Ethical Review ; Ethics Committees, Research ; *Fetal Research ; *Fetus/cytology ; Humans ; Nebraska ; *Neurosciences ; Politics ; *Research
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-09-08
    Description: During animal development, cells become progressively more restricted in the cell types to which they can give rise. In the central nervous system (CNS), for example, multipotential stem cells produce various kinds of specified precursors that divide a limited number of times before they terminally differentiate into either neurons or glial cells. We show here that certain extracellular signals can induce oligodendrocyte precursor cells to revert to multipotential neural stem cells, which can self-renew and give rise to neurons and astrocytes, as well as to oligodendrocytes. Thus, these precursor cells have greater developmental potential than previously thought.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kondo, T -- Raff, M -- New York, N.Y. -- Science. 2000 Sep 8;289(5485):1754-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Developmental Neurobiology Programme, MRC Laboratory for Molecular Cell Biology and the Biology Department, University College London, London WC1E 6BT, UK. t.kondo@ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10976069" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Astrocytes/chemistry/*cytology ; Blood ; Bone Morphogenetic Proteins/pharmacology ; Cell Culture Techniques ; *Cell Differentiation ; Cells, Cultured ; Culture Media ; Culture Media, Serum-Free ; Fibroblast Growth Factor 2/pharmacology ; Galactosylceramides/analysis ; Glial Fibrillary Acidic Protein/analysis ; Glutamate Decarboxylase/biosynthesis/genetics ; Isoenzymes/biosynthesis/genetics ; Neurofilament Proteins/analysis/biosynthesis ; Neurons/chemistry/*cytology ; Oligodendroglia/chemistry/*cytology ; Optic Nerve/cytology ; Platelet-Derived Growth Factor/pharmacology ; Rats ; Stem Cells/chemistry/*cytology ; Thyroid Hormones/pharmacology
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  • 21
    Publication Date: 2000-09-29
    Description: A20 is a cytoplasmic zinc finger protein that inhibits nuclear factor kappaB (NF-kappaB) activity and tumor necrosis factor (TNF)-mediated programmed cell death (PCD). TNF dramatically increases A20 messenger RNA expression in all tissues. Mice deficient for A20 develop severe inflammation and cachexia, are hypersensitive to both lipopolysaccharide and TNF, and die prematurely. A20-deficient cells fail to terminate TNF-induced NF-kappaB responses. These cells are also more susceptible than control cells to undergo TNF-mediated PCD. Thus, A20 is critical for limiting inflammation by terminating TNF-induced NF-kappaB responses in vivo.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3582399/" 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/PMC3582399/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, E G -- Boone, D L -- Chai, S -- Libby, S L -- Chien, M -- Lodolce, J P -- Ma, A -- 5T32GM07183/GM/NIGMS NIH HHS/ -- R01 DK052751/DK/NIDDK NIH HHS/ -- T32GM07839/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 29;289(5488):2350-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, The University of Chicago, 5841 South Maryland Avenue, MC 6084, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11009421" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cachexia/pathology/physiopathology ; Cells, Cultured ; Cysteine Endopeptidases ; DNA/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Fibroblasts/metabolism ; Gene Targeting ; *I-kappa B Proteins ; Inflammation/pathology/*physiopathology ; Interleukin-1/pharmacology ; Intestines/pathology ; Intracellular Signaling Peptides and Proteins ; Kidney/pathology ; Lipopolysaccharides/immunology ; Liver/pathology ; Mice ; NF-kappa B/*metabolism ; Nuclear Proteins ; Phosphorylation ; Proteins/genetics/*physiology ; Skin/pathology ; T-Lymphocytes/cytology/metabolism ; Tumor Necrosis Factor-alpha/*pharmacology ; Zinc Fingers
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  • 22
    Publication Date: 2000-05-08
    Description: To determine why proteasome inhibitors prevent thymocyte death, we examined whether proteasomes degrade anti-apoptotic molecules in cells induced to undergo apoptosis. The c-IAP1 and XIAP inhibitors of apoptosis were selectively lost in glucocorticoid- or etoposide-treated thymocytes in a proteasome-dependent manner before death. IAPs catalyzed their own ubiquitination in vitro, an activity requiring the RING domain. Overexpressed wild-type c-IAP1, but not a RING domain mutant, was spontaneously ubiquitinated and degraded, and stably expressed XIAP lacking the RING domain was relatively resistant to apoptosis-induced degradation and, correspondingly, more effective at preventing apoptosis than wild-type XIAP. Autoubiquitination and degradation of IAPs may be a key event in the apoptotic program.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Y -- Fang, S -- Jensen, J P -- Weissman, A M -- Ashwell, J D -- New York, N.Y. -- Science. 2000 May 5;288(5467):874-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immune Cell Biology, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10797013" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cells, Cultured ; Cysteine Endopeptidases/*metabolism ; Dexamethasone/pharmacology ; Etoposide/pharmacology ; Hybridomas ; Inhibitor of Apoptosis Proteins ; Ligases/*metabolism ; Mice ; Mice, Inbred C57BL ; Multienzyme Complexes/*metabolism ; Proteasome Endopeptidase Complex ; Protein Structure, Tertiary ; Proteins/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes/cytology/drug effects/*metabolism ; Thymus Gland/cytology ; Transfection ; Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; X-Linked Inhibitor of Apoptosis Protein
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  • 23
    Publication Date: 2000-03-31
    Description: Brucella abortus, a mammalian pathogen, and Rhizobium meliloti, a phylogenetically related plant symbiont, establish chronic infections in their respective hosts. Here a highly conserved B. abortus homolog of the R. meliloti bacA gene, which encodes a putative cytoplasmic membrane transport protein required for symbiosis, was identified. An isogenic B. abortus bacA mutant exhibited decreased survival in macrophages and greatly accelerated clearance from experimentally infected mice compared to the virulent parental strain. Thus, the bacA gene product is critical for the maintenance of two very diverse host-bacterial relationships.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LeVier, K -- Phillips, R W -- Grippe, V K -- Roop, R M 2nd -- Walker, G C -- GM31030/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 31;287(5462):2492-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10741969" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Bacterial/immunology ; Bacterial Proteins/genetics/*physiology ; Brucella abortus/genetics/*pathogenicity/physiology ; Brucellosis/immunology/*microbiology ; Cells, Cultured ; Female ; Hypersensitivity, Delayed ; Liver/microbiology ; Macrophages/immunology/*microbiology ; Medicago sativa/microbiology ; Membrane Proteins/genetics/*physiology ; *Membrane Transport Proteins ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutagenesis, Insertional ; Sinorhizobium meliloti/genetics/*physiology ; Spleen/microbiology ; Symbiosis ; Virulence
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  • 24
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-08-12
    Description: In work reported on page 452, researchers have found a way to coax certain introns, bits of genetic debris that litter the DNA and interrupt the coding sequences of many genes, to hop into the exact sequences where the researchers want them. The method could enhance all sorts of genetic manipulations, from studying basic gene function to combating viral infections to delivering genes for gene therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strauss, E -- New York, N.Y. -- Science. 2000 Jul 21;289(5478):374.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10939940" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; DNA/*genetics/metabolism ; *Gene Targeting ; *Gene Transfer Techniques ; Genes, Viral ; Genetic Engineering ; Genetic Therapy ; HIV/genetics ; Humans ; *Introns ; Receptors, CCR5/genetics
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  • 25
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-02-26
    Description: The debate on the use of human embryos for research will be one of the more important issues of the 21st century. Unlike recombinant DNA technology, embryonic stem cell research most probably will result in the destruction of living embryos. Many people consider this research immoral, illegal, and unnecessary. Therefore, it is imperative to proceed cautiously. Federal funding of research using human embryos or pluripotent cells derived from them would be inappropriate until further resolution of the ethical issues has been achieved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, F E -- New York, N.Y. -- Science. 2000 Feb 25;287(5457):1424.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Reformed Theological Seminary, Fourth Presbyterian Church, 5500 River Road, Bethesda, MD 20816-3399, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10688779" target="_blank"〉PubMed〈/a〉
    Keywords: *Bioethics ; Biomedical Research ; Cells, Cultured ; *Embryo Research ; Embryo, Mammalian/*cytology ; Government Regulation ; Guidelines as Topic ; Humans ; National Institutes of Health (U.S.) ; Public Policy ; *Research Support as Topic ; Risk Assessment ; *Stem Cells ; United States ; Value of Life
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  • 26
    Publication Date: 2000-06-24
    Description: T helper 1 (TH1) cells mediate cellular immunity, whereas TH2 cells potentiate antiparasite and humoral immunity. We used a complementary DNA subtraction method, representational display analysis, to show that the small guanosine triphosphatase Rac2 is expressed selectively in murine TH1 cells. Rac induces the interferon-gamma (IFN-gamma) promoter through cooperative activation of the nuclear factor kappa B and p38 mitogen-activated protein kinase pathways. Tetracycline-regulated transgenic mice expressing constitutively active Rac2 in T cells exhibited enhanced IFN-gamma production. Dominant-negative Rac inhibited IFN-gamma production in murine T cells. Moreover, T cells from Rac2-/- mice showed decreased IFN-gamma production under TH1 conditions in vitro. Thus, Rac2 activates TH1-specific signaling and IFN-gamma gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, B -- Yu, H -- Zheng, W -- Voll, R -- Na, S -- Roberts, A W -- Williams, D A -- Davis, R J -- Ghosh, S -- Flavell, R A -- New York, N.Y. -- Science. 2000 Jun 23;288(5474):2219-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology and Howard Hughes Medical Institute, Yale University School of Medicine, 310 Cedar Street, New Haven, CT 06520-8011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10864872" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cells, Cultured ; Cytokines/biosynthesis/genetics ; Gene Expression Regulation ; Humans ; Interferon-gamma/biosynthesis/*genetics ; JNK Mitogen-Activated Protein Kinases ; Jurkat Cells ; Lymphocyte Activation ; Mice ; Mice, Transgenic ; Mitogen-Activated Protein Kinases/metabolism ; NF-kappa B/metabolism ; Promoter Regions, Genetic ; Signal Transduction ; Th1 Cells/cytology/*immunology/*metabolism ; Transfection ; p38 Mitogen-Activated Protein Kinases ; rac GTP-Binding Proteins/genetics/*metabolism
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  • 27
    Publication Date: 2000-06-02
    Description: The differentiation potential of stem cells in tissues of the adult has been thought to be limited to cell lineages present in the organ from which they were derived, but there is evidence that some stem cells may have a broader differentiation repertoire. We show here that neural stem cells from the adult mouse brain can contribute to the formation of chimeric chick and mouse embryos and give rise to cells of all germ layers. This demonstrates that an adult neural stem cell has a very broad developmental capacity and may potentially be used to generate a variety of cell types for transplantation in different diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clarke, D L -- Johansson, C B -- Wilbertz, J -- Veress, B -- Nilsson, E -- Karlstrom, H -- Lendahl, U -- Frisen, J -- New York, N.Y. -- Science. 2000 Jun 2;288(5471):1660-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Biology, Medical Nobel Institute, Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10834848" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/cytology/physiology ; Brain/*cytology ; Cell Aggregation ; *Cell Differentiation ; Cell Lineage ; Cells, Cultured ; Chick Embryo ; Coculture Techniques ; Ectoderm/cytology ; Embryonic and Fetal Development ; Endoderm/cytology ; Liver/cytology/embryology ; Mesoderm/cytology ; Mice ; Microinjections ; Morula/cytology/physiology ; Muscles/cytology/embryology ; Stem Cell Transplantation ; Stem Cells/*cytology/physiology ; Transplantation Chimera
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  • 28
    Publication Date: 2000-07-06
    Description: Definition of cellular responses to cytokines often involves cross-communication through their respective receptors. Here, signaling by interferon-gamma (IFN-gamma) is shown to depend on the IFN-alpha/beta receptor components. Although these IFNs transmit signals through distinct receptor complexes, the IFN-alpha/beta receptor component, IFNAR1, facilitates efficient assembly of IFN-gamma-activated transcription factors. This cross talk is contingent on a constitutive subthreshold IFN-alpha/beta signaling and the association between the two nonligand-binding receptor components, IFNAR1 and IFNGR2, in the caveolar membrane domains. This aspect of signaling cross talk by IFNs may apply to other cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takaoka, A -- Mitani, Y -- Suemori, H -- Sato, M -- Yokochi, T -- Noguchi, S -- Tanaka, N -- Taniguchi, T -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2357-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Graduate School of Medicine and Faculty of Medicine, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875919" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/*metabolism ; Cells, Cultured ; Cytopathogenic Effect, Viral ; DNA-Binding Proteins/metabolism ; Dimerization ; Encephalomyocarditis virus/drug effects/physiology ; Interferon Type I/*metabolism ; Interferon-alpha/genetics/metabolism/pharmacology ; Interferon-beta/genetics/metabolism/pharmacology ; Interferon-gamma/*metabolism/pharmacology ; Janus Kinase 1 ; Janus Kinase 2 ; Membrane Proteins ; Mice ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/metabolism ; *Proto-Oncogene Proteins ; *Receptor Cross-Talk ; Receptor, Interferon alpha-beta ; Receptors, Interferon/genetics/*metabolism ; Recombinant Proteins ; STAT1 Transcription Factor ; *Signal Transduction ; Trans-Activators/metabolism
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  • 29
    Publication Date: 2000-10-06
    Description: Rearrangements involving the RET gene are common in radiation-associated papillary thyroid cancer (PTC). The RET/PTC1 type of rearrangement is an inversion of chromosome 10 mediated by illegitimate recombination between the RET and the H4 genes, which are 30 megabases apart. Here we ask whether despite the great linear distance between them, RET and H4 recombination might be promoted by their proximity in the nucleus. We used two-color fluorescence in situ hybridization and three-dimensional microscopy to map the positions of the RET and H4 loci within interphase nuclei. At least one pair of RET and H4 was juxtaposed in 35% of normal human thyroid cells and in 21% of peripheral blood lymphocytes, but only in 6% of normal mammary epithelial cells. Spatial contiguity of RET and H4 may provide a structural basis for generation of RET/PTC1 rearrangement by allowing a single radiation track to produce a double-strand break in each gene at the same site in the nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nikiforova, M N -- Stringer, J R -- Blough, R -- Medvedovic, M -- Fagin, J A -- Nikiforov, Y E -- CA 72597/CA/NCI NIH HHS/ -- P01 ES 05652-10/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):138-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021799" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Breast/cytology ; Cells, Cultured ; Chromosome Inversion ; Chromosomes, Human, Pair 10/*genetics ; Cytoskeletal Proteins ; *Drosophila Proteins ; Epithelial Cells ; Gene Rearrangement ; Humans ; In Situ Hybridization, Fluorescence ; Interphase ; Lymphocytes ; Neoplasms, Radiation-Induced/genetics ; Oncogene Proteins, Fusion/*genetics ; Protein-Tyrosine Kinases ; Proteins/*genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-ret ; Receptor Protein-Tyrosine Kinases/*genetics ; *Recombination, Genetic ; Reverse Transcriptase Polymerase Chain Reaction ; Thyroid Gland/*cytology/*radiation effects ; Thyroid Neoplasms/genetics
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  • 30
    Publication Date: 2000-10-06
    Description: Genes that control the early stages of adipogenesis remain largely unknown. Here, we show that murine GATA-2 and GATA-3 are specifically expressed in white adipocyte precursors and that their down-regulation sets the stage for terminal differentiation. Constitutive GATA-2 and GATA-3 expression suppressed adipocyte differentiation and trapped cells at the preadipocyte stage. This effect is mediated, at least in part, through the direct suppression of peroxisome proliferator-activated receptor gamma. GATA-3-deficient embryonic stem cells exhibit an enhanced capacity to differentiate into adipocytes, and defective GATA-2 and GATA-3 expression is associated with obesity. Thus, GATA-2 and GATA-3 regulate adipocyte differentiation through molecular control of the preadipocyte-adipocyte transition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tong, Q -- Dalgin, G -- Xu, H -- Ting, C N -- Leiden, J M -- Hotamisligil, G S -- DK56894/DK/NIDDK NIH HHS/ -- F32DK09940/DK/NIDDK NIH HHS/ -- R37AI29673/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):134-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Sciences and Department of Nutrition, Harvard School of Public Health, 665 Huntington Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021798" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adipocytes/*cytology/*metabolism ; Adipose Tissue/cytology/metabolism ; Adipose Tissue, Brown/cytology/metabolism ; Animals ; Cell Differentiation ; Cells, Cultured ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; GATA2 Transcription Factor ; GATA3 Transcription Factor ; Gene Expression ; Mice ; Mutation ; Obesity/genetics/metabolism ; Promoter Regions, Genetic ; Receptors, Cytoplasmic and Nuclear/genetics/metabolism ; Stem Cells/cytology ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic ; Zinc Fingers
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  • 31
    Publication Date: 2000-03-17
    Description: The mature mammalian retina is thought to lack regenerative capacity. Here, we report the identification of a stem cell in the adult mouse eye, which represents a possible substrate for retinal regeneration. Single pigmented ciliary margin cells clonally proliferate in vitro to form sphere colonies of cells that can differentiate into retinal-specific cell types, including rod photoreceptors, bipolar neurons, and Muller glia. Adult retinal stem cells are localized to the pigmented ciliary margin and not to the central and peripheral retinal pigmented epithelium, indicating that these cells may be homologous to those found in the eye germinal zone of other nonmammalian vertebrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tropepe, V -- Coles, B L -- Chiasson, B J -- Horsford, D J -- Elia, A J -- McInnes, R R -- van der Kooy, D -- New York, N.Y. -- Science. 2000 Mar 17;287(5460):2032-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, University of Toronto, Medical Sciences Building 1105, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10720333" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Count ; Cell Differentiation ; Cell Division ; Cell Lineage ; Cell Size ; Cell Survival ; Cells, Cultured ; Clone Cells ; Colony-Forming Units Assay ; Fibroblast Growth Factor 2/pharmacology ; Homeodomain Proteins/biosynthesis ; Intermediate Filament Proteins/biosynthesis ; Mice ; *Nerve Tissue Proteins ; Nestin ; Neuroglia/cytology/metabolism ; Neurons/cytology/metabolism ; Pigment Epithelium of Eye/cytology/embryology ; Retina/*cytology/embryology/metabolism ; Retinal Rod Photoreceptor Cells/cytology/metabolism ; Stem Cells/*cytology/metabolism ; Transcription Factors/biosynthesis
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-06
    Description: Until now, neurobiologists have had little luck in finding the matchmakers of nerve cell connections, called synapses, in the brain. In today's issue of Cell, researchers report that a single protein can apparently trigger synapse formation between brain neurons isolated from mice and grown in culture. If the finding is borne out in living animals, it could provide fresh insights into how the brain is wired during embryonic development and might eventually provide new ways to enhance or at least maintain synapse formation in the brains of patients suffering from neurodegenerative diseases such as Parkinson's or Alzheimer's.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gura, T -- New York, N.Y. -- Science. 2000 Jun 9;288(5472):1718-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10877681" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology ; Cell Adhesion Molecules, Neuronal ; Cells, Cultured ; Membrane Proteins/analysis/genetics/*metabolism ; Mice ; Mice, Knockout ; Nerve Tissue Proteins/analysis/genetics/*metabolism ; Neurons/*physiology ; Synapses/*physiology ; Synaptic Membranes/chemistry
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gura, T -- New York, N.Y. -- Science. 2000 May 5;288(5467):786-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10809641" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/*pharmacology ; *Apoptosis ; Apoptosis Regulatory Proteins ; Cell Death ; Cells, Cultured ; Clinical Trials as Topic ; Culture Techniques ; Drug Screening Assays, Antitumor ; Humans ; Liver/cytology/*drug effects ; Liver Diseases/pathology ; Membrane Glycoproteins/*pharmacology ; Neoplasms/*drug therapy/pathology ; TNF-Related Apoptosis-Inducing Ligand ; Tumor Necrosis Factor-alpha/*pharmacology
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-03-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2000 Feb 25;287(5457):1421-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10722392" target="_blank"〉PubMed〈/a〉
    Keywords: *Aborted Fetus ; Animals ; Bioethics ; Biomedical Research ; Brain Diseases ; Brain Tissue Transplantation ; Cell Death ; Cell Differentiation ; Cells, Cultured ; Dopamine/biosynthesis ; Embryo, Mammalian/*cytology ; *Fetal Research ; *Fetal Tissue Transplantation ; Humans ; Neuroglia/cytology ; Neurons/*cytology/metabolism/*transplantation ; Parkinson Disease/*therapy ; *Stem Cell Transplantation ; Stem Cells/cytology ; Substantia Nigra/cytology/embryology ; Therapeutic Human Experimentation
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  • 35
    Publication Date: 2000-05-12
    Description: A critical function of tumor suppressor p53 is the induction of apoptosis in cells exposed to noxious stresses. We report a previously unidentified pro-apoptotic gene, Noxa. Expression of Noxa induction in primary mouse cells exposed to x-ray irradiation was dependent on p53. Noxa encodes a Bcl-2 homology 3 (BH3)-only member of the Bcl-2 family of proteins; this member contains the BH3 region but not other BH domains. When ectopically expressed, Noxa underwent BH3 motif-dependent localization to mitochondria and interacted with anti-apoptotic Bcl-2 family members, resulting in the activation of caspase-9. We also demonstrate that blocking the endogenous Noxa induction results in the suppression of apoptosis. Noxa may thus represent a mediator of p53-dependent apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oda, E -- Ohki, R -- Murasawa, H -- Nemoto, J -- Shibue, T -- Yamashita, T -- Tokino, T -- Taniguchi, T -- Tanaka, N -- New York, N.Y. -- Science. 2000 May 12;288(5468):1053-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Graduate School of Medicine and Faculty of Medicine, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10807576" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; *Apoptosis ; Caspase 9 ; Caspases/metabolism ; Cell Line ; Cells, Cultured ; DNA Damage ; Enzyme Activation ; Gene Expression Profiling ; Gene Expression Regulation ; Humans ; Mice ; Mitochondria/metabolism ; Molecular Sequence Data ; Promoter Regions, Genetic ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-bcl-2/chemistry/*physiology/*secretion ; RNA, Messenger/genetics/metabolism ; T-Lymphocytes/metabolism ; Tumor Suppressor Protein p53/*physiology ; bcl-2-Associated X Protein
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  • 36
    Publication Date: 2000-01-29
    Description: Malfolded proteins in the endoplasmic reticulum (ER) induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs). Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and IRE1alpha-/- fibroblasts were impaired in JNK activation by ER stress. The cytoplasmic part of IRE1 bound TRAF2, an adaptor protein that couples plasma membrane receptors to JNK activation. Dominant-negative TRAF2 inhibited activation of JNK by IRE1. Activation of JNK by endogenous signals initiated in the ER proceeds by a pathway similar to that initiated by cell surface receptors in response to extracellular signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Urano, F -- Wang, X -- Bertolotti, A -- Zhang, Y -- Chung, P -- Harding, H P -- Ron, D -- DK47119/DK/NIDDK NIH HHS/ -- ES08681/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 28;287(5453):664-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Skirball Institute of Biomolecular Medicine, Departments of Medicine, Cell Biology and the Kaplan Cancer Center, New York University Medical School, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10650002" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Endoplasmic Reticulum/*metabolism ; Endoribonucleases/genetics/*metabolism ; Enzyme Activation ; Gene Targeting ; Humans ; JNK Mitogen-Activated Protein Kinases ; *Membrane Proteins ; Mitogen-Activated Protein Kinases/*metabolism ; Multienzyme Complexes/genetics/*metabolism ; Protein Kinases/genetics/*metabolism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Proteins/chemistry/genetics/*metabolism ; Rats ; Recombinant Fusion Proteins/metabolism ; TNF Receptor-Associated Factor 2 ; Thapsigargin/pharmacology ; Two-Hybrid System Techniques ; eIF-2 Kinase/metabolism
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-05-12
    Description: Influenza B virus is a human pathogen whose origin and possible reservoir in nature are not known. An influenza B virus was isolated from a naturally infected harbor seal (Phoca vitulina) and was found to be infectious to seal kidney cells in vitro. Sequence analyses and serology indicated that influenza virus B/Seal/Netherlands/1/99 is closely related to strains that circulated in humans 4 to 5 years earlier. Retrospective analyses of sera collected from 971 seals showed a prevalence of antibodies to influenza B virus in 2% of the animals after 1995 and in none before 1995. This animal reservoir, harboring influenza B viruses that have circulated in the past, may pose a direct threat to humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Osterhaus, A D -- Rimmelzwaan, G F -- Martina, B E -- Bestebroer, T M -- Fouchier, R A -- HD 15527/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2000 May 12;288(5468):1051-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Influenza Center, Department of Virology, Erasmus University, Doctor Molewaterplein 50, 3015 GE Rotterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10807575" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral/blood ; Cell Line ; Cells, Cultured ; Disease Reservoirs ; Dogs ; Enzyme-Linked Immunosorbent Assay ; Genes, Viral ; Hemagglutination Inhibition Tests ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Humans ; Influenza B virus/classification/genetics/immunology/*isolation & purification ; Neutralization Tests ; Orthomyxoviridae Infections/epidemiology/*veterinary/virology ; Pharynx/virology ; Reverse Transcriptase Polymerase Chain Reaction ; Seals, Earless/*virology ; Viral Nonstructural Proteins/genetics ; Virus Shedding
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-08-26
    Description: Contact-mediated axon repulsion by ephrins raises an unresolved question: these cell surface ligands form a high-affinity multivalent complex with their receptors present on axons, yet rather than being bound, axons can be rapidly repelled. We show here that ephrin-A2 forms a stable complex with the metalloprotease Kuzbanian, involving interactions outside the cleavage region and the protease domain. Eph receptor binding triggered ephrin-A2 cleavage in a localized reaction specific to the cognate ligand. A cleavage-inhibiting mutation in ephrin-A2 delayed axon withdrawal. These studies reveal mechanisms for protease recognition and control of cell surface proteins, and, for ephrin-A2, they may provide a means for efficient axon detachment and termination of signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hattori, M -- Osterfield, M -- Flanagan, J G -- EY11559/EY/NEI NIH HHS/ -- HD29417/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1360-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Program in Neuroscience, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958785" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Axons/*physiology ; Cell Adhesion ; Cell Communication ; Cell Membrane/metabolism ; Cells, Cultured ; Disintegrins/genetics/*metabolism ; *Drosophila Proteins ; Ephrin-A2 ; Gene Expression ; Glycosylphosphatidylinositols/metabolism ; Growth Cones/physiology ; Humans ; Ligands ; Metalloendopeptidases/genetics/*metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Nervous System/embryology/enzymology ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, EphA3 ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription Factors/chemistry/genetics/*metabolism ; Tumor Cells, Cultured
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-09-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 2000 Sep 8;289(5485):1666.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11001723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Blood ; Cell Culture Techniques ; *Cell Differentiation ; Cells, Cultured ; Culture Media ; Fibroblast Growth Factors/pharmacology ; Neurons/*cytology ; Oligodendroglia/*cytology ; Rats ; Stem Cells/*cytology
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-06-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 2000 Jun 2;288(5471):1559-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10858126" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Cells/cytology ; Brain/*cytology ; Cell Aggregation ; *Cell Differentiation ; Cells, Cultured ; Chick Embryo ; Embryo, Mammalian ; Mice ; Organ Specificity ; Stem Cell Transplantation ; Stem Cells/*cytology/physiology
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  • 41
    Publication Date: 2000-07-15
    Description: p53 plays an essential pro-apoptotic role, a function thought to be shared with its family members p73 and p63. Here, we show that p73 is primarily present in developing neurons as a truncated isoform whose levels are dramatically decreased when sympathetic neurons apoptose after nerve growth factor (NGF) withdrawal. Increased expression of truncated p73 rescues these neurons from apoptosis induced by NGF withdrawal or p53 overexpression. In p73-/- mice, all isoforms of p73 are deleted and the apoptosis of developing sympathetic neurons is greatly enhanced. Thus, truncated p73 is an essential anti-apoptotic protein in neurons, serving to counteract the pro-apoptotic function of p53.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pozniak, C D -- Radinovic, S -- Yang, A -- McKeon, F -- Kaplan, D R -- Miller, F D -- New York, N.Y. -- Science. 2000 Jul 14;289(5477):304-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neuronal Survival, Brain Tumor Research Center, Montreal Neurological Institute, McGill University, Montreal, Canada H3A 2B4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10894779" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Animals ; Apoptosis/*physiology ; Cells, Cultured ; DNA-Binding Proteins/biosynthesis/chemistry/*physiology ; Escherichia coli ; Genes, Tumor Suppressor ; Humans ; Mice ; Mice, Inbred BALB C ; Nerve Growth Factor/pharmacology ; Neurons/*physiology ; Nuclear Proteins/biosynthesis/chemistry/*physiology ; Protein Isoforms/biosynthesis/chemistry/physiology ; Recombinant Proteins ; Sympathetic Nervous System/cytology/*physiology ; Tumor Suppressor Protein p53/antagonists & inhibitors/*physiology ; Tumor Suppressor Proteins
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-08-12
    Description: When researchers in Edmonton, Canada, announced last month that a new procedure for transplanting pancreatic islet cells had freed seven adults with type I diabetes from taking insulin, the results generated a great deal of public enthusiasm. Some important caveats tended to get lost, however. One drawback is that transplant recipients would need to take immunosuppressive drugs for the rest of their lives to keep from rejecting the tissue. But more importantly, even if the benefits of the transplants outweigh the risks of the drugs, there's just not enough islet tissue to go around and there won't be anytime soon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwillich, T -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):531-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10939961" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Glucose/metabolism ; Cell Culture Techniques ; Cell Division ; Cells, Cultured ; Diabetes Mellitus, Type 1/*surgery ; Embryo, Mammalian ; Graft Rejection/prevention & control ; Humans ; Immunosuppressive Agents/therapeutic use ; Insulin/biosynthesis ; Islets of Langerhans/*cytology/metabolism ; *Islets of Langerhans Transplantation ; Mice ; Stem Cells/cytology ; Tissue Donors
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  • 43
    Publication Date: 2000-10-06
    Description: Benzodiazepine tranquilizers are used in the treatment of anxiety disorders. To identify the molecular and neuronal target mediating the anxiolytic action of benzodiazepines, we generated and analyzed two mouse lines in which the alpha2 or alpha3 GABAA (gamma-aminobutyric acid type A) receptors, respectively, were rendered insensitive to diazepam by a knock-in point mutation. The anxiolytic action of diazepam was absent in mice with the alpha2(H101R) point mutation but present in mice with the alpha3(H126R) point mutation. These findings indicate that the anxiolytic effect of benzodiazepine drugs is mediated by alpha2 GABAA receptors, which are largely expressed in the limbic system, but not by alpha3 GABAA receptors, which predominate in the reticular activating system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Low, K -- Crestani, F -- Keist, R -- Benke, D -- Brunig, I -- Benson, J A -- Fritschy, J M -- Rulicke, T -- Bluethmann, H -- Mohler, H -- Rudolph, U -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):131-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Pharmacology and Toxicology, University of Zurich, and Swiss Federal Institute of Technology Zurich (ETH), Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Anxiety Agents/metabolism/*pharmacology ; Behavior, Animal/drug effects ; Binding Sites ; Brain/drug effects/metabolism ; Cells, Cultured ; Diazepam/metabolism/*pharmacology ; Dose-Response Relationship, Drug ; Female ; Gene Targeting ; Hippocampus/cytology ; Membrane Potentials/drug effects ; Mice ; Patch-Clamp Techniques ; Phenobarbital/pharmacology ; Point Mutation ; Pyramidal Cells/drug effects/physiology ; Receptors, GABA-A/chemistry/genetics/*metabolism ; Synaptic Transmission ; gamma-Aminobutyric Acid/pharmacology
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  • 44
    Publication Date: 2000-12-23
    Description: Niemann-Pick type C2 disease (NP-C2) is a fatal hereditary disorder of unknown etiology characterized by defective egress of cholesterol from lysosomes. Here we show that the disease is caused by a deficiency in HE1, a ubiquitously expressed lysosomal protein identified previously as a cholesterol-binding protein. HE1 was undetectable in fibroblasts from NP-C2 patients but present in fibroblasts from unaffected controls and NP-C1 patients. Mutations in the HE1 gene, which maps to chromosome 14q24.3, were found in NP-C2 patients but not in controls. Treatment of NP-C2 fibroblasts with exogenous recombinant HE1 protein ameliorated lysosomal accumulation of low density lipoprotein-derived cholesterol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naureckiene, S -- Sleat, D E -- Lackland, H -- Fensom, A -- Vanier, M T -- Wattiaux, R -- Jadot, M -- Lobel, P -- DK45992/DK/NIDDK NIH HHS/ -- DK54317/DK/NIDDK NIH HHS/ -- NS37918/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 22;290(5500):2298-301.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, NJ, 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11125141" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; CHO Cells ; *Carrier Proteins ; Cell Membrane/metabolism ; Cells, Cultured ; Cholesterol/*metabolism ; Cricetinae ; Culture Media, Conditioned ; Fibroblasts/metabolism ; Glycoproteins/chemistry/*genetics/*metabolism/pharmacology ; Humans ; Lysosomes/*metabolism ; Molecular Sequence Data ; Mutation ; Niemann-Pick Diseases/*genetics/metabolism ; Rats ; Receptor, IGF Type 2/metabolism ; Recombinant Proteins/metabolism/pharmacology ; Transfection
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 45
    Publication Date: 2000-12-23
    Description: Niemann-Pick C1 (NPC1) disease is characterized by cholesterol accumulation in lysosomes and aberrant feedback regulation of cellular cholesterol homeostasis. We provide evidence that the NPC1 protein has homology with the resistance-nodulation-division (RND) family of prokaryotic permeases and may normally function as a transmembrane efflux pump. Studies of acriflavine loading in normal and NPC1 fibroblasts indicated that NPC1 uses a proton motive force to remove accumulated acriflavine from the endosomal/lysosomal system. Expression of NPC1 in Escherichia coli (i) facilitated the transport of acriflavine across the plasma membrane, causing cytosolic accumulation, and (ii) resulted in transport of oleic acid but not cholesterol or cholesterol-oleate across the plasma membrane. These studies establish NPC1 as a eukaryotic member of the RND permease family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davies, J P -- Chen, F W -- Ioannou, Y A -- R01 DK54736/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 22;290(5500):2295-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Box 1498, The Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11125140" target="_blank"〉PubMed〈/a〉
    Keywords: Acriflavine/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Biological Transport ; *Carrier Proteins ; Cell Membrane/metabolism ; Cells, Cultured ; Cholesterol/metabolism ; Cholesterol Esters/metabolism ; Endosomes/metabolism ; Escherichia coli/genetics/metabolism ; Fibroblasts ; Fluorescence ; Fluorescent Dyes/metabolism ; Humans ; Lysosomes/metabolism ; *Membrane Glycoproteins ; Membrane Proteins/chemistry ; Membrane Transport Proteins/chemistry/*metabolism ; Molecular Sequence Data ; Niemann-Pick Diseases/genetics/*metabolism ; Oleic Acid/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/chemistry/*metabolism ; Proton-Motive Force ; Recombinant Proteins/metabolism ; Sequence Alignment
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 46
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-05-29
    Description: The ets family transcription factor PU.1 is required for the development of multiple lineages of the immune system. Using retroviral transduction of PU.1 complementary DNA into mutant hematopoietic progenitors, we demonstrate that differing concentrations of the protein regulate the development of B lymphocytes as compared with macrophages. A low concentration of PU. 1 protein induces the B cell fate, whereas a high concentration promotes macrophage differentiation and blocks B cell development. Conversely, a transcriptionally weakened mutant protein preferentially induces B cell generation. Our results suggest that graded expression of a transcription factor can be used to specify distinct cell fates in the hematopoietic system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeKoter, R P -- Singh, H -- New York, N.Y. -- Science. 2000 May 26;288(5470):1439-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Molecular Genetics and Cell Biology, The University of Chicago, 5841 South Maryland Avenue, MC1028, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827957" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/cytology/*physiology ; Cell Differentiation ; Cell Division ; Cell Lineage ; Cells, Cultured ; Coculture Techniques ; DNA, Complementary ; Gene Expression ; Genetic Vectors ; Green Fluorescent Proteins ; Hematopoiesis ; Hematopoietic Stem Cells/cytology/*physiology ; Luminescent Proteins/genetics ; Macrophages/cytology/*physiology ; Mice ; Mutation ; Proto-Oncogene Proteins/*genetics/*physiology ; Retroviridae/genetics ; Trans-Activators/*genetics/*physiology ; Transduction, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 47
    Publication Date: 2000-11-18
    Description: PSD-95 is a neuronal PDZ protein that associates with receptors and cytoskeletal elements at synapses, but whose function is uncertain. We found that overexpression of PSD-95 in hippocampal neurons can drive maturation of glutamatergic synapses. PSD-95 expression enhanced postsynaptic clustering and activity of glutamate receptors. Postsynaptic expression of PSD-95 also enhanced maturation of the presynaptic terminal. These effects required synaptic clustering of PSD-95 but did not rely on its guanylate kinase domain. PSD-95 expression also increased the number and size of dendritic spines. These results demonstrate that PSD-95 can orchestrate synaptic development and are suggestive of roles for PSD-95 in synapse stabilization and plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉El-Husseini, A E -- Schnell, E -- Chetkovich, D M -- Nicoll, R A -- Bredt, D S -- New York, N.Y. -- Science. 2000 Nov 17;290(5495):1364-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11082065" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Dendrites/ultrastructure ; Excitatory Postsynaptic Potentials ; Hippocampus/cytology ; Interneurons/cytology/metabolism/*physiology ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Nerve Tissue Proteins/chemistry/genetics/metabolism/*physiology ; Patch-Clamp Techniques ; Presynaptic Terminals/physiology ; Protein Structure, Tertiary ; Pyramidal Cells/cytology/metabolism/*physiology ; Rats ; Receptor Aggregation ; Receptors, AMPA/metabolism ; Receptors, Glutamate/*metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/metabolism/*physiology ; Synaptic Transmission ; Synaptic Vesicles/physiology ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 48
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-02-26
    Description: Europe's historic plurality and the lack of a commonly accepted definition of the moral status of the embryo have led to varying regulation in European countries. Council of Europe and European Union legislation, based on fundamental ethical principles, does exist for specific issues, such as prohibition against producing embryos solely for research. Such principles have recently been elucidated by the European Group on Ethics in Science and New Technologies. Newly emerging research techniques are beginning to cause reconsideration of the regulation of embryo research in Europe.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lenoir, N -- New York, N.Y. -- Science. 2000 Feb 25;287(5457):1425-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Conseil Constitutionnel, 2 rue de Montpensier, Paris 75001, France. noelle.lenoir@wanadoo.fr.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10688780" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; *Bioethics ; Cells, Cultured ; *Embryo Research ; Embryo, Mammalian/*cytology ; Europe ; European Union ; *Government Regulation ; Humans ; *Internationality ; Moral Obligations ; Public Policy ; *Research/legislation & jurisprudence ; Social Values ; *Stem Cells ; Value of Life
    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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  • 49
    Publication Date: 2000-01-29
    Description: The mechanism responsible for electromotility of outer hair cells in the ear is unknown but is thought to reside within the plasma membrane. Lipid lateral diffusion in the outer hair cell plasma membrane is a sigmoidal function of transmembrane potential and bathing media osmolality. Cell depolarization or hyposmotic challenge shorten the cell and reduce membrane fluidity by half. Changing the membrane tension with amphipathic drugs results in similar reductions. These dynamic changes in membrane fluidity represent the modulation of membrane tension by lipid-protein interactions. The voltage dependence may be associated with the force-generating motors that contribute to the exquisite sensitivity of mammalian hearing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1976274/" 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/PMC1976274/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oghalai, J S -- Zhao, H B -- Kutz, J W -- Brownell, W E -- R01 DC000354/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 28;287(5453):658-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Otolaryngology and Communicative Sciences, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10650000" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/drug effects/physiology ; Cells, Cultured ; Chlorpromazine/pharmacology ; Diffusion ; Erythrocyte Membrane/drug effects/physiology ; Fluorescent Dyes/metabolism ; Guinea Pigs ; Hair Cells, Auditory, Outer/drug effects/*physiology/ultrastructure ; Lipid Bilayers ; *Membrane Fluidity ; Membrane Potentials ; Osmolar Concentration ; Patch-Clamp Techniques ; Phospholipids/*physiology ; Pressure ; Pyridinium Compounds/metabolism ; Rats ; Salicylates/pharmacology
    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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