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  • Tumor Cells, Cultured  (43)
  • American Association for the Advancement of Science (AAAS)  (43)
  • American Chemical Society
  • American Chemical Society (ACS)
  • Copernicus
  • Elsevier
  • National Academy of Sciences
  • Public Library of Science
  • 2015-2019
  • 2005-2009
  • 1990-1994  (43)
  • 1994  (43)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (43)
  • American Chemical Society
  • American Chemical Society (ACS)
  • Copernicus
  • Elsevier
    • +
Years
  • 2015-2019
  • 2005-2009
  • 1990-1994  (43)
Year
  • 1
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    Premature p34cdc2 activation required for apoptosis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-25
    Description: Activation of the serine-threonine kinase p34cdc2 at an inappropriate time during the cell cycle leads to cell death that resembles apoptosis. Premature activation of p34cdc2 was shown to be required for apoptosis induced by a lymphocyte granule protease. The kinase was rapidly activated and tyrosine dephosphorylated at the initiation of apoptosis. DNA fragmentation and nuclear collapse could be prevented by blocking p34cdc2 activity with excess peptide substrate, or by inactivating p34cdc2 in a temperature-sensitive mutant. Premature p34cdc2 activation may be a general mechanism by which cells induced to undergo apoptosis initiate the disruption of the nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi, L -- Nishioka, W K -- Th'ng, J -- Bradbury, E M -- Litchfield, D W -- Greenberg, A H -- New York, N.Y. -- Science. 1994 Feb 25;263(5150):1143-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8108732" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; CDC2 Protein Kinase/*metabolism ; DNA Damage ; Deoxyribonucleases/pharmacology ; Enzyme Activation ; Enzyme Induction ; Membrane Glycoproteins/pharmacology ; Mice ; Mitosis ; Molecular Sequence Data ; Perforin ; Phosphorylation ; Pore Forming Cytotoxic Proteins ; Serine Endopeptidases/pharmacology ; Tumor Cells, Cultured
    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
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    DNA loop repair by human cell extracts (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: An activity in human cell extracts is described that repairs DNA with loops of five or more unpaired bases. Repair is strand-specific and is directed by a nick located 5' or 3' to the loop. This repair is observed in a colorectal cancer cell line that is devoid of a wild-type hMLH1 gene and is deficient in repair of mismatches. However, a cell line with deletions in both hMSH2 alleles is deficient in repair of both loops and mismatches. Defects in loop repair may be relevant to the repetitive-sequence instability observed in cancers and other hereditary diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Umar, A -- Boyer, J C -- Kunkel, T A -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):814-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973637" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Base Composition ; Base Sequence ; Carrier Proteins ; Cell Extracts ; Cell Line ; Colorectal Neoplasms/*genetics ; *DNA Repair ; DNA, Satellite/genetics/metabolism ; *DNA-Binding Proteins ; HeLa Cells ; Humans ; Molecular Sequence Data ; MutS Homolog 2 Protein ; Neoplasm Proteins/*genetics/physiology ; Nuclear Proteins ; Nucleic Acid Heteroduplexes/*metabolism ; Proto-Oncogene Proteins/*genetics/physiology ; Repetitive Sequences, Nucleic Acid ; Tumor Cells, Cultured
    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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  • 3
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    Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-24
    Description: Glycosyl-phosphatidylinositol (GPI)-anchored proteins have been reported to reside in clusters collected over small membrane invaginations called caveolae. The detection of different GPI-anchored proteins with fluorescently labeled monoclonal antibodies showed that these proteins are not constitutively concentrated in caveolae; they enter these structures independently after cross-linking with polyclonal secondary antibodies. Analysis of the cell surface distribution of the GPI-anchored folate receptor by electron microscopy confirms these observations. Thus, multimerization of GPI-anchored proteins regulates their sequestration in caveolae, but in the absence of agents that promote clustering they are diffusely distributed over the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayor, S -- Rothberg, K G -- Maxfield, F R -- DK27083/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1948-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7516582" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Antibodies, Monoclonal ; Antigens, CD/analysis/immunology/metabolism ; Antigens, CD55 ; Antigens, Surface/analysis/immunology/metabolism ; Antigens, Thy-1 ; Carrier Proteins/analysis/immunology/*metabolism ; Caveolin 1 ; *Caveolins ; Cell Membrane/*metabolism/ultrastructure ; Fluorescent Antibody Technique ; Folate Receptors, GPI-Anchored ; Folic Acid/metabolism ; Glycosylphosphatidylinositols/analysis/*metabolism ; Humans ; Immunoglobulin G/metabolism ; Membrane Glycoproteins/analysis/immunology/metabolism ; Membrane Proteins/analysis ; Mice ; Microscopy, Electron ; *Receptors, Cell Surface ; Tumor Cells, Cultured
    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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  • 4
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    Inhibition of NF-kappa B by sodium salicylate and aspirin (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-12
    Description: The transcription factor nuclear factor-kappa B (NF-kappa B) is critical for the inducible expression of multiple cellular and viral genes involved in inflammation and infection including interleukin-1 (IL-1), IL-6, and adhesion molecules. The anti-inflammatory drugs sodium salicylate and aspirin inhibited the activation of NF-kappa B, which further explains the mechanism of action of these drugs. This inhibition prevented the degradation of the NF-kappa B inhibitor, I kappa B, and therefore NF-kappa B was retained in the cytosol. Sodium salicylate and aspirin also inhibited NF-kappa B-dependent transcription from the Ig kappa enhancer and the human immunodeficiency virus (HIV) long terminal repeat (LTR) in transfected T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kopp, E -- Ghosh, S -- R01 AI 33443-01A1/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):956-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06536.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052854" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aspirin/*pharmacology ; Cell Line ; Enhancer Elements, Genetic ; Gene Expression/drug effects ; Genes, Reporter ; HIV Long Terminal Repeat ; HIV-1/genetics ; Humans ; Immunoglobulin kappa-Chains/genetics ; Lipopolysaccharides/pharmacology ; Mice ; NF-kappa B/*antagonists & inhibitors/metabolism ; Phosphorylation ; Promoter Regions, Genetic ; Protein Biosynthesis/drug effects ; Proto-Oncogene Proteins/metabolism ; Sodium Salicylate/*pharmacology ; T-Lymphocytes/metabolism ; Transcription Factor RelB ; *Transcription Factors ; Transfection ; Tumor Cells, Cultured
    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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  • 5
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    Role of bone marrow-derived cells in presenting MHC class I-restricted tumor antigens (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-13
    Description: Many tumors express tumor-specific antigens capable of being presented to CD8+ T cells by major histocompatibility complex (MHC) class I molecules. Antigen presentation models predict that the tumor cell itself should present these antigens to T cells. However, when conditions for the priming of tumor-specific responses were examined in mice, no detectable presentation of MHC class I-restricted tumor antigens by the tumor itself was found. Rather, tumor antigens were exclusively presented by host bone marrow-derived cells. Thus, MHC class I-restricted antigens are efficiently transferred in vivo to bone marrow-derived antigen-presenting cells, which suggests that human leukocyte antigen matching may be less critical in the application of tumor vaccines than previously thought.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, A Y -- Golumbek, P -- Ahmadzadeh, M -- Jaffee, E -- Pardoll, D -- Levitsky, H -- New York, N.Y. -- Science. 1994 May 13;264(5161):961-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7513904" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Presenting Cells/*immunology ; Antigens, Neoplasm/*immunology ; Bone Marrow/immunology ; Bone Marrow Cells ; Colonic Neoplasms/immunology ; Epitopes ; Female ; Granulocyte-Macrophage Colony-Stimulating Factor/genetics/immunology ; H-2 Antigens/immunology ; Histocompatibility Antigens Class I/*immunology ; Melanoma, Experimental/immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Nucleocapsid Proteins ; *Nucleoproteins ; T-Lymphocytes, Cytotoxic/*immunology ; Tumor Cells, Cultured ; Viral Core Proteins/immunology
    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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  • 6
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    A specific inhibitor of the epidermal growth factor receptor tyrosine kinase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-19
    Description: A small molecule called PD 153035 inhibited the epidermal growth factor (EGF) receptor tyrosine kinase with a 5-pM inhibition constant. The inhibitor was specific for the EGF receptor tyrosine kinase and inhibited other purified tyrosine kinases only at micromolar or higher concentrations. PD 153035 rapidly suppressed autophosphorylation of the EGF receptor at low nanomolar concentrations in fibroblasts or in human epidermoid carcinoma cells and selectively blocked EGF-mediated cellular processes including mitogenesis, early gene expression, and oncogenic transformation. PD 153035 demonstrates an increase in potency over that of other tyrosine kinase inhibitors of four to five orders of magnitude for inhibition of isolated EGF receptor tyrosine kinase and three to four orders of magnitude for inhibition of cellular phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fry, D W -- Kraker, A J -- McMichael, A -- Ambroso, L A -- Nelson, J M -- Leopold, W R -- Connors, R W -- Bridges, A J -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1093-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, MI 48105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066447" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Cell Transformation, Neoplastic/drug effects ; Epidermal Growth Factor/pharmacology ; Fibroblast Growth Factor 2/pharmacology ; Gene Expression/drug effects ; Humans ; Kinetics ; Mice ; Mitosis/drug effects ; Phosphorylation/drug effects ; Platelet-Derived Growth Factor/pharmacology ; Protein-Tyrosine Kinases/antagonists & inhibitors ; Quinazolines/*antagonists & inhibitors ; Receptor, Epidermal Growth Factor/*antagonists & inhibitors ; Tumor Cells, Cultured ; Tyrosine/metabolism
    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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  • 7
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    Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-25
    Description: The T cell antigen receptor (TCR) initiates signals by interacting with cytoplasmic protein tyrosine kinases (PTKs) through a 17-residue sequence motif [called the antigen recognition activation motif (ARAM)] that is contained in the TCR zeta and CD3 chains. TCR stimulation induces the tyrosine phosphorylation of several cellular substrates, including the ARAMs. Lck kinase activity is required for phosphorylation of two conserved tyrosine residues in an ARAM. This phosphorylation leads to the recruitment of a second cytoplasmic PTK, ZAP-70, through both of the ZAP-70 Src homology 2 domains and its phosphorylation. Thus, TCR signal transduction is initiated by the sequential interaction of two PTKs with TCR ARAMs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iwashima, M -- Irving, B A -- van Oers, N S -- Chan, A C -- Weiss, A -- AR-20684/AR/NIAMS NIH HHS/ -- GM39553/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 25;263(5150):1136-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7509083" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD8/metabolism ; Cell Line ; Cytoplasm/enzymology ; Haplorhini ; Humans ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Signal Transduction ; Tumor Cells, Cultured ; Tyrosine/analogs & derivatives/metabolism ; ZAP-70 Protein-Tyrosine Kinase
    Print ISSN: 0036-8075
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  • 8
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    Coding of hemolysins within the ribosomal RNA repeat on a plasmid in Entamoeba histolytica (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-11
    Description: The pathogenesis of amoebic dysentery is a result of cytolysis of the colonic mucosa by the parasitic protozoan Entamoeba histolytica. The cytolysis results in extensive local ulceration and allows the amoeba to penetrate and metastasize to distant sites. Factors involved in this process were defined with three clones that express hemolytic activities in Escherichia coli. These potential amoebic virulence determinants were also toxic to human colonic epithelial cells, the primary cellular targets in amoebal invasion of the large intestine. The coding sequences for the hemolysins were close to each other on a 2.6-kilobase segment of a 25-kilobase extrachromosomal DNA element. The structural genes for the hemolysins were within inverted repeats that encode ribosomal RNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jansson, A -- Gillin, F -- Kagardt, U -- Hagblom, P -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1440-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Uppsala University, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128227" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Survival/drug effects ; Cloning, Molecular ; Entamoeba histolytica/*genetics/pathogenicity ; Escherichia coli/genetics ; *Genes, Protozoan ; Hemolysin Proteins/*genetics/toxicity ; Molecular Sequence Data ; Open Reading Frames ; *Plasmids ; RNA, Protozoan/genetics ; RNA, Ribosomal/*genetics ; Repetitive Sequences, Nucleic Acid ; Tumor Cells, Cultured ; Virulence
    Print ISSN: 0036-8075
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  • 9
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    Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-04
    Description: The 2;5 chromosomal translocation occurs in most anaplastic large-cell non-Hodgkin's lymphomas arising from activated T lymphocytes. This rearrangement was shown to fuse the NPM nucleolar phosphoprotein gene on chromosome 5q35 to a previously unidentified protein tyrosine kinase gene, ALK, on chromosome 2p23. In the predicted hybrid protein, the amino terminus of nucleophosmin (NPM) is linked to the catalytic domain of anaplastic lymphoma kinase (ALK). Expressed in the small intestine, testis, and brain but not in normal lymphoid cells, ALK shows greatest sequence similarity to the insulin receptor subfamily of kinases. Unscheduled expression of the truncated ALK may contribute to malignant transformation in these lymphomas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morris, S W -- Kirstein, M N -- Valentine, M B -- Dittmer, K G -- Shapiro, D N -- Saltman, D L -- Look, A T -- CA 21765/CA/NCI NIH HHS/ -- KO8 CA 01702/CA/NCI NIH HHS/ -- P01 CA 20180/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Oncology, St. Jude Children's Research Hospital, Memphis, TN 38105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122112" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Brain/enzymology ; Cell Transformation, Neoplastic ; Chromosome Walking ; Chromosomes, Human, Pair 2 ; Chromosomes, Human, Pair 5 ; Cloning, Molecular ; Gene Expression Regulation, Neoplastic ; Humans ; Intestine, Small/enzymology ; Lymphoma, Large-Cell, Anaplastic/chemistry/enzymology/*genetics ; Male ; Molecular Sequence Data ; Nuclear Proteins/chemistry/*genetics ; Phosphoproteins/chemistry/*genetics ; Promoter Regions, Genetic ; Protein-Tyrosine Kinases/chemistry/*genetics ; RNA, Messenger/genetics/metabolism ; Receptor Protein-Tyrosine Kinases ; Sequence Alignment ; Signal Transduction ; Testis/enzymology ; *Translocation, Genetic ; Tumor Cells, Cultured
    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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  • 10
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    Association of intestinal peptide transport with a protein related to the cadherin superfamily (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-15
    Description: The first step in oral absorption of many medically important peptide-based drugs is mediated by an intestinal proton-dependent peptide transporter. This transporter facilitates the oral absorption of beta-lactam antibiotics and angiotensin-converting enzyme inhibitors from the intestine into enterocytes lining the luminal wall. A monoclonal antibody that blocked uptake of cephalexin was used to identify and clone a gene that encodes an approximately 92-kilodalton membrane protein that was associated with the acquisition of peptide transport activity by transport-deficient cells. The amino acid sequence deduced from the complementary DNA sequence of the cloned gene indicated that this transport-associated protein shares several conserved structural elements with the cadherin superfamily of calcium-dependent, cell-cell adhesion proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dantzig, A H -- Hoskins, J A -- Tabas, L B -- Bright, S -- Shepard, R L -- Jenkins, I L -- Duckworth, D C -- Sportsman, J R -- Mackensen, D -- Rosteck, P R Jr -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153632" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; CHO Cells ; Cadherins/*chemistry ; Carrier Proteins/*chemistry/genetics/isolation & purification/metabolism ; Cephalexin/*metabolism ; Cloning, Molecular ; Cricetinae ; Glycosylation ; Humans ; Hydrogen-Ion Concentration ; Intestinal Mucosa/*metabolism ; Leucine/analogs & derivatives/metabolism ; *Membrane Transport Proteins ; Mice ; Mice, Inbred A ; Molecular Sequence Data ; Open Reading Frames ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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  • 11
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    Fas and perforin pathways as major mechanisms of T cell-mediated cytotoxicity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-22
    Description: Two molecular mechanisms of T cell-mediated cytotoxicity, one perforin-based, the other Fas-based, have been demonstrated. To determine the extent of their contribution to T cell-mediated cytotoxicity, a range of effector cells from normal control or perforin-deficient mice were tested against a panel of target cells with various levels of Fas expression. All cytotoxicity observed was due to either of these mechanisms, and no third mechanism was detected. Thus, the perforin- and Fas-based mechanisms may account for all T cell-mediated cytotoxicity in short-term in vitro assays.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kagi, D -- Vignaux, F -- Ledermann, B -- Burki, K -- Depraetere, V -- Nagata, S -- Hengartner, H -- Golstein, P -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):528-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7518614" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD95 ; Antigens, Surface/*immunology ; Cells, Cultured ; Concanavalin A/pharmacology ; *Cytotoxicity, Immunologic ; Ionomycin/pharmacology ; Leukemia L1210 ; Lymphocyte Culture Test, Mixed ; Lymphocytic choriomeningitis virus/immunology ; Membrane Glycoproteins/*immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Molecular Sequence Data ; Perforin ; Pore Forming Cytotoxic Proteins ; T-Lymphocytes, Cytotoxic/*immunology ; Tetradecanoylphorbol Acetate/pharmacology ; Tumor Cells, Cultured
    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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  • 12
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    Activation of the sphingomyelin cycle through the low-affinity neurotrophin receptor (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-09
    Description: The role of the low-affinity neurotrophin receptor (p75NTR) in signal transduction is undefined. Nerve growth factor can activate the sphingomyelin cycle, generating the putative-lipid second messenger ceramide. In T9 glioma cells, addition of a cell-permeable ceramide analog mimicked the effects of nerve growth factor on cell growth inhibition and process formation. This signaling pathway appears to be mediated by p75NTR in T9 cells and NIH 3T3 cells overexpressing p75NTR. Expression of an epidermal growth factor receptor-p75NTR chimera in T9 cells imparted to epidermal growth factor the ability to activate the sphingomyelin cycle. These data demonstrate that p75NTR is capable of signaling independently of the trk neurotrophin receptor (p140trk) and that ceramide may be a mediator in neurotrophin biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dobrowsky, R T -- Werner, M H -- Castellino, A M -- Chao, M V -- Hannun, Y A -- AG05531/AG/NIA NIH HHS/ -- GM43825/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Medicine and Cell Biology, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8079174" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Astrocytes/cytology/*metabolism ; Ceramides/metabolism/pharmacology ; Epidermal Growth Factor/pharmacology ; Glioblastoma ; Mice ; Nerve Growth Factors/pharmacology ; Proto-Oncogene Proteins/metabolism ; Rats ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, Epidermal Growth Factor/metabolism ; Receptor, trkA ; Receptors, Nerve Growth Factor/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Sphingomyelins/*metabolism ; Tumor Cells, Cultured
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  • 13
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    Effective tumor vaccine generated by fusion of hepatoma cells with activated B cells (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-28
    Description: Fusion of BERH-2 rat hepatocellular carcinoma cells with activated B cells produced hybrid cells that lost their tumorigenicity and became immunogenic. Syngeneic rats injected with BERH-2-B hybrid cells became resistant to challenge with parental BERH-2 cells, and rats with established BERH-2 hepatomas were cured by subsequent injection of BERH-2-B cells. Both CD4+ and CD8+ cells were essential for the induction of protective immunity; however, only CD8+ cells were required for the eradication of BERH-2 tumors. The generation of hybrid tumor cells that elicit antitumor immune responses may be a useful strategy for cancer immunotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guo, Y -- Wu, M -- Chen, H -- Wang, X -- Liu, G -- Li, G -- Ma, J -- Sy, M S -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):518-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tumor Immunology and Biotherapy Center, Eastern Institute of Hepatobiliary Surgery, Shanghai, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7507262" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD80/analysis ; B-Lymphocytes/*immunology ; CD4-Positive T-Lymphocytes/immunology ; Cell Fusion ; Female ; Histocompatibility Antigens Class II/analysis ; Hybrid Cells/*immunology ; Immunotherapy, Active ; Liver Neoplasms, Experimental/*immunology/prevention & control/therapy ; Lymphocyte Activation ; Neoplasm Transplantation ; Rats ; Rats, Wistar ; T-Lymphocyte Subsets/immunology ; Tumor Cells, Cultured ; Vaccination ; Vaccines/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: A homozygous mutation in the kinase domain of ZAP-70, a T cell receptor-associated protein tyrosine kinase, produced a distinctive form of human severe combined immunodeficiency. Manifestations of this disorder included profound immunodeficiency, absence of peripheral CD8+ T cells, and abundant peripheral CD4+ T cells that were refractory to T cell receptor-mediated activation. These findings demonstrate that ZAP-70 is essential for human T cell function and suggest that CD4+ and CD8+ T cells depend on different intracellular signaling pathways to support their development or survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elder, M E -- Lin, D -- Clever, J -- Chan, A C -- Hope, T J -- Weiss, A -- Parslow, T G -- AI29313/AI/NIAID NIH HHS/ -- GM43574/GM/NIGMS NIH HHS/ -- RR01271/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of California, San Francisco 94143-0110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202712" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cloning, Molecular ; Female ; Frameshift Mutation ; Gene Deletion ; Homozygote ; Humans ; Infant ; Male ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*genetics/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Severe Combined Immunodeficiency/*genetics/immunology ; Signal Transduction ; T-Lymphocyte Subsets/*immunology ; Transfection ; Tumor Cells, Cultured ; ZAP-70 Protein-Tyrosine Kinase
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  • 15
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    New tumor suppressor may rival p53 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):344-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153613" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/*genetics ; Chromosomes, Human, Pair 9 ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p16 ; *Cyclin-Dependent Kinases ; Gene Deletion ; *Genes, Tumor Suppressor ; Genes, p53 ; Humans ; Melanoma/genetics ; Mutation ; Neoplasms/*genetics ; Protein Kinase Inhibitors ; *Proto-Oncogene Proteins ; Tumor Cells, Cultured
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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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    Mutation of a mutL homolog in hereditary colon cancer (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-18
    Description: Some cases of hereditary nonpolyposis colorectal cancer (HNPCC) are due to alterations in a mutS-related mismatch repair gene. A search of a large database of expressed sequence tags derived from random complementary DNA clones revealed three additional human mismatch repair genes, all related to the bacterial mutL gene. One of these genes (hMLH1) resides on chromosome 3p21, within 1 centimorgan of markers previously linked to cancer susceptibility in HNPCC kindreds. Mutations of hMLH1 that would disrupt the gene product were identified in such kindreds, demonstrating that this gene is responsible for the disease. These results suggest that defects in any of several mismatch repair genes can cause HNPCC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papadopoulos, N -- Nicolaides, N C -- Wei, Y F -- Ruben, S M -- Carter, K C -- Rosen, C A -- Haseltine, W A -- Fleischmann, R D -- Fraser, C M -- Adams, M D -- CA35494/CA/NCI NIH HHS/ -- CA47527/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1625-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Oncology Center, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128251" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; *Adenosine Triphosphatases ; Amino Acid Sequence ; Bacterial Proteins/chemistry/*genetics ; Base Sequence ; Carrier Proteins ; Chromosome Mapping ; *Chromosomes, Human, Pair 3 ; Codon ; Colorectal Neoplasms, Hereditary Nonpolyposis/*genetics ; *DNA Repair ; *DNA-Binding Proteins ; *Escherichia coli Proteins ; Female ; Frameshift Mutation ; *Genes ; Genetic Markers ; Humans ; Male ; Molecular Sequence Data ; MutS Homolog 2 Protein ; Mutation ; Neoplasm Proteins/chemistry/*genetics ; Nuclear Proteins ; Open Reading Frames ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/genetics ; Sequence Deletion ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-25
    Description: GADD45 is a ubiquitously expressed mammalian gene that is induced by DNA damage and certain other stresses. Like another p53-regulated gene, p21WAF1/CIP1, whose product binds to cyclin-dependent kinases (Cdk's) and proliferating cell nuclear antigen (PCNA), GADD45 has been associated with growth suppression. Gadd45 was found to bind to PCNA, a normal component of Cdk complexes and a protein involved in DNA replication and repair. Gadd45 stimulated DNA excision repair in vitro and inhibited entry of cells into S phase. These results establish GADD45 as a link between the p53-dependent cell cycle checkpoint and DNA repair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, M L -- Chen, I T -- Zhan, Q -- Bae, I -- Chen, C Y -- Gilmer, T M -- Kastan, M B -- O'Connor, P M -- Fornace, A J Jr -- ES05777/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1376-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Pharmacology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973727" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Division/drug effects ; Cell Line ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins/metabolism ; DNA/biosynthesis ; DNA Damage ; *DNA Repair ; *Genes, p53 ; Humans ; Intracellular Signaling Peptides and Proteins ; Proliferating Cell Nuclear Antigen/*metabolism ; Proteins/*metabolism/pharmacology ; Recombinant Proteins/metabolism/pharmacology ; S Phase/*drug effects ; Transfection ; Tumor Cells, Cultured
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  • 18
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    Identification of a peptide recognized by five melanoma-specific human cytotoxic T cell lines (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-04-29
    Description: Of several thousand peptides presented by the major histocompatibility molecule HLA-A2.1, at least nine are recognized by melanoma-specific cytotoxic T lymphocytes (CTLs). Tandem mass spectrometry was used to identify and to sequence one of these peptide epitopes. Melanoma-specific CTLs had an exceptionally high affinity for this nine-residue peptide, which reconstituted an epitope for CTL lines from each of five different melanoma patients tested. Recognition by multiple CTL lines suggests that this may be a promising candidate for use in peptide-based melanoma vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cox, A L -- Skipper, J -- Chen, Y -- Henderson, R A -- Darrow, T L -- Shabanowitz, J -- Engelhard, V H -- Hunt, D F -- Slingluff, C L Jr -- AI33993/AI/NIAID NIH HHS/ -- CA57653/CA/NCI NIH HHS/ -- GM37537/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 29;264(5159):716-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Virginia, Charlottesville 22908.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7513441" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Neoplasm/*immunology ; Chromatography, High Pressure Liquid ; Epitopes/immunology ; HLA-A2 Antigen/immunology ; Humans ; Mass Spectrometry ; Melanoma/*immunology ; Molecular Sequence Data ; Oligopeptides/*immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Tumor Cells, Cultured
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  • 19
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    Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6 (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-04-01
    Description: The STAT family of proteins carries out a dual function: signal transduction and activation of transcription. A new family member, Stat3, becomes activated through phosphorylation on tyrosine as a DNA binding protein in response to epidermal growth factor (EGF) and interleukin-6 (IL-6) but not interferon gamma (IFN-gamma). It is likely that this phosphoprotein forms homodimers as well as heterodimers with the first described member of the STAT family, Stat91 (renamed Stat1 alpha), which is activated by the IFNs and EGF. Differential activation of different STAT proteins in response to different ligands should help to explain specificity in nuclear signaling from the cell surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhong, Z -- Wen, Z -- Darnell, J E Jr -- AI32489/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):95-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140422" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; Epidermal Growth Factor/*pharmacology ; Humans ; Interferon-gamma ; Interleukin-6/*pharmacology ; Mice ; Molecular Sequence Data ; Phosphorylation ; Regulatory Sequences, Nucleic Acid ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Sequence Alignment ; Trans-Activators/metabolism ; Transfection ; Tumor Cells, Cultured ; Tyrosine/metabolism
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  • 20
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    Transformation of lupus-inducing drugs to cytotoxic products by activated neutrophils (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-11-04
    Description: Drug-induced lupus is a serious side effect of certain medications, but the chemical features that confer this property and the underlying pathogenesis are puzzling. Prototypes of all six therapeutic classes of lupus-inducing drugs were highly cytotoxic only in the presence of activated neutrophils. Removal of extracellular hydrogen peroxide before, but not after, exposure of the drug to activated neutrophils prevented cytotoxicity. Neutrophil-dependent cytotoxicity required the enzymatic action of myeloperoxidase, resulting in the chemical transformation of the drug to a reactive product. The capacity of drugs to serve as myeloperoxidase substrates in vitro was associated with the ability to induce lupus in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jiang, X -- Khursigara, G -- Rubin, R L -- MO1 RR00833/RR/NCRR NIH HHS/ -- R01 AG09574/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):810-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W. M. Keck Autoimmune Disease Center, Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973636" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Assay ; Biotransformation ; Cell Death/*drug effects ; Chlorpromazine/analogs & derivatives/metabolism/toxicity ; Humans ; Hydralazine/analogs & derivatives/metabolism/toxicity ; Hydrogen Peroxide/metabolism ; Isoniazid/analogs & derivatives/metabolism/toxicity ; Lupus Erythematosus, Systemic/*chemically induced ; Mice ; *Neutrophil Activation ; Neutrophils/enzymology/*metabolism ; Peroxidase/*metabolism ; Procainamide/analogs & derivatives/metabolism/toxicity ; Propylthiouracil/analogs & derivatives/metabolism/toxicity ; Quinidine/analogs & derivatives/metabolism/toxicity ; Tumor Cells, Cultured
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  • 21
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    Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-01-28
    Description: A gene encoding a protein related to the serpin family of protease inhibitors was identified as a candidate tumor suppressor gene that may play a role in human breast cancer. The gene product, called maspin, is expressed in normal mammary epithelial cells but not in most mammary carcinoma cell lines. Transfection of MDA-MB-435 mammary carcinoma cells with the maspin gene did not alter the cells' growth properties in vitro, but reduced the cells' ability to induce tumors and metastasize in nude mice and to invade through a basement membrane matrix in vitro. Analysis of human breast cancer specimens revealed that loss of maspin expression occurred most frequently in advanced cancers. These results support the hypothesis that maspin functions as a tumor suppressor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zou, Z -- Anisowicz, A -- Hendrix, M J -- Thor, A -- Neveu, M -- Sheng, S -- Rafidi, K -- Seftor, E -- Sager, R -- CA39814/CA/NCI NIH HHS/ -- P01 CA22427/CA/NCI NIH HHS/ -- R01 CA59702/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):526-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cancer Genetics, Dana-Farber Cancer Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8290962" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Breast/*chemistry ; Breast Neoplasms/*chemistry/pathology ; Down-Regulation ; Epithelium/chemistry ; Female ; Gene Expression ; Genes, Tumor Suppressor ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; Neoplasm Metastasis ; Neoplasm Transplantation ; Neoplasms, Experimental/pathology ; Proteins/analysis/genetics/*physiology ; Sequence Analysis ; Serpins/analysis/genetics/*physiology ; Transfection ; Tumor Cells, Cultured
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  • 22
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    An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-05-27
    Description: Normal processing of the amyloid beta protein precursor (beta APP) results in secretion of a soluble 4-kilodalton protein essentially identical to the amyloid beta protein (A beta) that forms insoluble fibrillar deposits in Alzheimer's disease. Human neuroblastoma (M17) cells transfected with constructs expressing wild-type beta APP or the beta APP717 mutants linked to familial Alzheimer's disease were compared by (i) isolation of metabolically labeled 4-kilodalton A beta from conditioned medium, digestion with cyanogen bromide, and analysis of the carboxyl-terminal peptides released, or (ii) analysis of the A beta in conditioned medium with sandwich enzyme-linked immunosorbent assays that discriminate A beta 1-40 from the longer A beta 1-42. Both methods demonstrated that the 4-kilodalton A beta released from wild-type beta APP is primarily but not exclusively A beta 1-40. The beta APP717 mutations, which are located three residues carboxyl to A beta 43, consistently caused a 1.5- to 1.9-fold increase in the percentage of longer A beta generated. Long A beta (for example, A beta 1-42) forms insoluble amyloid fibrils more rapidly than A beta 1-40. Thus, the beta APP717 mutants may cause Alzheimer's disease because they secrete increased amounts of long A beta, thereby fostering amyloid deposition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suzuki, N -- Cheung, T T -- Cai, X D -- Odaka, A -- Otvos, L Jr -- Eckman, C -- Golde, T E -- Younkin, S G -- AG06656/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1994 May 27;264(5163):1336-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Discovery Research Division, Takeda Chemical Industries, Ltd., Ibaraki, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8191290" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/genetics ; Amyloid beta-Peptides/chemistry/*secretion ; Amyloid beta-Protein Precursor/chemistry/genetics/*metabolism ; Culture Media, Conditioned ; Enzyme-Linked Immunosorbent Assay ; Humans ; *Mutation ; Neuroblastoma ; Transfection ; Tumor Cells, Cultured
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  • 23
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    Accumulation of HLA-DM, a regulator of antigen presentation, in MHC class II compartments (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-12-02
    Description: The HLA-DM genes encode an unconventional HLA (human leukocyte antigen) class II molecule that is required for appropriate binding of peptide to classical HLA class II products. In the absence of DM, other class II molecules are unstable upon electrophoresis in sodium dodecyl sulfate and are largely associated with a nested set of peptides derived from the invariant chain called CLIP, for class II-associated invariant chain peptides. DMA and DMB associated and accumulated in multilaminar, intracellular compartments with classical class II molecules, but were found infrequently, if at all, at the cell surface. Thus, DM may facilitate peptide binding to class II molecules within these intracellular compartments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanderson, F -- Kleijmeer, M J -- Kelly, A -- Verwoerd, D -- Tulp, A -- Neefjes, J J -- Geuze, H J -- Trowsdale, J -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1566-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Immunogenetics Laboratory, Imperial Cancer Research Fund, Holborn, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985027" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Cell Compartmentation ; Cell Line ; Cell Membrane/immunology ; Endoplasmic Reticulum/immunology ; Genes, MHC Class II ; HLA-D Antigens/analysis/genetics/*metabolism ; Histocompatibility Antigens Class I/analysis ; Histocompatibility Antigens Class II/analysis/*metabolism ; Humans ; L Cells (Cell Line) ; Mice ; Microscopy, Immunoelectron ; Subcellular Fractions/immunology ; Tumor Cells, Cultured
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  • 24
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    Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: The EPH-related transmembrane tyrosine kinases constitute the largest known family of receptor-like tyrosine kinases, with many members displaying specific patterns of expression in the developing and adult nervous system. A family of cell surface-bound ligands exhibiting distinct, but overlapping, specificities for these EPH-related kinases was identified. These ligands were unable to act as conventional soluble factors. However, they did function when presented in membrane-bound form, suggesting that they require direct cell-to-cell contact to activate their receptors. Membrane attachment may serve to facilitate ligand dimerization or aggregation, because antibody-mediated clustering activated previously inactive soluble forms of these ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Gale, N W -- Aldrich, T H -- Maisonpierre, P C -- Lhotak, V -- Pawson, T -- Goldfarb, M -- Yancopoulos, G D -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973638" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/*metabolism ; *DNA-Binding Proteins ; Ephrin-A1 ; Ephrin-B1 ; Humans ; Ligands ; Membrane Proteins/chemistry/*metabolism ; Molecular Sequence Data ; Neurons/metabolism ; Phosphorylation ; Proteins/chemistry/*metabolism ; *Proto-Oncogene Proteins ; Receptor Protein-Tyrosine Kinases/*metabolism ; *Receptor, EphA5 ; Recombinant Fusion Proteins/metabolism ; Retroviridae Proteins, Oncogenic/*metabolism ; Solubility ; *Transcription Factors ; Transfection ; Tumor Cells, Cultured ; ets-Domain Protein Elk-1
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  • 25
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    Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-07
    Description: Interleukin-6 (IL-6), leukemia inhibitory factor, oncostatin M, interleukin-11, and ciliary neurotrophic factor bind to receptor complexes that share the signal transducer gp130. Upon binding, the ligands rapidly activate DNA binding of acute-phase response factor (APRF), a protein antigenically related to the p91 subunit of the interferon-stimulated gene factor-3 alpha (ISGF-3 alpha). These cytokines caused tyrosine phosphorylation of APRF and ISGF-3 alpha p91. Protein kinases of the Jak family were also rapidly tyrosine phosphorylated, and both APRF and Jak1 associated with gp130. These data indicate that Jak family protein kinases may participate in IL-6 signaling and that APRF may be activated in a complex with gp130.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lutticken, C -- Wegenka, U M -- Yuan, J -- Buschmann, J -- Schindler, C -- Ziemiecki, A -- Harpur, A G -- Wilks, A F -- Yasukawa, K -- Taga, T -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):89-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Biochemistry, RWTH Aachen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272872" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, CD ; Base Sequence ; Cytokine Receptor gp130 ; Cytokines/pharmacology ; DNA-Binding Proteins/*metabolism ; Humans ; Interferon-Stimulated Gene Factor 3 ; Interferon-Stimulated Gene Factor 3, gamma Subunit ; Interferon-gamma/pharmacology ; Interleukin-6/*pharmacology ; Janus Kinase 1 ; Membrane Glycoproteins/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Signal Transduction ; *Trans-Activators ; Transcription Factors/metabolism ; Tumor Cells, Cultured ; Tyrosine/metabolism
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  • 26
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    Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-23
    Description: Upon entry into a host cell, retroviruses direct the reverse transcription of the viral RNA genome and the establishment of an integrated proviral DNA. The retroviral integrase protein (IN) is responsible for the insertion of the viral DNA into host chromosomal targets. The two-hybrid system was used to identify a human gene product that binds tightly to the human immunodeficiency virus-type 1 (HIV-1) integrase in vitro and stimulates its DNA-joining activity. The sequence of the gene suggests that the protein is a human homolog of yeast SNF5, a transcriptional activator required for high-level expression of many genes. The gene, termed INI1 (for integrase interactor 1), may encode a nuclear factor that promotes integration and targets incoming viral DNA to active genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalpana, G V -- Marmon, S -- Wang, W -- Crabtree, G R -- Goff, S P -- U01 AI 24845/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):2002-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801128" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosomal Proteins, Non-Histone ; DNA Nucleotidyltransferases/*metabolism ; DNA, Complementary/genetics ; DNA, Viral/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; HIV-1/*enzymology/genetics ; Humans ; Integrases ; Molecular Sequence Data ; Molecular Weight ; Oligodeoxyribonucleotides/metabolism ; Open Reading Frames ; Sequence Alignment ; Transcription Factors/chemistry/*metabolism ; Tumor Cells, Cultured ; Virus Integration ; Zinc Fingers
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    cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-26
    Description: Proteasomes are the proteolytic complex responsible for major histocompatibility complex (MHC) class I-restricted antigen presentation. Interferon gamma treatment increases expression MHC-encoded LMP2 and LMP7 subunits of the proteasome and decreases expression of two proteasome subunits, named X and Y, which alters the proteolytic specificity of proteasomes. Molecular cloning of complementary DNAs encoding X and Y showed that their proteins are proteasomal subunits with high amino acid similarity to LMP7 and LMP2, respectively. Thus, interferon gamma may induce subunit replacements of X and Y by LMP7 and LMP2, respectively, producing proteasomes perhaps more appropriate for the immunological processing of endogenous antigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akiyama, K -- Yokota, K -- Kagawa, S -- Shimbara, N -- Tamura, T -- Akioka, H -- Nothwang, H G -- Noda, C -- Tanaka, K -- Ichihara, A -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1231-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Urology, School of Medicine, University of Tokushima, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066462" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; *Cysteine Endopeptidases ; DNA, Complementary/genetics ; *Down-Regulation ; Endopeptidases/chemistry/genetics ; Humans ; Interferon-gamma/*pharmacology ; Major Histocompatibility Complex ; Molecular Sequence Data ; *Multienzyme Complexes ; *Proteasome Endopeptidase Complex ; Proteins/chemistry/*genetics/metabolism ; Sequence Homology, Amino Acid ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 28
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    Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-21
    Description: A number of bacterial protein toxins, including adenylate cyclase (AC) toxin from Bordetella pertussis, require the product of an accessory gene in order to express their biological activities. In this study, mass spectrometry was used to demonstrate that activated, wild-type AC toxin was modified by amide-linked palmitoylation on the epsilon-amino group of lysine 983. This modification was absent from a mutant in which the accessory gene had been disrupted. A synthetic palmitoylated peptide corresponding to the tryptic fragment (glutamine 972 to arginine 984) that contained the acylation blocked AC toxin-induced accumulation of adenosine 3',5'-monophosphate, whereas the non-acylated peptide had no effect.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hackett, M -- Guo, L -- Shabanowitz, J -- Hunt, D F -- Hewlett, E L -- DK38942/DK/NIDDK NIH HHS/ -- GM37537/GM/NIGMS NIH HHS/ -- R0-1 AI18000/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):433-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Virginia, Charlottesville 22901.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939682" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; *Adenylate Cyclase Toxin ; Amino Acid Sequence ; Animals ; Chromatography, High Pressure Liquid ; Cyclic AMP/metabolism ; Hemolysis ; Humans ; Lysine/*metabolism ; Mass Spectrometry ; Molecular Sequence Data ; Mutation ; Palmitates/*metabolism ; Peptide Fragments/chemistry/toxicity ; Sheep ; Tumor Cells, Cultured ; Virulence Factors, Bordetella/chemistry/*metabolism/toxicity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 29
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    Differential adhesion of cells to enantiomorphous crystal surfaces (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-11
    Description: Interactions during cell adhesion to external surfaces may reach the level of discrimination of molecular chirality. Cultured epithelial cells interact differently with the [011] faces of the (R,R) and (S,S) calcium tartrate tetrahydrate crystals. In a modified version of the classical Pasteur experiment, the enantiomorphous crystals were sorted out from a 1:1 mixture by the selective adhesion of cells to the (R,R) crystals. This stereospecificity results from molecular recognition between chiral components on the cell surface and the structured crystal surface. Crystals may allow experimental differentiation between distinct stages in cell substrate contacts, providing mechanistic information not readily attainable on conventional heterogeneous surfaces.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanein, D -- Geiger, B -- Addadi, L -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1413-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128221" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Adhesion ; Cell Line ; Computer Graphics ; Crystallization ; Humans ; Oligopeptides/pharmacology ; Stereoisomerism ; Surface Properties ; *Tartrates ; Tumor Cells, Cultured ; Xenopus laevis
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    Link to hereditary melanoma brightens mood for p16 gene (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1364-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073268" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/*genetics ; *Chromosomes, Human, Pair 9 ; Cyclin-Dependent Kinase Inhibitor p16 ; Female ; Genes, Tumor Suppressor ; Humans ; Male ; Melanoma/*genetics ; Mutation ; Pedigree ; Tumor Cells, Cultured
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    A challenge to p16 gene as a major tumor suppressor (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1846.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009205" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/genetics ; *Chromosomes, Human, Pair 9 ; Cyclin-Dependent Kinase Inhibitor p16 ; Gene Deletion ; *Genes, Tumor Suppressor ; Humans ; Mutation ; Neoplasms/*genetics ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Association of insulin receptor substrate-1 with integrins (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: Insulin stimulation was found to promote association of the alpha v beta 3 integrin (a vitronectin receptor) with insulin receptor substrate-1 (IRS-1), an intracellular protein that mediates insulin signaling by binding other signaling molecules, including growth factor receptor-bound protein 2 (Grb2) and phosphatidylinositol-3' kinase. Insulin-treated cells expressing the alpha v beta 3 integrin showed 2.5 times more DNA synthesis when plated on vitronectin than on other substrates, whereas cells expressing another vitronectin receptor, alpha v beta 5, did not show this difference. The association between integrin and IRS-1 may be a mechanism for the synergistic action of growth factor and extracellular matrix receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vuori, K -- Ruoslahti, E -- CA 28896/CA/NCI NIH HHS/ -- CA 30199/CA/NCI NIH HHS/ -- CA 42507/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1576-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center, La Jolla Cancer Research Foundation, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7527156" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Collagen ; DNA/biosynthesis ; Glycoproteins ; Humans ; Insulin/pharmacology ; Insulin Receptor Substrate Proteins ; Integrins/*metabolism ; Molecular Sequence Data ; Phosphoproteins/*metabolism ; Phosphorylation ; Rats ; Receptor, Insulin ; Receptors, Cytoadhesin/*metabolism ; Receptors, Vitronectin ; Transfection ; Tumor Cells, Cultured ; Vitronectin
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  • 33
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    Phospholipase D: a downstream effector of ARF in granulocytes (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-01-28
    Description: Activation of the phospholipase D (PLD) pathway is a widespread response when cells are activated by agonists that bind receptors on the cell surface. A 16-kD cytosolic component can reconstitute guanosine triphosphate (GTP)-mediated activation of phospholipase D in HL60 cells depleted of their cytosol by permeabilization. This factor was purified and identified as two small GTP-binding proteins, ARF1 and ARF3. Recombinant ARF1 substituted for purified ARF proteins in the reconstitution assay. These results indicate that phospholipase D is a downstream effector of ARF1 and ARF3. The well-established role of ARF in vesicular traffic would suggest that alterations in lipid content by PLD are an important determinant in vesicular dynamics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cockcroft, S -- Thomas, G M -- Fensome, A -- Geny, B -- Cunningham, E -- Gout, I -- Hiles, I -- Totty, N F -- Truong, O -- Hsuan, J J -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):523-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University College London, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8290961" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Amino Acid Sequence ; Animals ; Cattle ; Cytosol/chemistry ; Enzyme Activation ; GTP-Binding Proteins/chemistry/isolation & purification/*metabolism ; *Glycerophospholipids ; Granulocytes/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Humans ; Molecular Sequence Data ; Phosphatidic Acids/metabolism ; Phosphatidylcholines/metabolism ; Phospholipase D/*metabolism ; Recombinant Proteins/metabolism ; Tumor Cells, Cultured
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  • 34
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    Regulation of MHC class II expression by interferon-gamma mediated by the transactivator gene CIITA (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-07-01
    Description: Major histocompatibility complex (MHC) class II genes are expressed constitutively in only a few cell types, but they can be induced in the majority of them, in particular by interferon-gamma (IFN-gamma). The MHC class II transactivator gene CIITA is defective in a form of primary MHC class II deficiency. Here it is shown that CIITA expression is controlled and induced by IFN-gamma. A functional CIITA gene is necessary for class II induction, and transfection of CIITA is sufficient to activate expression of MHC class II genes in class II-negative cells in the absence of IFN-gamma. CIITA is therefore a general regulator of both inducible and constitutive MHC class II expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steimle, V -- Siegrist, C A -- Mottet, A -- Lisowska-Grospierre, B -- Mach, B -- New York, N.Y. -- Science. 1994 Jul 1;265(5168):106-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Microbiology, University of Geneva Medical School, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8016643" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 16 ; Fibroblasts ; *Gene Expression Regulation ; *Genes, MHC Class II ; Histocompatibility Antigens Class II/biosynthesis/*genetics ; Humans ; Interferon-gamma/*pharmacology ; Models, Genetic ; *Nuclear Proteins ; RNA, Messenger/genetics/metabolism ; Trans-Activators/biosynthesis/*genetics ; Transfection ; Tumor Cells, Cultured
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    Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-02-04
    Description: Human platelet-derived growth factor receptors (PDGFRs) expressed in human Hep G2 cells internalized and concentrated in a juxtanuclear region near the Golgi network within 10 minutes after the cells were treated with PDGF. A PDGFR mutant (F5) that lacks high-affinity binding sites for the Src homology 2 domain-containing proteins phosphatidylinositol-3 kinase (PI-3 kinase), Ras guanosine triphosphatase activating protein, phospholipase C-gamma, and a phosphotyrosine phosphatase (Syp) remained at the cell periphery. Restoration of the PI-3 kinase binding sites on F5 completely restored the ability of the receptor to concentrate intracellularly. A PDGFR mutant lacking only PI-3 kinase binding sites failed to concentrate intracellularly. Thus, PI-3 kinase binding sites appear both necessary and sufficient for the normal endocytic trafficking of the activated PDGFR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joly, M -- Kazlauskas, A -- Fay, F S -- Corvera, S -- DK40330/DK/NIDDK NIH HHS/ -- GM48339/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):684-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Medicine, University of Massachusetts Medical School, Worcester 01605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303278" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cell Membrane/metabolism ; Endocytosis ; GTPase-Activating Proteins ; Golgi Apparatus/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Isoenzymes/metabolism ; Mutation ; Phosphatidylinositol 3-Kinases ; Phospholipase C gamma ; Phosphotransferases (Alcohol Group Acceptor)/*metabolism ; Platelet-Derived Growth Factor/pharmacology ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/metabolism ; Proteins/metabolism ; Receptors, Platelet-Derived Growth Factor/genetics/*metabolism ; Tumor Cells, Cultured ; Type C Phospholipases/metabolism ; ras GTPase-Activating Proteins
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  • 36
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    A cell cycle regulator potentially involved in genesis of many tumor types (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-15
    Description: A putative tumor suppressor locus on the short arm of human chromosome 9 has been localized to a region of less than 40 kilobases by means of homozygous deletions in melanoma cell lines. This region contained a gene, Multiple Tumor Suppressor 1 (MTS1), that encodes a previously identified inhibitor (p16) of cyclin-dependent kinase 4. MTS1 was homozygously deleted at high frequency in cell lines derived from tumors of lung, breast, brain, bone, skin, bladder, kidney, ovary, and lymphocyte. Melanoma cell lines that carried at least one copy of MTS1 frequently carried nonsense, missense, or frameshift mutations in the gene. These findings suggest that MTS1 mutations are involved in tumor formation in a wide range of tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kamb, A -- Gruis, N A -- Weaver-Feldhaus, J -- Liu, Q -- Harshman, K -- Tavtigian, S V -- Stockert, E -- Day, R S 3rd -- Johnson, B E -- Skolnick, M H -- CA-48711/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):436-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Myriad Genetics, Inc., Salt Lake City, UT 84108.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153634" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Carrier Proteins/*genetics ; Cell Cycle ; Chromosomes, Human, Pair 9 ; Cosmids ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p16 ; *Cyclin-Dependent Kinases ; Exons ; Gene Deletion ; *Genes, Tumor Suppressor ; Humans ; Introns ; Melanoma/*genetics ; Molecular Sequence Data ; Mutation ; Neoplasms/*genetics ; Protein Kinase Inhibitors ; *Proto-Oncogene Proteins ; Tumor Cells, Cultured
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    Reversal of terminal differentiation mediated by p107 in Rb-/- muscle cells (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-06-03
    Description: The terminal differentiation of mammalian muscle cells requires the tumor suppressor retinoblastoma protein (Rb). Unlike their wild-type counterparts, multinucleated myotubes from mouse cells deficient in Rb (Rb-/-) were induced by serum to re-enter the cell cycle. Development of the myogenic phenotype in Rb-/- cells correlated with increased expression of p107, which interacted with myogenic transcription factors. Serum-induced cell cycle reentry, on the other hand, correlated with decreased p107 expression. Thus, although p107 could substitute for Rb as a cofactor for differentiation, it could not maintain the terminally differentiated state in Rb-/- myotubes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, J W -- Gu, W -- Zhu, L -- Mahdavi, V -- Nadal-Ginard, B -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1467-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197461" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood ; Cell Cycle ; Cell Differentiation ; Cell Line ; Culture Media ; Gene Expression ; Helix-Loop-Helix Motifs ; Humans ; Mice ; Muscles/*cytology/metabolism ; Myogenin/metabolism ; *Nuclear Proteins ; Proteins/genetics/*physiology ; Recombinant Fusion Proteins/metabolism ; Retinoblastoma Protein/genetics/*physiology ; Retinoblastoma-Like Protein p107 ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured
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    Tissue-specific targeting of retroviral vectors through ligand-receptor interactions (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-25
    Description: The development of retroviral vectors that target specific cell types could have important implications for the design of gene therapy strategies. A chimeric protein containing the polypeptide hormone erythropoietin and part of the env protein of ecotropic Moloney murine leukemia virus was engineered into the virus. This murine virus became several times more infectious for murine cells bearing the erythropoietin receptor, and it also became infectious for human cells bearing the erythropoietin receptor. This type of tissue-specific targeting by means of ligand-receptor interactions may have broad applications to a variety of gene delivery systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasahara, N -- Dozy, A M -- Kan, Y W -- AM16666/AM/NIADDK NIH HHS/ -- HL 20985/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1373-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Laboratory Medicine, University of California, San Francisco 94143-0724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973726" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Base Sequence ; Cell Line ; Erythrocytes/chemistry/*virology ; Erythropoietin/genetics/metabolism ; Genetic Therapy/methods ; Genetic Vectors/*genetics/physiology ; HeLa Cells ; Humans ; Ligands ; Mice ; Molecular Sequence Data ; Moloney murine leukemia virus/*genetics/physiology ; Receptors, Erythropoietin/*metabolism ; Receptors, Virus/metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection ; Tumor Cells, Cultured ; Viral Envelope Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 39
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    Binding and suppression of the Myc transcriptional activation domain by p107 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-08
    Description: An amino-terminal transactivation domain is required for Myc to function as a transcription factor controlling cell proliferation, differentiation, and apoptosis. A complementary DNA expression library was screened with a Myc fusion protein to identify proteins interacting with this domain, and a clone encoding the Rb-related p107 protein was isolated. The p107 protein was shown to associate with Myc in vivo and to suppress the activity of the Myc transactivation domain. However, mutant forms of Myc from Burkitt lymphoma cells, which contain sequence alterations in the transactivation domain, were resistant to p107-mediated suppression. Thus, disruption of a regulatory interaction between Myc and p107 may be important in tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, W -- Bhatia, K -- Magrath, I T -- Dang, C V -- Dalla-Favera, R -- CA 37165/CA/NCI NIH HHS/ -- CA 51497/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 8;264(5156):251-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8146655" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; DNA-Binding Proteins/metabolism ; Helix-Loop-Helix Motifs ; Lymphoma, B-Cell ; Mice ; Molecular Sequence Data ; *Nuclear Proteins ; Point Mutation ; Proteins/*metabolism ; Proto-Oncogene Proteins c-myc/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoblastoma-Like Protein p107 ; *Suppression, Genetic ; *Transcription Factors ; *Transcriptional Activation ; Transfection ; Tumor Cells, Cultured
    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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  • 40
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    Rates of p16 (MTS1) mutations in primary tumors with 9p loss (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cairns, P -- Mao, L -- Merlo, A -- Lee, D J -- Schwab, D -- Eby, Y -- Tokino, K -- van der Riet, P -- Blaugrund, J E -- Sidransky, D -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):415-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023167" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/*genetics ; *Chromosome Deletion ; *Chromosomes, Human, Pair 9 ; Codon ; Cyclin-Dependent Kinase Inhibitor p16 ; *Genes, Tumor Suppressor ; Humans ; *Mutation ; Neoplasms/*genetics ; Protein Kinase Inhibitors ; Tumor Cells, Cultured
    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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  • 41
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    Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-03
    Description: The estrogen receptor is a transcription factor which, when bound to estradiol, binds DNA and regulates expression of estrogen-responsive genes. A 160-kilodalton estrogen receptor-associated protein, ERAP160, was identified that exhibits estradiol-dependent binding to the receptor. Mutational analysis of the receptor shows that its ability to activate transcription parallels its ability to bind ERAP160. Antiestrogens are unable to promote ERAP160 binding and can block the estrogen-dependent interaction of the receptor and ERAP160 in a dose-dependent manner. This evidence suggests that ERAP160 may mediate estradiol-dependent transcriptional activation by the estrogen receptor. Furthermore, the ability of antiestrogens to block estrogen receptor-ERAP160 complex formation could account for their therapeutic effects in breast cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halachmi, S -- Marden, E -- Martin, G -- MacKay, H -- Abbondanza, C -- Brown, M -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1455-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Biological and Biomedical Sciences, Harvard Medical School, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197458" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Carrier Proteins/*metabolism ; Cell Line ; Diethylstilbestrol/pharmacology ; Estradiol/*metabolism ; Estrogen Antagonists/*pharmacology ; Humans ; Molecular Sequence Data ; Point Mutation ; Receptors, Estrogen/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Tamoxifen/pharmacology ; *Transcriptional Activation ; Tumor Cells, Cultured
    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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  • 42
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    Specific association of human telomerase activity with immortal cells and cancer (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-23
    Description: Synthesis of DNA at chromosome ends by telomerase may be necessary for indefinite proliferation of human cells. A highly sensitive assay for measuring telomerase activity was developed. In cultured cells representing 18 different human tissues, 98 of 100 immortal and none of 22 mortal populations were positive for telomerase. Similarly, 90 of 101 biopsies representing 12 human tumor types and none of 50 normal somatic tissues were positive. Normal ovaries and testes were positive, but benign tumors such as fibroids were negative. Thus, telomerase appears to be stringently repressed in normal human somatic tissues but reactivated in cancer, where immortal cells are likely required to maintain tumor growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, N W -- Piatyszek, M A -- Prowse, K R -- Harley, C B -- West, M D -- Ho, P L -- Coviello, G M -- Wright, W E -- Weinrich, S L -- Shay, J W -- AG07992/AG/NIA NIH HHS/ -- CA50195/CA/NCI NIH HHS/ -- CA65178/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):2011-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geron Corporation, Menlo Park, CA 94025.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7605428" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Division ; Cell Line ; Cell Line, Transformed/enzymology ; DNA Nucleotidylexotransferase/*metabolism ; Enzyme Activation ; Enzyme Repression ; Female ; Humans ; Male ; Molecular Sequence Data ; Neoplasms/*enzymology ; Ovary/enzymology ; Polymerase Chain Reaction ; Testis/enzymology ; Tumor Cells, Cultured
    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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  • 43
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    Growth-promoting effects of glycine-extended progastrin (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: Peptide alpha amidation is required to produce some hormones, such as gastrin, from their glycine-extended precursors. This terminal posttranslational processing reaction is thought to be essential for the biological activation of many peptide hormones; only amidated gastrin exerts a physiological effect that results in gastric acid secretion. However, both amidated gastrin and glycine-extended gastrin stimulate proliferation of exocrine pancreatic cell line AR4-2J through selective receptors for the substrate and the product, respectively, of peptide alpha amidation. Thus, the amidation reaction may function as a determinant of the specific biological actions of products derived from prohormones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seva, C -- Dickinson, C J -- Yamada, T -- K08-DK-01903/DK/NIDDK NIH HHS/ -- P30-DK-34933/DK/NIDDK NIH HHS/ -- R01-DK-34306/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):410-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Michigan Medical Center, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023165" target="_blank"〉PubMed〈/a〉
    Keywords: Benzodiazepinones/pharmacology ; Binding Sites ; Cell Division/*drug effects ; Gastrins/metabolism/*pharmacology ; Humans ; Indoles/pharmacology ; Meglumine/analogs & derivatives/pharmacology ; Octreotide/pharmacology ; Ornithine Decarboxylase/metabolism ; *Phenylurea Compounds ; Receptors, Cholecystokinin/antagonists & inhibitors ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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