Participation of Tyrosine Phosphorylation in the Cytopathic Effect of Human Immunodeficiency Virus-1
Protein tyrosine phosphorylation is a common mechanism of signaling in pathways that regulate T cell receptor-mediated cell activation, cell proliferation, and the cell cycle. Because human immunodeficiency virus (HIV) is thought to affect normal cell signaling, tyrosine phosphorylation may be assoc...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1992-04, Vol.256 (5056), p.542-545 |
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| creator | Cohen, David I. Tani, Yoshihiko Tian, Huan Boone, Elizabeth Samelson, Lawrence E. Lane, H. Clifford |
| description | Protein tyrosine phosphorylation is a common mechanism of signaling in pathways that regulate T cell receptor-mediated cell activation, cell proliferation, and the cell cycle. Because human immunodeficiency virus (HIV) is thought to affect normal cell signaling, tyrosine phosphorylation may be associated with HIV cytopathicity. In both HIV-infected cells and transfected cells that stably express HIV envelope glycoproteins undergoing HIVgp41-induced cell fusion, a 30-kilodalton protein was phosphorylated on tyrosine with kinetics similar to those of syncytium formation and cell death. When tyrosine phosphorylation was inhibited by the protein tyrosine kinase inhibitor herbimycin A, envelopemediated syncytium formation was coordinately reduced. These studies show that specific intracellular signals, which apparently participate in cytopathicity, are generated by HIV and suggest strategies by which the fusion process might be interrupted. |
| doi_str_mv | 10.1126/science.1570514 |
| format | Article |
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Clifford</creator><creatorcontrib>Cohen, David I. ; Tani, Yoshihiko ; Tian, Huan ; Boone, Elizabeth ; Samelson, Lawrence E. ; Lane, H. Clifford</creatorcontrib><description>Protein tyrosine phosphorylation is a common mechanism of signaling in pathways that regulate T cell receptor-mediated cell activation, cell proliferation, and the cell cycle. Because human immunodeficiency virus (HIV) is thought to affect normal cell signaling, tyrosine phosphorylation may be associated with HIV cytopathicity. In both HIV-infected cells and transfected cells that stably express HIV envelope glycoproteins undergoing HIVgp41-induced cell fusion, a 30-kilodalton protein was phosphorylated on tyrosine with kinetics similar to those of syncytium formation and cell death. When tyrosine phosphorylation was inhibited by the protein tyrosine kinase inhibitor herbimycin A, envelopemediated syncytium formation was coordinately reduced. These studies show that specific intracellular signals, which apparently participate in cytopathicity, are generated by HIV and suggest strategies by which the fusion process might be interrupted.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1570514</identifier><identifier>PMID: 1570514</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Acquired immune deficiency syndrome ; AIDS ; AIDS/HIV ; Benzoquinones ; Biological and medical sciences ; CD4 Antigens - physiology ; Cell Line ; Cell lines ; Cellular biology ; Coculture techniques ; Cultured cells ; Cytopathogenic Effect, Viral - physiology ; Cytopathology ; Fundamental and applied biological sciences. Psychology ; Gels ; HIV ; HIV (Viruses) ; HIV 1 ; HIV Envelope Protein gp41 - genetics ; HIV Envelope Protein gp41 - physiology ; HIV-1 - physiology ; human immunodeficiency virus 1 ; Humans ; Infections ; Inhibition ; Lactams, Macrocyclic ; Microbiology ; Pathology, Cellular ; Phosphoproteins - metabolism ; Phosphorylation ; Physiological aspects ; Protein tyrosine kinase ; Protein-Tyrosine Kinases - antagonists & inhibitors ; Protein-Tyrosine Kinases - metabolism ; Quinones - pharmacology ; Receptors, Antigen, T-Cell - physiology ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Reprography ; Rifabutin - analogs & derivatives ; Signal Transduction - physiology ; T lymphocytes ; T-Lymphocytes - microbiology ; T-Lymphocytes - physiology ; Transfection ; Tyrosine - metabolism ; Viability ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - physiology ; Virology</subject><ispartof>Science (American Association for the Advancement of Science), 1992-04, Vol.256 (5056), p.542-545</ispartof><rights>Copyright 1992 American Association for the Advancement of Science</rights><rights>1992 INIST-CNRS</rights><rights>COPYRIGHT 1992 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1992 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Apr 24, 1992</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c706t-7ff93582203a013ed2c3874747382f63d9900e28e0a11e75449a69057e7d7b083</citedby><cites>FETCH-LOGICAL-c706t-7ff93582203a013ed2c3874747382f63d9900e28e0a11e75449a69057e7d7b083</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2877221$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2877221$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5340542$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1570514$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cohen, David I.</creatorcontrib><creatorcontrib>Tani, Yoshihiko</creatorcontrib><creatorcontrib>Tian, Huan</creatorcontrib><creatorcontrib>Boone, Elizabeth</creatorcontrib><creatorcontrib>Samelson, Lawrence E.</creatorcontrib><creatorcontrib>Lane, H. Clifford</creatorcontrib><title>Participation of Tyrosine Phosphorylation in the Cytopathic Effect of Human Immunodeficiency Virus-1</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Protein tyrosine phosphorylation is a common mechanism of signaling in pathways that regulate T cell receptor-mediated cell activation, cell proliferation, and the cell cycle. Because human immunodeficiency virus (HIV) is thought to affect normal cell signaling, tyrosine phosphorylation may be associated with HIV cytopathicity. In both HIV-infected cells and transfected cells that stably express HIV envelope glycoproteins undergoing HIVgp41-induced cell fusion, a 30-kilodalton protein was phosphorylated on tyrosine with kinetics similar to those of syncytium formation and cell death. When tyrosine phosphorylation was inhibited by the protein tyrosine kinase inhibitor herbimycin A, envelopemediated syncytium formation was coordinately reduced. These studies show that specific intracellular signals, which apparently participate in cytopathicity, are generated by HIV and suggest strategies by which the fusion process might be interrupted.</description><subject>Acquired immune deficiency syndrome</subject><subject>AIDS</subject><subject>AIDS/HIV</subject><subject>Benzoquinones</subject><subject>Biological and medical sciences</subject><subject>CD4 Antigens - physiology</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Cellular biology</subject><subject>Coculture techniques</subject><subject>Cultured cells</subject><subject>Cytopathogenic Effect, Viral - physiology</subject><subject>Cytopathology</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Gels</topic><topic>HIV</topic><topic>HIV (Viruses)</topic><topic>HIV 1</topic><topic>HIV Envelope Protein gp41 - genetics</topic><topic>HIV Envelope Protein gp41 - physiology</topic><topic>HIV-1 - physiology</topic><topic>human immunodeficiency virus 1</topic><topic>Humans</topic><topic>Infections</topic><topic>Inhibition</topic><topic>Lactams, Macrocyclic</topic><topic>Microbiology</topic><topic>Pathology, Cellular</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Physiological aspects</topic><topic>Protein tyrosine kinase</topic><topic>Protein-Tyrosine Kinases - antagonists & inhibitors</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Quinones - pharmacology</topic><topic>Receptors, Antigen, T-Cell - physiology</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Reprography</topic><topic>Rifabutin - analogs & derivatives</topic><topic>Signal Transduction - physiology</topic><topic>T lymphocytes</topic><topic>T-Lymphocytes - microbiology</topic><topic>T-Lymphocytes - physiology</topic><topic>Transfection</topic><topic>Tyrosine - metabolism</topic><topic>Viability</topic><topic>Viral Envelope Proteins - genetics</topic><topic>Viral Envelope Proteins - physiology</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cohen, David I.</creatorcontrib><creatorcontrib>Tani, Yoshihiko</creatorcontrib><creatorcontrib>Tian, Huan</creatorcontrib><creatorcontrib>Boone, Elizabeth</creatorcontrib><creatorcontrib>Samelson, Lawrence E.</creatorcontrib><creatorcontrib>Lane, H. 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In both HIV-infected cells and transfected cells that stably express HIV envelope glycoproteins undergoing HIVgp41-induced cell fusion, a 30-kilodalton protein was phosphorylated on tyrosine with kinetics similar to those of syncytium formation and cell death. When tyrosine phosphorylation was inhibited by the protein tyrosine kinase inhibitor herbimycin A, envelopemediated syncytium formation was coordinately reduced. These studies show that specific intracellular signals, which apparently participate in cytopathicity, are generated by HIV and suggest strategies by which the fusion process might be interrupted.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>1570514</pmid><doi>10.1126/science.1570514</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1992-04, Vol.256 (5056), p.542-545 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743396998 |
| source | MEDLINE; American Association for the Advancement of Science; Jstor Complete Legacy |
| subjects | Acquired immune deficiency syndrome AIDS AIDS/HIV Benzoquinones Biological and medical sciences CD4 Antigens - physiology Cell Line Cell lines Cellular biology Coculture techniques Cultured cells Cytopathogenic Effect, Viral - physiology Cytopathology Fundamental and applied biological sciences. Psychology Gels HIV HIV (Viruses) HIV 1 HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp41 - physiology HIV-1 - physiology human immunodeficiency virus 1 Humans Infections Inhibition Lactams, Macrocyclic Microbiology Pathology, Cellular Phosphoproteins - metabolism Phosphorylation Physiological aspects Protein tyrosine kinase Protein-Tyrosine Kinases - antagonists & inhibitors Protein-Tyrosine Kinases - metabolism Quinones - pharmacology Receptors, Antigen, T-Cell - physiology Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Reprography Rifabutin - analogs & derivatives Signal Transduction - physiology T lymphocytes T-Lymphocytes - microbiology T-Lymphocytes - physiology Transfection Tyrosine - metabolism Viability Viral Envelope Proteins - genetics Viral Envelope Proteins - physiology Virology |
| title | Participation of Tyrosine Phosphorylation in the Cytopathic Effect of Human Immunodeficiency Virus-1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T20%3A11%3A56IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Participation%20of%20Tyrosine%20Phosphorylation%20in%20the%20Cytopathic%20Effect%20of%20Human%20Immunodeficiency%20Virus-1&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Cohen,%20David%20I.&rft.date=1992-04-24&rft.volume=256&rft.issue=5056&rft.spage=542&rft.epage=545&rft.pages=542-545&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.1570514&rft_dat=%3Cgale_proqu%3EA12127252%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213548454&rft_id=info:pmid/1570514&rft_galeid=A12127252&rft_jstor_id=2877221&rfr_iscdi=true |