An Interleukin-4-Induced Transcription Factor: IL-4 Stat
Interleukin-4 (IL-4) is an immunomodulatory cytokine secreted by activated T lymphocytes, basophils, and mast cells. It plays an important role in modulating the balance of T helper (Th) cell subsets, favoring expansion of the Th2 lineage relative to Th1. Imbalance of these T lymphocyte subsets has...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1994-09, Vol.265 (5179), p.1701-1706 |
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| creator | Hou, Jinzhao Schindler, Ulrike Henzel, William J. Ho, Tze Chun Brasseur, Mike McKnight, Steven L. |
| description | Interleukin-4 (IL-4) is an immunomodulatory cytokine secreted by activated T lymphocytes, basophils, and mast cells. It plays an important role in modulating the balance of T helper (Th) cell subsets, favoring expansion of the Th2 lineage relative to Th1. Imbalance of these T lymphocyte subsets has been implicated in immunological diseases including allergy, inflammation, and autoimmune disease. IL-4 may mediate its biological effects, at least in part, by activating a tyrosine-phosphorylated DNA binding protein. This protein has now been purified and its encoding gene cloned. Examination of the primary amino acid sequence of this protein indicates that it is a member of the signal transducers and activators of transcription (Stat) family of DNA binding proteins, hereby designated IL-4 Stat. Study of the inhibitory activities of phosphotyrosine-containing peptides derived from the intracellular domain of the IL-4 receptor provided evidence for direct coupling of receptor and transcription factor during the IL-4 Stat activation cycle. Such observations indicate that IL-4 Stat has the same functional domain for both receptor coupling and dimerization. |
| doi_str_mv | 10.1126/science.8085155 |
| format | Article |
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It plays an important role in modulating the balance of T helper (Th) cell subsets, favoring expansion of the Th2 lineage relative to Th1. Imbalance of these T lymphocyte subsets has been implicated in immunological diseases including allergy, inflammation, and autoimmune disease. IL-4 may mediate its biological effects, at least in part, by activating a tyrosine-phosphorylated DNA binding protein. This protein has now been purified and its encoding gene cloned. Examination of the primary amino acid sequence of this protein indicates that it is a member of the signal transducers and activators of transcription (Stat) family of DNA binding proteins, hereby designated IL-4 Stat. Study of the inhibitory activities of phosphotyrosine-containing peptides derived from the intracellular domain of the IL-4 receptor provided evidence for direct coupling of receptor and transcription factor during the IL-4 Stat activation cycle. Such observations indicate that IL-4 Stat has the same functional domain for both receptor coupling and dimerization.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.8085155</identifier><identifier>PMID: 8085155</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; B lymphocytes ; Base Sequence ; Biochemistry ; Biological and medical sciences ; Cell Line ; Cell physiology ; cloning ; Cloning, Molecular ; Cross-Linking Reagents ; Crosslinking ; Deoxyribonucleic acid ; Dimerization ; Dimers ; DNA ; DNA - metabolism ; DNA binding proteins ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - isolation & purification ; DNA-Binding Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; gene expression ; Genes ; Humans ; IL-4 Stat protein ; Immune response ; Immune response regulation ; Immunity (Disease) ; induction ; Interleukin-4 ; Interleukin-4 - pharmacology ; Interleukin-4 Receptor alpha Subunit ; man ; Messenger RNA ; Models, Biological ; Molecular and cellular biology ; Molecular Sequence Data ; Monocytes - metabolism ; Phosphopeptides - metabolism ; Phosphopeptides - pharmacology ; Phosphorylation ; Polymers ; prediction ; Proteins ; Receptors ; Receptors, Cell Surface ; Receptors, Interleukin-4 ; Receptors, Mitogen - metabolism ; Regulation ; Responses to growth factors, tumor promotors, other factors ; Somatic cells ; STAT6 Transcription Factor ; Trans-Activators - chemistry ; Trans-Activators - genetics ; Trans-Activators - isolation & purification ; Trans-Activators - metabolism ; transcription factors ; Transcription Factors - chemistry ; Transcription Factors - genetics ; Transcription Factors - metabolism</subject><ispartof>Science (American Association for the Advancement of Science), 1994-09, Vol.265 (5179), p.1701-1706</ispartof><rights>Copyright 1994 American Association for the Advancement of Science</rights><rights>1994 INIST-CNRS</rights><rights>COPYRIGHT 1994 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1994 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Sep 16, 1994</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c741t-a1d2c6f312896247e0e203631b463c552ab9902c3b04cf09929f3c19f5aaf2b13</citedby><cites>FETCH-LOGICAL-c741t-a1d2c6f312896247e0e203631b463c552ab9902c3b04cf09929f3c19f5aaf2b13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2884613$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2884613$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,777,781,800,2871,2872,27905,27906,57998,58231</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4215334$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8085155$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hou, Jinzhao</creatorcontrib><creatorcontrib>Schindler, Ulrike</creatorcontrib><creatorcontrib>Henzel, William J.</creatorcontrib><creatorcontrib>Ho, Tze Chun</creatorcontrib><creatorcontrib>Brasseur, Mike</creatorcontrib><creatorcontrib>McKnight, Steven L.</creatorcontrib><title>An Interleukin-4-Induced Transcription Factor: IL-4 Stat</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Interleukin-4 (IL-4) is an immunomodulatory cytokine secreted by activated T lymphocytes, basophils, and mast cells. It plays an important role in modulating the balance of T helper (Th) cell subsets, favoring expansion of the Th2 lineage relative to Th1. Imbalance of these T lymphocyte subsets has been implicated in immunological diseases including allergy, inflammation, and autoimmune disease. IL-4 may mediate its biological effects, at least in part, by activating a tyrosine-phosphorylated DNA binding protein. This protein has now been purified and its encoding gene cloned. Examination of the primary amino acid sequence of this protein indicates that it is a member of the signal transducers and activators of transcription (Stat) family of DNA binding proteins, hereby designated IL-4 Stat. Study of the inhibitory activities of phosphotyrosine-containing peptides derived from the intracellular domain of the IL-4 receptor provided evidence for direct coupling of receptor and transcription factor during the IL-4 Stat activation cycle. Such observations indicate that IL-4 Stat has the same functional domain for both receptor coupling and dimerization.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>B lymphocytes</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>cloning</subject><subject>Cloning, Molecular</subject><subject>Cross-Linking Reagents</subject><subject>Crosslinking</subject><subject>Deoxyribonucleic acid</subject><subject>Dimerization</subject><subject>Dimers</subject><subject>DNA</subject><subject>DNA - metabolism</subject><subject>DNA binding proteins</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - isolation & purification</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. 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proteins</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - isolation & purification</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene expression</topic><topic>Genes</topic><topic>Humans</topic><topic>IL-4 Stat protein</topic><topic>Immune response</topic><topic>Immune response regulation</topic><topic>Immunity (Disease)</topic><topic>induction</topic><topic>Interleukin-4</topic><topic>Interleukin-4 - pharmacology</topic><topic>Interleukin-4 Receptor alpha Subunit</topic><topic>man</topic><topic>Messenger RNA</topic><topic>Models, Biological</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Monocytes - metabolism</topic><topic>Phosphopeptides - metabolism</topic><topic>Phosphopeptides - pharmacology</topic><topic>Phosphorylation</topic><topic>Polymers</topic><topic>prediction</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Receptors, Cell Surface</topic><topic>Receptors, Interleukin-4</topic><topic>Receptors, Mitogen - metabolism</topic><topic>Regulation</topic><topic>Responses to growth factors, tumor promotors, other 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(American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1994-09-16</date><risdate>1994</risdate><volume>265</volume><issue>5179</issue><spage>1701</spage><epage>1706</epage><pages>1701-1706</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Interleukin-4 (IL-4) is an immunomodulatory cytokine secreted by activated T lymphocytes, basophils, and mast cells. It plays an important role in modulating the balance of T helper (Th) cell subsets, favoring expansion of the Th2 lineage relative to Th1. Imbalance of these T lymphocyte subsets has been implicated in immunological diseases including allergy, inflammation, and autoimmune disease. IL-4 may mediate its biological effects, at least in part, by activating a tyrosine-phosphorylated DNA binding protein. This protein has now been purified and its encoding gene cloned. Examination of the primary amino acid sequence of this protein indicates that it is a member of the signal transducers and activators of transcription (Stat) family of DNA binding proteins, hereby designated IL-4 Stat. Study of the inhibitory activities of phosphotyrosine-containing peptides derived from the intracellular domain of the IL-4 receptor provided evidence for direct coupling of receptor and transcription factor during the IL-4 Stat activation cycle. Such observations indicate that IL-4 Stat has the same functional domain for both receptor coupling and dimerization.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>8085155</pmid><doi>10.1126/science.8085155</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1994-09, Vol.265 (5179), p.1701-1706 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76708859 |
| source | MEDLINE; Science Magazine; Jstor Complete Legacy |
| subjects | Amino Acid Sequence Amino acids B lymphocytes Base Sequence Biochemistry Biological and medical sciences Cell Line Cell physiology cloning Cloning, Molecular Cross-Linking Reagents Crosslinking Deoxyribonucleic acid Dimerization Dimers DNA DNA - metabolism DNA binding proteins DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology gene expression Genes Humans IL-4 Stat protein Immune response Immune response regulation Immunity (Disease) induction Interleukin-4 Interleukin-4 - pharmacology Interleukin-4 Receptor alpha Subunit man Messenger RNA Models, Biological Molecular and cellular biology Molecular Sequence Data Monocytes - metabolism Phosphopeptides - metabolism Phosphopeptides - pharmacology Phosphorylation Polymers prediction Proteins Receptors Receptors, Cell Surface Receptors, Interleukin-4 Receptors, Mitogen - metabolism Regulation Responses to growth factors, tumor promotors, other factors Somatic cells STAT6 Transcription Factor Trans-Activators - chemistry Trans-Activators - genetics Trans-Activators - isolation & purification Trans-Activators - metabolism transcription factors Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism |
| title | An Interleukin-4-Induced Transcription Factor: IL-4 Stat |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T14%3A42%3A40IST&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=An%20Interleukin-4-Induced%20Transcription%20Factor:%20IL-4%20Stat&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Hou,%20Jinzhao&rft.date=1994-09-16&rft.volume=265&rft.issue=5179&rft.spage=1701&rft.epage=1706&rft.pages=1701-1706&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.8085155&rft_dat=%3Cgale_proqu%3EA15755885%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=213548252&rft_id=info:pmid/8085155&rft_galeid=A15755885&rft_jstor_id=2884613&rfr_iscdi=true |