Interleukin-1β activates a short STAT-3 isoform in clonal insulin-secreting cells
Identifieur interne : 000D73 ( Main/Corpus ); précédent : 000D72; suivant : 000D74Interleukin-1β activates a short STAT-3 isoform in clonal insulin-secreting cells
Auteurs : Nicholas M. Morton ; Rolf P. De Groot ; Michael A. Cawthorne ; Valur EmilssonSource :
- FEBS Letters [ 0014-5793 ] ; 1998.
Abstract
Interleukin-1β (IL-1β) is a potent inflammatory cytokine involved in type 1 diabetes and acts through defined IL-1β signaling pathways. In the present work we describe induction of DNA binding activity to signal transducer and activator of transcription (STAT) in response to IL-1β in clonal insulin-secreting cells. Moreover, IL-1β activates a short isoform of STAT-3 that potently stimulates transcription. Immunoprecipitation studies reveal an interaction between the activated STAT-3 and the IL-1 receptor accessory protein indicating an association between the two signaling pathways. This may be a novel point of transduction cross talk and an additional mechanism utilised by IL-1β in the pancreatic β-cell during the process of type 1 diabetes.
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DOI: 10.1016/S0014-5793(98)01623-8
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Cawthorne</name><affiliation><mods:affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</mods:affiliation></affiliation></author><author><name sortKey="Emilsson, Valur" sort="Emilsson, Valur" uniqKey="Emilsson V" first="Valur" last="Emilsson">Valur Emilsson</name><affiliation><mods:affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</mods:affiliation></affiliation><affiliation><mods:affiliation>Corresponding author. Fax: (44) (1280) 822245. 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Morton</name><affiliation><mods:affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</mods:affiliation></affiliation></author><author><name sortKey="De Groot, Rolf P" sort="De Groot, Rolf P" uniqKey="De Groot R" first="Rolf P." last="De Groot">Rolf P. De Groot</name><affiliation><mods:affiliation>Department of Pulmonary Diseases, University Hospital Utrecht, P.O. Box 85500, 3508 GA Utrecht, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Cawthorne, Michael A" sort="Cawthorne, Michael A" uniqKey="Cawthorne M" first="Michael A." last="Cawthorne">Michael A. Cawthorne</name><affiliation><mods:affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</mods:affiliation></affiliation></author><author><name sortKey="Emilsson, Valur" sort="Emilsson, Valur" uniqKey="Emilsson V" first="Valur" last="Emilsson">Valur Emilsson</name><affiliation><mods:affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</mods:affiliation></affiliation><affiliation><mods:affiliation>Corresponding author. Fax: (44) (1280) 822245. E-mail: valur.emilsson@buckingham.ac.uk</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">FEBS Letters</title><title level="j" type="abbrev">FEBS</title><idno type="ISSN">0014-5793</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">442</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="57">57</biblScope><biblScope unit="page" to="60">60</biblScope></imprint><idno type="ISSN">0014-5793</idno></series><idno type="istex">D7F2399CD8FED943471BB11ED805B8AFB48B84A4</idno><idno type="DOI">10.1016/S0014-5793(98)01623-8</idno><idno type="PII">S0014-5793(98)01623-8</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0014-5793</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Interleukin-1β (IL-1β) is a potent inflammatory cytokine involved in type 1 diabetes and acts through defined IL-1β signaling pathways. In the present work we describe induction of DNA binding activity to signal transducer and activator of transcription (STAT) in response to IL-1β in clonal insulin-secreting cells. Moreover, IL-1β activates a short isoform of STAT-3 that potently stimulates transcription. Immunoprecipitation studies reveal an interaction between the activated STAT-3 and the IL-1 receptor accessory protein indicating an association between the two signaling pathways. This may be a novel point of transduction cross talk and an additional mechanism utilised by IL-1β in the pancreatic β-cell during the process of type 1 diabetes.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Nicholas M. Morton</name><affiliations><json:string>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</json:string></affiliations></json:item><json:item><name>Rolf P. de Groot</name><affiliations><json:string>Department of Pulmonary Diseases, University Hospital Utrecht, P.O. Box 85500, 3508 GA Utrecht, The Netherlands</json:string></affiliations></json:item><json:item><name>Michael A. Cawthorne</name><affiliations><json:string>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</json:string></affiliations></json:item><json:item><name>Valur Emilsson</name><affiliations><json:string>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</json:string><json:string>Corresponding author. Fax: (44) (1280) 822245. E-mail: valur.emilsson@buckingham.ac.uk</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Interleukin 1β</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Signal transducer and activator of transcription 3</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Clonal β-cell</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Interleukin 1 receptor accessory protein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>IL-1β, interleukin-1β</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>IL-1RI, interleukin-1 receptor type I</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>IL-1RAcP, interleukin-1 receptor accessory protein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>STAT, signal transducer and activator of transcription</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>JAK, Janus kinase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>IBMX, isobutyl methyl xanthine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>GAS, interferon-γ-activated sequence</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CAT, chloramphenicol acetyltransferase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>IRE, interferon-γ/interleukin-6 response element</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>ICAM, intercellular adhesion molecule</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>IRF-1, interferon response factor-1</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>SIE, SIS inducible element</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cAMP, cyclic adenosine monophosphate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>GLP-1, glucagon-like peptide 1</value></json:item></subject><language><json:string>eng</json:string></language><abstract>Interleukin-1β (IL-1β) is a potent inflammatory cytokine involved in type 1 diabetes and acts through defined IL-1β signaling pathways. In the present work we describe induction of DNA binding activity to signal transducer and activator of transcription (STAT) in response to IL-1β in clonal insulin-secreting cells. Moreover, IL-1β activates a short isoform of STAT-3 that potently stimulates transcription. Immunoprecipitation studies reveal an interaction between the activated STAT-3 and the IL-1 receptor accessory protein indicating an association between the two signaling pathways. This may be a novel point of transduction cross talk and an additional mechanism utilised by IL-1β in the pancreatic β-cell during the process of type 1 diabetes.</abstract><qualityIndicators><score>4.405</score><pdfVersion>1.2</pdfVersion><pdfPageSize>588 x 804 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>18</keywordCount><abstractCharCount>752</abstractCharCount><pdfWordCount>3097</pdfWordCount><pdfCharCount>19181</pdfCharCount><pdfPageCount>4</pdfPageCount><abstractWordCount>109</abstractWordCount></qualityIndicators><title>Interleukin-1β activates a short STAT-3 isoform in clonal insulin-secreting cells</title><pii><json:string>S0014-5793(98)01623-8</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>442</volume><pii><json:string>S0014-5793(00)X0201-3</json:string></pii><pages><last>60</last><first>57</first></pages><issn><json:string>0014-5793</json:string></issn><issue>1</issue><genre></genre><language><json:string>unknown</json:string></language><title>FEBS Letters</title><publicationDate>1999</publicationDate></host><categories><wos><json:string>BIOCHEMISTRY & MOLECULAR BIOLOGY</json:string><json:string>BIOPHYSICS</json:string><json:string>CELL BIOLOGY</json:string></wos></categories><publicationDate>1998</publicationDate><copyrightDate>1999</copyrightDate><doi><json:string>10.1016/S0014-5793(98)01623-8</json:string></doi><id>D7F2399CD8FED943471BB11ED805B8AFB48B84A4</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/D7F2399CD8FED943471BB11ED805B8AFB48B84A4/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/D7F2399CD8FED943471BB11ED805B8AFB48B84A4/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/D7F2399CD8FED943471BB11ED805B8AFB48B84A4/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Interleukin-1β activates a short STAT-3 isoform in clonal insulin-secreting cells</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1999</date></publicationStmt><notesStmt><note type="content">Fig. 1: IL-1β induces time- and dose-dependent DNA binding activity on the IRF-1 STAT consensus. IL-1β (50 pg/ml)-induced STAT DNA binding to the IRF-1 is observed by 5 min, peaks at 15–20 min and returns to basal by 30 min (upper panel). The STAT DNA binding is observed over the concentration range of 0.5–500 pg/ml (upper panel). Supershift analyses of IL-1β (50 pg/ml)-induced STAT DNA binding to the IRF-1 with C-terminal antibodies to STAT-1, -2, -3, -5a, -5b and -6 are shown in the bottom panel. The arrows point at the STAT DNA complex.</note><note type="content">Fig. 2: IL-1β induces STAT-3 DNA binding activity. An appropriate time (15 min) and dose of IL-1β (50 pg/ml) was selected from results on the IRF-1 probe, to study the effects of IL-1β on m67SIE binding activity. IL-1β (50 pg/ml) induced the STAT DNA binding activity of the m67SIE probe that is known to bind STAT-3 avidly. The arrow points at the STAT DNA band shift.</note><note type="content">Fig. 3: IL-1β causes a time-dependent induction of a STAT-3 immunoreactive protein in RINm5F nuclear extracts. RINm5F were pre-incubated in serum-free medium for 24 h and then exposed to IL-1β (50 pg/ml) for the times indicated below the lanes. Time-dependent induction of a protein complex (∼67 kDa) that cross-reacts with a phospho (Y705) STAT-3 antibody. Time-dependent induction of a STAT-3 N-terminal immunoreactive protein that co-migrates with the tyrosine phosphorylated STAT-3 species at approximately 67 kDa.</note><note type="content">Fig. 4: IL-1β induces transcriptional activation from the IRE-CAT. RINm5F cells were transiently transfected with reporter plasmids driven by the STAT consensus promoter element indicated below the axis. After a period of serum starvation, the RINm5F were exposed to IL-1β (50 pg/ml) for 12 h and then assessed for induction of CAT activity. The IRE-CAT reporter construct was strongly induced whereas a slight induction at the GAS-CAT and no induction from a control plasmid pBL or βCAS-CAT constructs were observed.</note><note type="content">Fig. 5: IL-1β induces the interaction of activated STAT-3 with the IL-1RAcP. RINm5F cells were treated with IL-1β (50 pg/ml) for the indicated time and then lysed. Immunoprecipitation was performed on whole cell lysates with an anti-phospho STAT-3 Y705 antibody. Identical immunoprecipitates were then probed with either an N-terminal directed STAT-3 antibody or an anti-IL-1RAcP monoclonal antibody on separate gels. IL-1β treatment increases the association with a peak at 2 min that rapidly declines by 10 min.</note><note type="content">Fig. 6: Increasing intracellular cAMP attenuates the IL-1β-inducible STAT DNA binding. The cells were pre-incubated in serum-free medium and then given a second pre-incubation for 15 min with 10 nM GLP-1 or 10 μM forskolin/50 μM IBMX. IL-1β (50 pg/ml) was then added in the presence of the compounds and the nuclear extracts isolated. The nuclear extracts were then incubated with [γ-32P]ATP end-labelled m67SIE probe and the complexes separated on 4% PAGE gels and analysed by autoradiography.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Interleukin-1β activates a short STAT-3 isoform in clonal insulin-secreting cells</title><author><persName><forename type="first">Nicholas M.</forename><surname>Morton</surname></persName><affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</affiliation></author><author><persName><forename type="first">Rolf P.</forename><surname>de Groot</surname></persName><affiliation>Department of Pulmonary Diseases, University Hospital Utrecht, P.O. Box 85500, 3508 GA Utrecht, The Netherlands</affiliation></author><author><persName><forename type="first">Michael A.</forename><surname>Cawthorne</surname></persName><affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</affiliation></author><author><persName><forename type="first">Valur</forename><surname>Emilsson</surname></persName><email>valur.emilsson@buckingham.ac.uk</email><affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</affiliation></author></analytic><monogr><title level="j">FEBS Letters</title><title level="j" type="abbrev">FEBS</title><idno type="pISSN">0014-5793</idno><idno type="PII">S0014-5793(00)X0201-3</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998"></date><biblScope unit="volume">442</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="57">57</biblScope><biblScope unit="page" to="60">60</biblScope></imprint></monogr><idno type="istex">D7F2399CD8FED943471BB11ED805B8AFB48B84A4</idno><idno type="DOI">10.1016/S0014-5793(98)01623-8</idno><idno type="PII">S0014-5793(98)01623-8</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1999</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Interleukin-1β (IL-1β) is a potent inflammatory cytokine involved in type 1 diabetes and acts through defined IL-1β signaling pathways. In the present work we describe induction of DNA binding activity to signal transducer and activator of transcription (STAT) in response to IL-1β in clonal insulin-secreting cells. Moreover, IL-1β activates a short isoform of STAT-3 that potently stimulates transcription. Immunoprecipitation studies reveal an interaction between the activated STAT-3 and the IL-1 receptor accessory protein indicating an association between the two signaling pathways. This may be a novel point of transduction cross talk and an additional mechanism utilised by IL-1β in the pancreatic β-cell during the process of type 1 diabetes.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Interleukin 1β</term></item><item><term>Signal transducer and activator of transcription 3</term></item><item><term>Clonal β-cell</term></item><item><term>Interleukin 1 receptor accessory protein</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>IL-1β, interleukin-1β</term></item><item><term>IL-1RI, interleukin-1 receptor type I</term></item><item><term>IL-1RAcP, interleukin-1 receptor accessory protein</term></item><item><term>STAT, signal transducer and activator of transcription</term></item><item><term>JAK, Janus kinase</term></item><item><term>IBMX, isobutyl methyl xanthine</term></item><item><term>GAS, interferon-γ-activated sequence</term></item><item><term>CAT, chloramphenicol acetyltransferase</term></item><item><term>IRE, interferon-γ/interleukin-6 response element</term></item><item><term>ICAM, intercellular adhesion molecule</term></item><item><term>IRF-1, interferon response factor-1</term></item><item><term>SIE, SIS inducible element</term></item><item><term>cAMP, cyclic adenosine monophosphate</term></item><item><term>GLP-1, glucagon-like peptide 1</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998-11-13">Received</change><change when="1998">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/D7F2399CD8FED943471BB11ED805B8AFB48B84A4/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"><istex:entity SYSTEM="gr1" NDATA="IMAGE" name="gr1"></istex:entity><istex:entity SYSTEM="gr2" NDATA="IMAGE" name="gr2"></istex:entity><istex:entity SYSTEM="gr3" NDATA="IMAGE" name="gr3"></istex:entity><istex:entity SYSTEM="gr4" NDATA="IMAGE" name="gr4"></istex:entity><istex:entity SYSTEM="gr5" NDATA="IMAGE" name="gr5"></istex:entity><istex:entity SYSTEM="gr6" NDATA="IMAGE" name="gr6"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>FEBS</jid><aid>21368</aid><ce:pii>S0014-5793(98)01623-8</ce:pii><ce:doi>10.1016/S0014-5793(98)01623-8</ce:doi><ce:copyright year="1999" type="society">Federation of European Biochemical Societies</ce:copyright></item-info><head><ce:title>Interleukin-1β activates a short STAT-3 isoform in clonal insulin-secreting cells</ce:title><ce:author-group><ce:author><ce:given-name>Nicholas M.</ce:given-name><ce:surname>Morton</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref></ce:author><ce:author><ce:given-name>Rolf P.</ce:given-name><ce:surname>de Groot</ce:surname><ce:cross-ref refid="AFF2">b</ce:cross-ref></ce:author><ce:author><ce:given-name>Michael A.</ce:given-name><ce:surname>Cawthorne</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref></ce:author><ce:author><ce:given-name>Valur</ce:given-name><ce:surname>Emilsson</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref><ce:cross-ref refid="CORR1">*</ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Pulmonary Diseases, University Hospital Utrecht, P.O. Box 85500, 3508 GA Utrecht, The Netherlands</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Corresponding author. Fax: (44) (1280) 822245. E-mail: valur.emilsson@buckingham.ac.uk</ce:text></ce:correspondence></ce:author-group><ce:date-received day="13" month="11" year="1998"></ce:date-received><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Interleukin-1β (IL-1β) is a potent inflammatory cytokine involved in type 1 diabetes and acts through defined IL-1β signaling pathways. In the present work we describe induction of DNA binding activity to signal transducer and activator of transcription (STAT) in response to IL-1β in clonal insulin-secreting cells. Moreover, IL-1β activates a short isoform of STAT-3 that potently stimulates transcription. Immunoprecipitation studies reveal an interaction between the activated STAT-3 and the IL-1 receptor accessory protein indicating an association between the two signaling pathways. This may be a novel point of transduction cross talk and an additional mechanism utilised by IL-1β in the pancreatic β-cell during the process of type 1 diabetes.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Interleukin 1β</ce:text></ce:keyword><ce:keyword><ce:text>Signal transducer and activator of transcription 3</ce:text></ce:keyword><ce:keyword><ce:text>Clonal β-cell</ce:text></ce:keyword><ce:keyword><ce:text>Interleukin 1 receptor accessory protein</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>IL-1β, interleukin-1β</ce:text></ce:keyword><ce:keyword><ce:text>IL-1RI, interleukin-1 receptor type I</ce:text></ce:keyword><ce:keyword><ce:text>IL-1RAcP, interleukin-1 receptor accessory protein</ce:text></ce:keyword><ce:keyword><ce:text>STAT, signal transducer and activator of transcription</ce:text></ce:keyword><ce:keyword><ce:text>JAK, Janus kinase</ce:text></ce:keyword><ce:keyword><ce:text>IBMX, isobutyl methyl xanthine</ce:text></ce:keyword><ce:keyword><ce:text>GAS, interferon-γ-activated sequence</ce:text></ce:keyword><ce:keyword><ce:text>CAT, chloramphenicol acetyltransferase</ce:text></ce:keyword><ce:keyword><ce:text>IRE, interferon-γ/interleukin-6 response element</ce:text></ce:keyword><ce:keyword><ce:text>ICAM, intercellular adhesion molecule</ce:text></ce:keyword><ce:keyword><ce:text>IRF-1, interferon response factor-1</ce:text></ce:keyword><ce:keyword><ce:text>SIE, SIS inducible element</ce:text></ce:keyword><ce:keyword><ce:text>cAMP, cyclic adenosine monophosphate</ce:text></ce:keyword><ce:keyword><ce:text>GLP-1, glucagon-like peptide 1</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Interleukin-1β activates a short STAT-3 isoform in clonal insulin-secreting cells</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Interleukin-1β activates a short STAT-3 isoform in clonal insulin-secreting cells</title></titleInfo><name type="personal"><namePart type="given">Nicholas M.</namePart><namePart type="family">Morton</namePart><affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Rolf P.</namePart><namePart type="family">de Groot</namePart><affiliation>Department of Pulmonary Diseases, University Hospital Utrecht, P.O. Box 85500, 3508 GA Utrecht, The Netherlands</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Michael A.</namePart><namePart type="family">Cawthorne</namePart><affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Valur</namePart><namePart type="family">Emilsson</namePart><affiliation>Clore Laboratory, The University of Buckingham, Hunter Street, Buckingham MK18 1EG, UK</affiliation><affiliation>Corresponding author. Fax: (44) (1280) 822245. E-mail: valur.emilsson@buckingham.ac.uk</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued><dateCaptured encoding="w3cdtf">1998-11-13</dateCaptured><copyrightDate encoding="w3cdtf">1999</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Interleukin-1β (IL-1β) is a potent inflammatory cytokine involved in type 1 diabetes and acts through defined IL-1β signaling pathways. In the present work we describe induction of DNA binding activity to signal transducer and activator of transcription (STAT) in response to IL-1β in clonal insulin-secreting cells. Moreover, IL-1β activates a short isoform of STAT-3 that potently stimulates transcription. Immunoprecipitation studies reveal an interaction between the activated STAT-3 and the IL-1 receptor accessory protein indicating an association between the two signaling pathways. This may be a novel point of transduction cross talk and an additional mechanism utilised by IL-1β in the pancreatic β-cell during the process of type 1 diabetes.</abstract><note type="content">Fig. 1: IL-1β induces time- and dose-dependent DNA binding activity on the IRF-1 STAT consensus. IL-1β (50 pg/ml)-induced STAT DNA binding to the IRF-1 is observed by 5 min, peaks at 15–20 min and returns to basal by 30 min (upper panel). The STAT DNA binding is observed over the concentration range of 0.5–500 pg/ml (upper panel). Supershift analyses of IL-1β (50 pg/ml)-induced STAT DNA binding to the IRF-1 with C-terminal antibodies to STAT-1, -2, -3, -5a, -5b and -6 are shown in the bottom panel. The arrows point at the STAT DNA complex.</note><note type="content">Fig. 2: IL-1β induces STAT-3 DNA binding activity. An appropriate time (15 min) and dose of IL-1β (50 pg/ml) was selected from results on the IRF-1 probe, to study the effects of IL-1β on m67SIE binding activity. IL-1β (50 pg/ml) induced the STAT DNA binding activity of the m67SIE probe that is known to bind STAT-3 avidly. The arrow points at the STAT DNA band shift.</note><note type="content">Fig. 3: IL-1β causes a time-dependent induction of a STAT-3 immunoreactive protein in RINm5F nuclear extracts. RINm5F were pre-incubated in serum-free medium for 24 h and then exposed to IL-1β (50 pg/ml) for the times indicated below the lanes. Time-dependent induction of a protein complex (∼67 kDa) that cross-reacts with a phospho (Y705) STAT-3 antibody. Time-dependent induction of a STAT-3 N-terminal immunoreactive protein that co-migrates with the tyrosine phosphorylated STAT-3 species at approximately 67 kDa.</note><note type="content">Fig. 4: IL-1β induces transcriptional activation from the IRE-CAT. RINm5F cells were transiently transfected with reporter plasmids driven by the STAT consensus promoter element indicated below the axis. After a period of serum starvation, the RINm5F were exposed to IL-1β (50 pg/ml) for 12 h and then assessed for induction of CAT activity. The IRE-CAT reporter construct was strongly induced whereas a slight induction at the GAS-CAT and no induction from a control plasmid pBL or βCAS-CAT constructs were observed.</note><note type="content">Fig. 5: IL-1β induces the interaction of activated STAT-3 with the IL-1RAcP. RINm5F cells were treated with IL-1β (50 pg/ml) for the indicated time and then lysed. Immunoprecipitation was performed on whole cell lysates with an anti-phospho STAT-3 Y705 antibody. Identical immunoprecipitates were then probed with either an N-terminal directed STAT-3 antibody or an anti-IL-1RAcP monoclonal antibody on separate gels. IL-1β treatment increases the association with a peak at 2 min that rapidly declines by 10 min.</note><note type="content">Fig. 6: Increasing intracellular cAMP attenuates the IL-1β-inducible STAT DNA binding. The cells were pre-incubated in serum-free medium and then given a second pre-incubation for 15 min with 10 nM GLP-1 or 10 μM forskolin/50 μM IBMX. IL-1β (50 pg/ml) was then added in the presence of the compounds and the nuclear extracts isolated. The nuclear extracts were then incubated with [γ-32P]ATP end-labelled m67SIE probe and the complexes separated on 4% PAGE gels and analysed by autoradiography.</note><subject><genre>Keywords</genre><topic>Interleukin 1β</topic><topic>Signal transducer and activator of transcription 3</topic><topic>Clonal β-cell</topic><topic>Interleukin 1 receptor accessory protein</topic></subject><subject><genre>Abbreviations</genre><topic>IL-1β, interleukin-1β</topic><topic>IL-1RI, interleukin-1 receptor type I</topic><topic>IL-1RAcP, interleukin-1 receptor accessory protein</topic><topic>STAT, signal transducer and activator of transcription</topic><topic>JAK, Janus kinase</topic><topic>IBMX, isobutyl methyl xanthine</topic><topic>GAS, interferon-γ-activated sequence</topic><topic>CAT, chloramphenicol acetyltransferase</topic><topic>IRE, interferon-γ/interleukin-6 response element</topic><topic>ICAM, intercellular adhesion molecule</topic><topic>IRF-1, interferon response factor-1</topic><topic>SIE, SIS inducible element</topic><topic>cAMP, cyclic adenosine monophosphate</topic><topic>GLP-1, glucagon-like peptide 1</topic></subject><relatedItem type="host"><titleInfo><title>FEBS Letters</title></titleInfo><titleInfo type="abbreviated"><title>FEBS</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19990108</dateIssued></originInfo><identifier type="ISSN">0014-5793</identifier><identifier type="PII">S0014-5793(00)X0201-3</identifier><part><date>19990108</date><detail type="volume"><number>442</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>122</end></extent><extent unit="pages"><start>57</start><end>60</end></extent></part></relatedItem><identifier type="istex">D7F2399CD8FED943471BB11ED805B8AFB48B84A4</identifier><identifier type="DOI">10.1016/S0014-5793(98)01623-8</identifier><identifier type="PII">S0014-5793(98)01623-8</identifier><accessCondition type="use and reproduction" contentType="">© 1999Federation of European Biochemical Societies</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Federation of European Biochemical Societies, ©1999</recordOrigin></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/D7F2399CD8FED943471BB11ED805B8AFB48B84A4/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">BIOCHEMISTRY & MOLECULAR BIOLOGY</classCode><classCode scheme="WOS">BIOPHYSICS</classCode><classCode scheme="WOS">CELL BIOLOGY</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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