Evidence for a novel function of the CD40 ligand as a signalling molecule in T-lymphocytes
The interaction of the CD40 receptor with its ligand has been shown to be crucial for the activation of B-lymphocytes. Here, we provide evidence that the pg39 molecule/CD40 ligand (gp39/CD40L) also functions as a stimulatory molecule for T-lymphocytes. Activation of T-lymphocytes via gp39/CD40L indu...
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Veröffentlicht in: | FEBS letters 1997-11, Vol.417 (3), p.301-306 |
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creator | Brenner, Birgit Koppenhoefer, Ursula Grassmé, Heike Kun, Jutta Lang, Florian Gulbins, Erich |
description | The interaction of the CD40 receptor with its ligand has been shown to be crucial for the activation of B-lymphocytes. Here, we provide evidence that the pg39 molecule/CD40 ligand (gp39/CD40L) also functions as a stimulatory molecule for T-lymphocytes. Activation of T-lymphocytes via gp39/CD40L induced a strong activation of Jun-N-terminal kinase (JNK) and p38-K. Activation of these kinases correlates with a stimulation of Rac1 and inhibition of Rac1 prevents gp39/CD40L triggered JNK/p38-K activation. Further, cellular stimulation via the CD40 ligand results in tyrosine phosphorylation of cellular proteins and the activation of p56
lck. Inhibition of src-like kinases inhibits Rac1 as well as JNK/p38-K stimulation suggesting a signalling cascade from the gp39/CD40L via p56
lck and Rac1 to JNK/p38-K. |
doi_str_mv | 10.1016/S0014-5793(97)01306-9 |
format | Article |
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lck. Inhibition of src-like kinases inhibits Rac1 as well as JNK/p38-K stimulation suggesting a signalling cascade from the gp39/CD40L via p56
lck and Rac1 to JNK/p38-K.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)01306-9</identifier><identifier>PMID: 9409738</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Antigens, CD - physiology ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; CD40 Antigens - physiology ; CD40 Ligand ; gp39 ; Humans ; JNK Mitogen-Activated Protein Kinases ; Jun-N-terminal kinase ; Jurkat Cells ; Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism ; Membrane Glycoproteins - physiology ; Mice ; Mitogen-Activated Protein Kinases ; p38 Mitogen-Activated Protein Kinases ; Recombinant Proteins - metabolism ; Signal Transduction ; Spleen - enzymology ; T-lymphocytes ; T-Lymphocytes - immunology ; T-Lymphocytes - physiology ; Transfection ; Tyrosine kinase</subject><ispartof>FEBS letters, 1997-11, Vol.417 (3), p.301-306</ispartof><rights>1997 Federation of European Biochemical Societies</rights><rights>FEBS Letters 417 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4049-e9e44c722281429bb1f554ac48da31b2b43e6639f1bb355beb358f44d2d716e13</citedby><cites>FETCH-LOGICAL-c4049-e9e44c722281429bb1f554ac48da31b2b43e6639f1bb355beb358f44d2d716e13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2897%2901306-9$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(97)01306-9$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9409738$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brenner, Birgit</creatorcontrib><creatorcontrib>Koppenhoefer, Ursula</creatorcontrib><creatorcontrib>Grassmé, Heike</creatorcontrib><creatorcontrib>Kun, Jutta</creatorcontrib><creatorcontrib>Lang, Florian</creatorcontrib><creatorcontrib>Gulbins, Erich</creatorcontrib><title>Evidence for a novel function of the CD40 ligand as a signalling molecule in T-lymphocytes</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The interaction of the CD40 receptor with its ligand has been shown to be crucial for the activation of B-lymphocytes. Here, we provide evidence that the pg39 molecule/CD40 ligand (gp39/CD40L) also functions as a stimulatory molecule for T-lymphocytes. Activation of T-lymphocytes via gp39/CD40L induced a strong activation of Jun-N-terminal kinase (JNK) and p38-K. Activation of these kinases correlates with a stimulation of Rac1 and inhibition of Rac1 prevents gp39/CD40L triggered JNK/p38-K activation. Further, cellular stimulation via the CD40 ligand results in tyrosine phosphorylation of cellular proteins and the activation of p56
lck. Inhibition of src-like kinases inhibits Rac1 as well as JNK/p38-K stimulation suggesting a signalling cascade from the gp39/CD40L via p56
lck and Rac1 to JNK/p38-K.</description><subject>Animals</subject><subject>Antigens, CD - physiology</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>CD40 Antigens - physiology</subject><subject>CD40 Ligand</subject><subject>gp39</subject><subject>Humans</subject><subject>JNK Mitogen-Activated Protein Kinases</subject><subject>Jun-N-terminal kinase</subject><subject>Jurkat Cells</subject><subject>Lymphocyte Activation</subject><subject>Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism</subject><subject>Membrane Glycoproteins - physiology</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinases</subject><subject>p38 Mitogen-Activated Protein Kinases</subject><subject>Recombinant Proteins - metabolism</subject><subject>Signal Transduction</subject><subject>Spleen - enzymology</subject><subject>T-lymphocytes</subject><subject>T-Lymphocytes - immunology</subject><subject>T-Lymphocytes - physiology</subject><subject>Transfection</subject><subject>Tyrosine kinase</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1O6zAQhS0EgvLzCEheIe4iYMdOHK_QvaUFJCQWwIaN5TiTYuTYvXFS1LcnaSu2sPHIPmfOWN8gdE7JFSU0v34mhPIkE5JdSvGHUEbyRO6hCS0ESxjPi300-bYcoeMYP8hwL6g8RIeSEylYMUFvs5WtwBvAdWixxj6swOG696azweNQ4-4d8PSWE-zsQvsK6zjYol147Zz1C9wEB6Z3gK3HL4lbN8v3YNYdxFN0UGsX4WxXT9DrfPYyvU8en-4epn8fE8MJlwlI4NyINE0LylNZlrTOMq4NLyrNaJmWnEGeM1nTsmRZVsJwFjXnVVoJmgNlJ-him7tsw_8eYqcaGw04pz2EPiohecFzygZjtjWaNsTYQq2WrW10u1aUqJGp2jBVIzAlhdowVXLoO98N6MsGqu-uHcRBv9_qn9bB-nehaj77l26UUZBi8zyOutlGwQBsZaFV0dhxPZVtwXSqCvaHz34BIEGZAw</recordid><startdate>19971117</startdate><enddate>19971117</enddate><creator>Brenner, Birgit</creator><creator>Koppenhoefer, Ursula</creator><creator>Grassmé, Heike</creator><creator>Kun, Jutta</creator><creator>Lang, Florian</creator><creator>Gulbins, Erich</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19971117</creationdate><title>Evidence for a novel function of the CD40 ligand as a signalling molecule in T-lymphocytes</title><author>Brenner, Birgit ; Koppenhoefer, Ursula ; Grassmé, Heike ; Kun, Jutta ; Lang, Florian ; Gulbins, Erich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4049-e9e44c722281429bb1f554ac48da31b2b43e6639f1bb355beb358f44d2d716e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Antigens, CD - physiology</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>CD40 Antigens - physiology</topic><topic>CD40 Ligand</topic><topic>gp39</topic><topic>Humans</topic><topic>JNK Mitogen-Activated Protein Kinases</topic><topic>Jun-N-terminal kinase</topic><topic>Jurkat Cells</topic><topic>Lymphocyte Activation</topic><topic>Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism</topic><topic>Membrane Glycoproteins - physiology</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinases</topic><topic>p38 Mitogen-Activated Protein Kinases</topic><topic>Recombinant Proteins - metabolism</topic><topic>Signal Transduction</topic><topic>Spleen - enzymology</topic><topic>T-lymphocytes</topic><topic>T-Lymphocytes - immunology</topic><topic>T-Lymphocytes - physiology</topic><topic>Transfection</topic><topic>Tyrosine kinase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brenner, Birgit</creatorcontrib><creatorcontrib>Koppenhoefer, Ursula</creatorcontrib><creatorcontrib>Grassmé, Heike</creatorcontrib><creatorcontrib>Kun, Jutta</creatorcontrib><creatorcontrib>Lang, Florian</creatorcontrib><creatorcontrib>Gulbins, Erich</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brenner, Birgit</au><au>Koppenhoefer, Ursula</au><au>Grassmé, Heike</au><au>Kun, Jutta</au><au>Lang, Florian</au><au>Gulbins, Erich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for a novel function of the CD40 ligand as a signalling molecule in T-lymphocytes</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-11-17</date><risdate>1997</risdate><volume>417</volume><issue>3</issue><spage>301</spage><epage>306</epage><pages>301-306</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The interaction of the CD40 receptor with its ligand has been shown to be crucial for the activation of B-lymphocytes. Here, we provide evidence that the pg39 molecule/CD40 ligand (gp39/CD40L) also functions as a stimulatory molecule for T-lymphocytes. Activation of T-lymphocytes via gp39/CD40L induced a strong activation of Jun-N-terminal kinase (JNK) and p38-K. Activation of these kinases correlates with a stimulation of Rac1 and inhibition of Rac1 prevents gp39/CD40L triggered JNK/p38-K activation. Further, cellular stimulation via the CD40 ligand results in tyrosine phosphorylation of cellular proteins and the activation of p56
lck. Inhibition of src-like kinases inhibits Rac1 as well as JNK/p38-K stimulation suggesting a signalling cascade from the gp39/CD40L via p56
lck and Rac1 to JNK/p38-K.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9409738</pmid><doi>10.1016/S0014-5793(97)01306-9</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Antigens, CD - physiology Calcium-Calmodulin-Dependent Protein Kinases - metabolism CD40 Antigens - physiology CD40 Ligand gp39 Humans JNK Mitogen-Activated Protein Kinases Jun-N-terminal kinase Jurkat Cells Lymphocyte Activation Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism Membrane Glycoproteins - physiology Mice Mitogen-Activated Protein Kinases p38 Mitogen-Activated Protein Kinases Recombinant Proteins - metabolism Signal Transduction Spleen - enzymology T-lymphocytes T-Lymphocytes - immunology T-Lymphocytes - physiology Transfection Tyrosine kinase |
title | Evidence for a novel function of the CD40 ligand as a signalling molecule in T-lymphocytes |
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