IL‐4 activates a distinct signal transduction cascade from IL‐3 in factor‐dependent myeloid cells
Interleukin‐4 (IL‐4) was shown to induce a potent mitogenic response in the IL‐3‐dependent myeloid progenitor cell line, FDCP‐2. Although IL‐4 could not sustain long‐term growth of FDCP‐2 cells, it enhanced their growth in serum‐free medium containing IL‐3. IL‐4 triggered prominent tyrosine phosphor...
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| Veröffentlicht in: | The EMBO journal 1992-12, Vol.11 (13), p.4899-4908 |
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| creator | Wang, L.M. Keegan, A.D. Paul, W.E. Heidaran, M.A. Gutkind, J.S. Pierce, J.H. |
| description | Interleukin‐4 (IL‐4) was shown to induce a potent mitogenic response in the IL‐3‐dependent myeloid progenitor cell line, FDCP‐2. Although IL‐4 could not sustain long‐term growth of FDCP‐2 cells, it enhanced their growth in serum‐free medium containing IL‐3. IL‐4 triggered prominent tyrosine phosphorylation of a substrate(s) migrating at 170 kDa and less striking phosphorylation of several other proteins, including the IL‐4 receptor. By contrast, IL‐3 induced distinct tyrosine phosphorylation of proteins migrating at 145, 97, 70, 55 and 52 kDa in the same cell line. IL‐4 treatment of FDCP‐2 cells caused a dramatically strong association of phosphatidylinositol 3‐kinase (PI 3‐kinase) both with the 170 kDa tyrosine phosphorylated substrate and with the IL‐4 receptor itself. By contrast, IL‐3 triggered only weak association of PI 3‐kinase activity with the 97 kDa substrate. While IL‐4 did not affect cellular raf, IL‐3 stimulation did induce a shift in its mobility presumably due to serine/threonine phosphorylation. Taken together, our results indicate that IL‐4 and IL‐3 activate distinct phosphorylation cascades in the same cell background; this may reflect a difference in the biological function of these two cytokines. |
| doi_str_mv | 10.1002/j.1460-2075.1992.tb05596.x |
| format | Article |
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Although IL‐4 could not sustain long‐term growth of FDCP‐2 cells, it enhanced their growth in serum‐free medium containing IL‐3. IL‐4 triggered prominent tyrosine phosphorylation of a substrate(s) migrating at 170 kDa and less striking phosphorylation of several other proteins, including the IL‐4 receptor. By contrast, IL‐3 induced distinct tyrosine phosphorylation of proteins migrating at 145, 97, 70, 55 and 52 kDa in the same cell line. IL‐4 treatment of FDCP‐2 cells caused a dramatically strong association of phosphatidylinositol 3‐kinase (PI 3‐kinase) both with the 170 kDa tyrosine phosphorylated substrate and with the IL‐4 receptor itself. By contrast, IL‐3 triggered only weak association of PI 3‐kinase activity with the 97 kDa substrate. While IL‐4 did not affect cellular raf, IL‐3 stimulation did induce a shift in its mobility presumably due to serine/threonine phosphorylation. Taken together, our results indicate that IL‐4 and IL‐3 activate distinct phosphorylation cascades in the same cell background; this may reflect a difference in the biological function of these two cytokines.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1992.tb05596.x</identifier><identifier>PMID: 1334461</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group</publisher><subject>Analysis of the immune response. Humoral and cellular immunity ; Animals ; Biological and medical sciences ; Blotting, Western ; Cell Line ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; GTPase-Activating Proteins ; Hematopoietic Stem Cells - metabolism ; Immunobiology ; Interleukin-3 - metabolism ; Interleukin-4 - physiology ; Lymphokines, interleukins ( function, expression) ; Mice ; Phosphatidylinositol 3-Kinases ; Phosphorylation ; Phosphotransferases - metabolism ; Precipitin Tests ; Proteins - metabolism ; Receptors, Interleukin-4 ; Receptors, Mitogen - metabolism ; Regulatory factors and their cellular receptors ; Signal Transduction ; Substrate Specificity ; Type C Phospholipases - metabolism ; Tyrosine - metabolism</subject><ispartof>The EMBO journal, 1992-12, Vol.11 (13), p.4899-4908</ispartof><rights>1992 European Molecular Biology Organization</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5386-5ae2dc0e0b5d34ed826e9b0873d11887dbf3f3874e1d2f273d1ac9bb0ae3521e3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC556967/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC556967/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4460697$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1334461$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, L.M.</creatorcontrib><creatorcontrib>Keegan, A.D.</creatorcontrib><creatorcontrib>Paul, W.E.</creatorcontrib><creatorcontrib>Heidaran, M.A.</creatorcontrib><creatorcontrib>Gutkind, J.S.</creatorcontrib><creatorcontrib>Pierce, J.H.</creatorcontrib><title>IL‐4 activates a distinct signal transduction cascade from IL‐3 in factor‐dependent myeloid cells</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>Interleukin‐4 (IL‐4) was shown to induce a potent mitogenic response in the IL‐3‐dependent myeloid progenitor cell line, FDCP‐2. Although IL‐4 could not sustain long‐term growth of FDCP‐2 cells, it enhanced their growth in serum‐free medium containing IL‐3. IL‐4 triggered prominent tyrosine phosphorylation of a substrate(s) migrating at 170 kDa and less striking phosphorylation of several other proteins, including the IL‐4 receptor. By contrast, IL‐3 induced distinct tyrosine phosphorylation of proteins migrating at 145, 97, 70, 55 and 52 kDa in the same cell line. IL‐4 treatment of FDCP‐2 cells caused a dramatically strong association of phosphatidylinositol 3‐kinase (PI 3‐kinase) both with the 170 kDa tyrosine phosphorylated substrate and with the IL‐4 receptor itself. By contrast, IL‐3 triggered only weak association of PI 3‐kinase activity with the 97 kDa substrate. While IL‐4 did not affect cellular raf, IL‐3 stimulation did induce a shift in its mobility presumably due to serine/threonine phosphorylation. Taken together, our results indicate that IL‐4 and IL‐3 activate distinct phosphorylation cascades in the same cell background; this may reflect a difference in the biological function of these two cytokines.</description><subject>Analysis of the immune response. Humoral and cellular immunity</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cell Line</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>GTPase-Activating Proteins</subject><subject>Hematopoietic Stem Cells - metabolism</subject><subject>Immunobiology</subject><subject>Interleukin-3 - metabolism</subject><subject>Interleukin-4 - physiology</subject><subject>Lymphokines, interleukins ( function, expression)</subject><subject>Mice</subject><subject>Phosphatidylinositol 3-Kinases</subject><subject>Phosphorylation</subject><subject>Phosphotransferases - metabolism</subject><subject>Precipitin Tests</subject><subject>Proteins - metabolism</subject><subject>Receptors, Interleukin-4</subject><subject>Receptors, Mitogen - metabolism</subject><subject>Regulatory factors and their cellular receptors</subject><subject>Signal Transduction</subject><subject>Substrate Specificity</subject><subject>Type C Phospholipases - metabolism</subject><subject>Tyrosine - metabolism</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc1u1DAUhS0EKkPhEZAshNgl-D8JEou2KlA0iA2sLce-GTxKnMHOlM6OR-gz9klwOqMBVoiVf845V-fqQ-gFJSUlhL1el1QoUjBSyZI2DSunlkjZqPLmAVocpYdoQZiihaB18xg9SWlNCJF1RU_QCeVcCEUXaHW1vPt5K7Cxk782EyRssPNp8sFOOPlVMD2eognJbbNjDNiaZI0D3MVxwPdhjn3AXR4wxvxysIHgIEx42EE_eoct9H16ih51pk_w7HCeoq_vLr9cfCiWn99fXZwtCyt5rQppgDlLgLTScQGuZgqaltQVd5TWdeXajne8rgRQxzo2fxvbtC0xwCWjwE_R2_3czbYdwNlcJJpeb6IfTNzp0Xj9txL8N70ar7WUqlFVzr865OP4fQtp0oNP8wYmwLhNuuKCN4zzfxqpEpxSMRvf7I02jilF6I5lKNEzTr3WMzM9M9MzTn3AqW9y-Pmf6_yO7vll_eVBn7H0XSZlfTrasoeoZt7qbG_74XvY_UcBffnp_OP9nf8CptTCEg</recordid><startdate>199212</startdate><enddate>199212</enddate><creator>Wang, L.M.</creator><creator>Keegan, A.D.</creator><creator>Paul, W.E.</creator><creator>Heidaran, M.A.</creator><creator>Gutkind, J.S.</creator><creator>Pierce, J.H.</creator><general>Nature Publishing Group</general><scope>IQODW</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>7T5</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>199212</creationdate><title>IL‐4 activates a distinct signal transduction cascade from IL‐3 in factor‐dependent myeloid cells</title><author>Wang, L.M. ; Keegan, A.D. ; Paul, W.E. ; Heidaran, M.A. ; Gutkind, J.S. ; Pierce, J.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5386-5ae2dc0e0b5d34ed826e9b0873d11887dbf3f3874e1d2f273d1ac9bb0ae3521e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Analysis of the immune response. Humoral and cellular immunity</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cell Line</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>GTPase-Activating Proteins</topic><topic>Hematopoietic Stem Cells - metabolism</topic><topic>Immunobiology</topic><topic>Interleukin-3 - metabolism</topic><topic>Interleukin-4 - physiology</topic><topic>Lymphokines, interleukins ( function, expression)</topic><topic>Mice</topic><topic>Phosphatidylinositol 3-Kinases</topic><topic>Phosphorylation</topic><topic>Phosphotransferases - metabolism</topic><topic>Precipitin Tests</topic><topic>Proteins - metabolism</topic><topic>Receptors, Interleukin-4</topic><topic>Receptors, Mitogen - metabolism</topic><topic>Regulatory factors and their cellular receptors</topic><topic>Signal Transduction</topic><topic>Substrate Specificity</topic><topic>Type C Phospholipases - metabolism</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, L.M.</creatorcontrib><creatorcontrib>Keegan, A.D.</creatorcontrib><creatorcontrib>Paul, W.E.</creatorcontrib><creatorcontrib>Heidaran, M.A.</creatorcontrib><creatorcontrib>Gutkind, J.S.</creatorcontrib><creatorcontrib>Pierce, J.H.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, L.M.</au><au>Keegan, A.D.</au><au>Paul, W.E.</au><au>Heidaran, M.A.</au><au>Gutkind, J.S.</au><au>Pierce, J.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>IL‐4 activates a distinct signal transduction cascade from IL‐3 in factor‐dependent myeloid cells</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1992-12</date><risdate>1992</risdate><volume>11</volume><issue>13</issue><spage>4899</spage><epage>4908</epage><pages>4899-4908</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Interleukin‐4 (IL‐4) was shown to induce a potent mitogenic response in the IL‐3‐dependent myeloid progenitor cell line, FDCP‐2. Although IL‐4 could not sustain long‐term growth of FDCP‐2 cells, it enhanced their growth in serum‐free medium containing IL‐3. IL‐4 triggered prominent tyrosine phosphorylation of a substrate(s) migrating at 170 kDa and less striking phosphorylation of several other proteins, including the IL‐4 receptor. By contrast, IL‐3 induced distinct tyrosine phosphorylation of proteins migrating at 145, 97, 70, 55 and 52 kDa in the same cell line. IL‐4 treatment of FDCP‐2 cells caused a dramatically strong association of phosphatidylinositol 3‐kinase (PI 3‐kinase) both with the 170 kDa tyrosine phosphorylated substrate and with the IL‐4 receptor itself. By contrast, IL‐3 triggered only weak association of PI 3‐kinase activity with the 97 kDa substrate. While IL‐4 did not affect cellular raf, IL‐3 stimulation did induce a shift in its mobility presumably due to serine/threonine phosphorylation. Taken together, our results indicate that IL‐4 and IL‐3 activate distinct phosphorylation cascades in the same cell background; this may reflect a difference in the biological function of these two cytokines.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>1334461</pmid><doi>10.1002/j.1460-2075.1992.tb05596.x</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Analysis of the immune response. Humoral and cellular immunity Animals Biological and medical sciences Blotting, Western Cell Line Fundamental and applied biological sciences. Psychology Fundamental immunology GTPase-Activating Proteins Hematopoietic Stem Cells - metabolism Immunobiology Interleukin-3 - metabolism Interleukin-4 - physiology Lymphokines, interleukins ( function, expression) Mice Phosphatidylinositol 3-Kinases Phosphorylation Phosphotransferases - metabolism Precipitin Tests Proteins - metabolism Receptors, Interleukin-4 Receptors, Mitogen - metabolism Regulatory factors and their cellular receptors Signal Transduction Substrate Specificity Type C Phospholipases - metabolism Tyrosine - metabolism |
| title | IL‐4 activates a distinct signal transduction cascade from IL‐3 in factor‐dependent myeloid cells |
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