{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T03:44:45Z","timestamp":1790048685175,"version":"4.0.1"},"reference-count":60,"publisher":"The Endocrine Society","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>IGF-I stimulates cell growth through interaction of the IGF receptor with multiprotein signaling complexes. However, the mechanisms of IGF-I receptor-mediated signaling are not completely understood. We have previously shown that IGF-I-stimulated 3T3-L1 cell proliferation is dependent on Src activation of the ERK-1\/2 MAPK pathway. We hypothesized that IGF-I activation of the MAPK pathway is mediated through integrin activation of Src-containing signaling complexes. The disintegrin echistatin decreased IGF-I phosphorylation of Src and MAPK, and blocking antibodies to \u03b1v and \u03b23 integrin subunits inhibited IGF-I activation of MAPK, suggesting that \u03b1v\u03b23 integrins mediate IGF-I mitogenic signaling. IGF-I increased ligand binding to \u03b1v\u03b23 as detected by immunofluorescent staining of ligand-induced binding site antibody and stimulated phosphorylation of the \u03b23 subunit, consistent with inside-out activation of \u03b1v\u03b23 integrins. IGF-I increased tyrosine phosphorylation of the focal adhesion kinase (FAK) Pyk2 (calcium-dependent proline-rich tyrosine kinase-2) to a much greater extent than FAK, and increased association of Src with Pyk2 but not FAK. The intracellular calcium chelator BAPTA prevented IGF-I phosphorylation of Pyk2, Src, and MAPK, suggesting that IGF-I activation of Pyk2 is calcium dependent. Transient transfection with a dominant-negative Pyk2, which lacks the autophosphorylation and Src binding site, decreased IGF-I activation of MAPK, but no inhibition was seen with transfected wild-type Pyk2. These results indicate that IGF-I signaling to MAPK is dependent on inside-out activation of \u03b1v\u03b23 integrins and integrin-facilitated multiprotein complex formation involving Pyk2 activation and association with Src.<\/jats:p>","DOI":"10.1210\/me.2004-0481","type":"journal-article","created":{"date-parts":[[2005,3,11]],"date-time":"2005-03-11T02:53:52Z","timestamp":1110509632000},"page":"1859-1867","source":"Crossref","is-referenced-by-count":29,"title":["\u03b1v\u03b23 Integrins and Pyk2 Mediate Insulin-Like Growth Factor I Activation of Src and Mitogen-Activated Protein Kinase in 3T3-L1 Cells"],"prefix":"10.1210","volume":"19","author":[{"given":"Hiroko","family":"Sekimoto","sequence":"first","affiliation":[{"name":"Department of Pediatrics, Rhode Island Hospital and Brown Medical School, Providence, Rhode Island 02903"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jodi","family":"Eipper-Mains","sequence":"additional","affiliation":[{"name":"Department of 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