| http://purl.uniprot.org/citations/22869525 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22869525 | http://www.w3.org/2000/01/rdf-schema#comment | "Insulin-like growth factor I (IGF-I) is a mitogen for vascular smooth muscle cells (VSMC) and has been implicated in the development and progression of atherosclerosis. IGF binding proteins (IGFBPs) modify IGF-I actions independently of IGF binding, but a receptor-based mechanism by which they function has not been elucidated. We investigated the role of IGFBP-2 and receptor protein tyrosine phosphatase β (RPTPβ) in regulating IGF-I signaling and cellular proliferation. IGFBP-2 bound RPTPβ, which led to its dimerization and inactivation. This enhanced PTEN tyrosine phosphorylation and inhibited PTEN activity. Utilization of substrate trapping and phosphatase-dead mutants showed that RPTPβ bound specifically to PTEN and dephosphorylated it. IGFBP-2 knockdown led to decreased PTEN tyrosine phosphorylation and decreased AKT Ser473 activation. IGFBP-2 enhanced IGF-I-stimulated VSMC migration and proliferation. Analysis of aortas obtained from IGFBP-2(-/-) mice showed that RPTPβ was activated, and this was associated with inhibition of IGF-I stimulated AKT Ser473 phosphorylation and VSMC proliferation. These changes were rescued following administration of IGFBP-2. These findings present a novel mechanism for coordinate regulation of IGFBP-2 and IGF-I signaling functions that lead to stimulation of VSMC proliferation. The results have important implications for understanding how IGFBPs modulate the cellular response to IGF-I."xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.01011-12"xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/author | "Shen X."xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/author | "Rosen C.J."xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/author | "Clemmons D.R."xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/author | "Xi G."xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/author | "Wai C."xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/author | "Maile L.A."xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/pages | "4116-4130"xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/title | "Insulin-like growth factor (IGF) binding protein 2 functions coordinately with receptor protein tyrosine phosphatase beta and the IGF-I receptor to regulate IGF-I-stimulated signaling."xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://purl.uniprot.org/core/volume | "32"xsd:string |
| http://purl.uniprot.org/citations/22869525 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22869525 |
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