The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors

Journal Article · Sat Feb 15 00:00:00 EST 1992 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.89.4.1281· OSTI ID:5617894

Raines, E W; Lane, T F; Iruela-Arispe, M L; Ross, R; Sage, E H ^[1]

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1. Univ. of Washington, Seattle (United States)

Interactions among growth factors, cells, and extracellular matrix are critical to the regulation of directed cell migration and proliferation associated with development wound healing, and pathologic processes. Here the authors report the association of PDGF-AB and -BB, but not PDGF-AA, with the extracellular glycoprotein SPARC. Complexes of SPARC and {sup 125}I-labeled PDGF-BB or -AB were specifically immunoprecipitated by anti-SPARC immunoglobulins. {sup 125}I-PDGF-BB and -AB also bound specifically to SPARC that was immobilized on microtiter wells or bound to nitrocellulose after transfer from SDS/polyacrylamide gels. The binding of PDGF-BB to SPARC was pH-dependent; significant binding was detectable only above pH 6.6. Enhanced expression of both PDGF-B chain and SPARC was seen in advanced lesions of atherosclerosis. They suggest that the coordinate expression of SPARC and PDGF-B-containing dimers following vascular injury may regulate the activity of specific dimeric forms of PDGF in vivo.

• OSTI ID: 5617894
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 89:4; ISSN 0027-8424
• Country of Publication: United States
• Language: English

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