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The GPIIb-IIIa-like complex may function as a human melanoma cell adhesion receptor for thrombospondin

Journal Article · · Experimental Cell Research; (United States)
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  1. Lankenau Medical Research Center, Philadelphia, PA (United States)

The purpose of this study was to determine whether a heterodimeric complex immunologically related to the fibrinogen receptor could function as a thrombospondin (TSP) receptor in TSP-mediated cell-substratum adhesion of human melanoma cells. The authors found that polyclonal antibodies to the platelet GPIIb-IIIa complex, GPIIIa, and the human vitronectin receptor inhibited TSP-mediated cell adhesion by 63-68%. Immunoprecipitation of detergent extracts of {sup 125}I-surface-labeled melanoma cells using either anti-human platelet GPIIb-IIIa or anti-human vitronectin receptor antibody revealed the presence of a single heterodimeric complexes, suggesting that both antisera recognize the same integrin receptor, GPIIb-IIIa-like antigen. Adhesion of cells to TSP is likely mediated through a region of the TSP molecule containing the arginine-glycine-aspartic (RGD) peptide sequence, since cell attachment to TSP was inhibited 50-66% in the presence of peptides containing RGD. These results strongly suggest that a GPIIb-IIIa-like/vitronectin receptor can serve as a cell binding site for TSP in mediating cell-substratum adhesion.

OSTI ID:
5714695
Journal Information:
Experimental Cell Research; (United States), Journal Name: Experimental Cell Research; (United States) Vol. 182:2; ISSN ECREA; ISSN 0014-4827
Country of Publication:
United States
Language:
English