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Role of IIb‐IIIa‐like glycoproteins in cell‐substratum adhesion of human melanoma cells
Author(s) -
Knudsen Karen A.,
Smith Linda,
Smith Sena,
Karczewski Jerzy,
Tuszynski George P.
Publication year - 1988
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041360311
Subject(s) - glycoprotein , adhesion , chemistry , cell adhesion , microbiology and biotechnology , cell , melanoma , biochemistry , biology , cancer research , organic chemistry
The platelet fibrinogen receptor, glycoprotein complex IIb‐IIIa, was isolated from human platelets by lectin and monoclonal antibody affinity chromatography and a polyclonal antiserum (anti‐IIb‐IIIa) was generated and used to probe for the presence and function of IIb‐IIIa‐like molecules in two adherent human cell lines. Both C32 melanoma cells and W138 fibroblasts expressed a IIb‐IIIa‐like complex on their surface as indicated by immunoprecipitation of detergent extracts of surface radiolabeled cells. When added to cells plated in medium containing 10% serum, the anti‐IIb‐IIIa antiserum perturbed the adhesion of C32 melanoma cells, but not of W138 fibroblasts. In a serum‐free system, anti‐IIb‐IIIa antibodies inhibited attachment and spreading of C32 cells to fibrinogen, vitronectin, and fibronectin adsorbed to glass. Anti‐IIb‐IIIa had no effect on the attachment and spreading of W138 cells to the extracellular matrix proteins, however. Thus, the IIb‐IIIa‐like complex appears to play a predominant role in cell‐substratum adhesion of C32 cells, but not W138 cells, and may result from the fact that, on a protein basis, the C32 melanoma cells express approximately 3 times more complex on their surface than do W138 fibroblasts. The results suggest that the relative abundance of a particular adhesion receptor on the cell surface may govern its importance to cell‐substratum adhesion.