Immunochemical and amino-terminal sequence comparison of two cytoadhesins indicates they contain similar or identical beta subunits and distinct alpha subunits

• Published in: The Journal of biological chemistry 1987-04, Vol.262 (12), p.5437-5440
• Main Authors: Ginsberg, M.H., Loftus, J., Ryckwaert, J.J., Pierschbacher, M., Pytela, R., Ruoslahti, E., Plow, E.F.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Antibodies, Monoclonal; Blood Platelets - analysis; Cell Adhesion; Endothelium - analysis; Female; Humans; Macromolecular Substances; Platelet Membrane Glycoproteins - genetics; Platelet Membrane Glycoproteins - isolation & purification; Receptors, Immunologic - genetics; Receptors, Immunologic - isolation & purification; Receptors, Vitronectin; Umbilical Veins
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)45590-1

Platelet membrane glycoprotein (GP) IIb-IIIa is functionally and antigenically related to proteins present on many cell types, suggesting that it is a member of the proposed cytoadhesin family of membrane proteins. We have compared the purified tissue vitronectin receptor (VnR) with GP IIb-IIIa. Anti-VnR immunoprecipitated GP IIb-IIIa and a related endothelial cell protein. In immunoblots, GP IIIa reacted with anti-VnR and the beta subunit of the VnR reacted with poly and monoclonal anti-GP IIIa. In contrast, the alpha subunit of the VnR failed to react either with a polyclonal anti-GP IIb or with monoclonal anti-GP IIb. Furthermore, the amino-terminal sequence of GP IIIa and the beta subunit of VnR were identical at determined residues while the alpha subunit and the GP IIb were different, but showed 33% identity. These data indicate the identity or close homology of GP IIIa and the beta subunit of the VnR. In contrast, the alpha subunit and GP IIb are distinct polypeptides which may be homologous. Since GP IIb-IIIa and the VnR differ in ligand recognition specificity, the data also suggest that this specificity may be governed by the alpha subunit of cytoadhesins.