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

M. H. Ginsberg, Joseph C Loftus, J. J. Ryckwaert, M. Pierschbacher, R. Pytela, E. Ruoslahti, E. F. Plow

Research output: Contribution to journalArticle

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Abstract

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 β subunit of the VnR reacted with poly and monoclonal anti-GP IIIa. In contrast, the α 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 β subunit of VnR were identical at determined residues while the α subunit and the GP IIb were different, but showed 33% identity. These data indicate the identity or close homology of GP IIIa and the β subunit of the VnR. In contrast, the α 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 α subunit of cytoadhesins.

Original languageEnglish (US)
Pages (from-to)5437-5440
Number of pages4
JournalJournal of Biological Chemistry
Volume262
Issue number12
StatePublished - 1987
Externally publishedYes

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Integrin alphaVbeta3
Glycoproteins
Platelet Glycoprotein GPIIb-IIIa Complex
Platelet Membrane Glycoprotein IIb
Integrin beta3
Endothelial cells
Membrane Proteins
Proteins
Endothelial Cells
Tissue
Ligands
Peptides

ASJC Scopus subject areas

  • Biochemistry

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Immunochemical and amino-terminal sequence comparison of two cytoadhesins indicates they contain similar or identical β subunits and distinct α subunits. / Ginsberg, M. H.; Loftus, Joseph C; Ryckwaert, J. J.; Pierschbacher, M.; Pytela, R.; Ruoslahti, E.; Plow, E. F.

In: Journal of Biological Chemistry, Vol. 262, No. 12, 1987, p. 5437-5440.

Research output: Contribution to journalArticle

Ginsberg, M. H. ; Loftus, Joseph C ; Ryckwaert, J. J. ; Pierschbacher, M. ; Pytela, R. ; Ruoslahti, E. ; Plow, E. F. / Immunochemical and amino-terminal sequence comparison of two cytoadhesins indicates they contain similar or identical β subunits and distinct α subunits. In: Journal of Biological Chemistry. 1987 ; Vol. 262, No. 12. pp. 5437-5440.
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T1 - Immunochemical and amino-terminal sequence comparison of two cytoadhesins indicates they contain similar or identical β subunits and distinct α subunits

AU - Ginsberg, M. H.

AU - Loftus, Joseph C

AU - Ryckwaert, J. J.

AU - Pierschbacher, M.

AU - Pytela, R.

AU - Ruoslahti, E.

AU - Plow, E. F.

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N2 - 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 β subunit of the VnR reacted with poly and monoclonal anti-GP IIIa. In contrast, the α 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 β subunit of VnR were identical at determined residues while the α subunit and the GP IIb were different, but showed 33% identity. These data indicate the identity or close homology of GP IIIa and the β subunit of the VnR. In contrast, the α 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 α subunit of cytoadhesins.

AB - 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 β subunit of the VnR reacted with poly and monoclonal anti-GP IIIa. In contrast, the α 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 β subunit of VnR were identical at determined residues while the α subunit and the GP IIb were different, but showed 33% identity. These data indicate the identity or close homology of GP IIIa and the β subunit of the VnR. In contrast, the α 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 α subunit of cytoadhesins.

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