Phosphorylation of the human-transforming-growth-factor-beta-binding protein endoglin.
Biochem J
; 301 ( Pt 3): 765-8, 1994 Aug 01.
Article
em En
| MEDLINE
| ID: mdl-8053900
ABSTRACT
Endoglin is an homodimeric membrane antigen with capacity to bind transforming growth factor-beta (TGF-beta). Phosphorylation of human endoglin was demonstrated in endothelial cells as well as in mouse fibroblast transfectants expressing two isoforms, L-endoglin or S-endoglin, with distinct cytoplasmic domains. The extent of L-endoglin phosphorylation was found to be 8-fold higher than that of S-endoglin, and phosphopeptide analyses revealed at least three different phosphorylation sites for L-endoglin, whereas S-endoglin produces only one phosphopeptide. The immunoprecipitated L-endoglin was found to be phosphorylated mainly on serine, and, to a minor extent, on threonine, residues. Treatment of the cells with TGF-beta 1 or the protein kinase C inhibitor H-7 resulted in a reduction of the levels of endoglin phosphorylation.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Endotélio Vascular
/
Glicoproteínas de Membrana
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Fator de Crescimento Transformador beta
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Molécula 1 de Adesão de Célula Vascular
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article