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Título

Phosphorylation of the human-transforming-growth-factor-beta-binding protein endoglin

AutorLastres, Pedro ; Jorge, MartÍn-Perez; Langa, Carmen ; Bernabéu, Carmelo
Fecha de publicación1-ago-1994
EditorPortland Press
CitaciónBiochemical Journal 301(3): 765-768 (1994)
ResumenEndoglin 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.
Descripción4 pages, 2 figures.
Versión del editorhttp://www.biochemj.org/bj/301/bj3010765.htm
URIhttp://hdl.handle.net/10261/23948
ISSN0264-6021
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