2024-03-28T15:06:47Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/239482020-10-20T13:25:14Zcom_10261_22com_10261_1com_10261_86col_10261_275col_10261_339
2010-05-05T11:26:05Z
urn:hdl:10261/23948
Phosphorylation of the human-transforming-growth-factor-beta-binding protein endoglin
Lastres, Pedro
Jorge, MartÍn-Perez
Langa, Carmen
Bernabéu, Carmelo
4 pages, 2 figures.
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.
2010-05-05T11:26:05Z
2010-05-05T11:26:05Z
1994-08-01
artículo
Biochemical Journal 301(3): 765-768 (1994)
0264-6021
http://hdl.handle.net/10261/23948
eng
http://www.biochemj.org/bj/301/bj3010765.htm
openAccess
Portland Press