Premium
Possible involvement of two proteins (phosphoprotein and CD9(p24)) in regulation of platelet calcium fluxes
Author(s) -
Enouf J.,
Bredoux R.,
Boucheix C.,
Mirshahi M.,
Soria C.,
Levy-Toledano S.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80819-x
Subject(s) - phosphoprotein , protein subunit , phosphorylation , monoclonal antibody , immunoadsorption , chemistry , molecular mass , biochemistry , protein phosphorylation , platelet , vesicle , calcium , immunoprecipitation , microbiology and biotechnology , protein kinase a , antibody , biology , membrane , enzyme , immunology , gene , organic chemistry
The monoclonal antibody ALB 6 directed against the leukocyte differentiation antigen CD9 (p24) increases the calcium incorporation into isolated platelet membrane vesicles enriched in internal membranes. The similarities of the effects of both the monoclonal antibody and the catalytic subunit of the cAMP‐dependent protein kinase (C. subunit), which phosphorylates a protein of an apparent molecular mass of 23 kDa, led us to investigate the relationship between CD9 (p24) and the 23‐kDa phosphoprotein (p23). ALB 6 IgG does not inhibit the C.subunit‐induced phosphorylation of p23 and the immunoadsorption by ALB 6 IgG of p24 associated to membrane vesicles does not alter the phosphorylation pattern. Thus, proteins of similar molecular mass appear to be involved in calcium fluxes: one is recognized by the ALB 6 antibody while the other can be phosphorylated by the C‐subunit.