Possible involvement of two proteins (phosphoprotein and CD9(p24)) in regulation of platelet calcium fluxes

FEBS Letters

Enouf, J.¹  Levy-Toledano, S.¹  Mirshahi, M.³  Bredoux, R.¹  Soria, C.¹  Boucheix, C.² 

[1] Unité de Recherches sur la Thrombose Expérimentale et l'Hémostase INSERM U 150, Hôpital Lariboisière, 6 rue Guy Patin, F75475 Paris Cedex 10 France;INSERM U 253 Hôpital Paul Brousse, Villejuif, Paris, France;Service de Médecine, Interne et Oncologie, Hôtel Dieu, Paris, France

关键词: Platelet membrane;    Ca2+ transport;    Monoclonal antibody;    Cyclic AMP;    Phosphorylation;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    cAMP;    cyclic adenosine 3;    5'-mono-phosphate;   

DOI  :  10.1016/0014-5793(85)80819-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The monoclonal antibody ALB₆ 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). ALB₆ IgG does not inhibit the C.subunit-induced phosphorylation of p23 and the immunoadsorption by ALB₆ 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 ALB₆ antibody while the other can be phosphorylated by the C-subunit.

【 授权许可】

Unknown