Premium
The Na + /H + exchanger is phosphorylated in human platelets in response to activating agents
Author(s) -
Livne Avinoam A.,
Sardet Claude,
Pouyssegur Jacques
Publication year - 1991
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(91)80689-z
Subject(s) - okadaic acid , staurosporine , sodium–hydrogen antiporter , chemistry , amiloride , platelet , protein kinase c , phosphorylation , diacylglycerol kinase , intracellular ph , phosphatase , thrombin , biochemistry , biophysics , intracellular , sodium , biology , organic chemistry , immunology
α‐Thrombin, phorbol esters (PMA) and 1,2‐diacylglycerol (DAG), three activators of the amiloride‐sensitive Na + /H + exchange in human platelets, rapidly increase the intracellular pH and the level of phosphorylation of the Na + /H + exchanger protein (NHE1). This stimulatory effect is suppressed by staurosporine, a potent kinase inhibitor, and increased by okadaic acid, a potent inhibitor of phosphatase 1 and 2A. The modulations of NHE1 phosphorylation by these factors correlate well with their effects on platelet pH. Thus, we conclude that in platelets (i) Na + /H + exchange is mediated by NHE1. and (ii) platelet activating agents stimulate NHE1 via the modulation of the kinase/phosphatase equilibrium.