Premium
Stimulation by serotonin of 40 kDa and 20 kDa protein phosphorylation in human platelets
Author(s) -
de Chaffoy de Courcelles D.,
Roevens P.,
van Belle H.
Publication year - 1984
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(84)80506-2
Subject(s) - ketanserin , serotonin , platelet , stimulation , phosphorylation , myosin light chain kinase , protein kinase c , protein phosphorylation , phospholipase c , medicine , chemistry , cytosol , endocrinology , biochemistry , protein kinase a , biology , 5 ht receptor , signal transduction , receptor , enzyme
In human platelets, serotonin is known to induce a shape change followed by (reversible) aggregation. Recently, it was found that the amine triggers the elevation of cytosolic free calcium and activates phospholipase C. On stimulation of human platelets with serotonin we found an immediate increase in protein kinase C activity, phosphorylating its 40 kDa substrate protein. A 20 kDa protein, most likely the myosin light chain, was phosphorylated to the same extent. Ketanserin, a highly selective serotonin‐S 2 antagonist inhibited both phosphorylation processes at subnanomolar concentrations.