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Effects of 17‐hydroxywortmannin on serine/threonine‐protein kinases in human blood platelets
Author(s) -
Kocher Markus,
Clemetson Kenneth J.
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)81321-x
Subject(s) - kinase , thrombin , serine , platelet , signal transduction , biochemistry , phosphorylation , threonine , chemistry , microbiology and biotechnology , in vitro , mitogen activated protein kinase , protein phosphorylation , protein kinase a , biology , immunology
Protein kinases are involved in signal transduction in human blood platelets. A number of renaturable protein kinases have increased in vitro activities compared to controls due to covalent modifications when intact platelets are activated by thrombin. The effect of the platelet inhibitor 17‐hydroxywortmannin (HWT) on these protein kinases was investigated in intact platelets and in vitro. HWT inhibits the increase in activity of these protein kinases but it does not interact directly with their catalytic subunits. We conclude that HWT blocks a step in signal transduction which is necessary to activate these protein kinases via covalent modifications.