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Arachidonic and cis ‐unsaturated fatty acids induce selective platelet substrate phosphorylation through activation of cytosolic protein kinase C
Author(s) -
Waris Khan,
Samia El Touny,
Yusuf A. Hannun
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)80843-r
Subject(s) - cytosol , arachidonic acid , chemistry , phosphorylation , substrate (aquarium) , protein kinase a , biochemistry , protein kinase c , platelet , kinase , amp activated protein kinase , enzyme , biology , ampk , ecology , immunology
The ability of arachidonic acid and other fatty acids to induce phosphorylation of endogenous substrates and the role of protein kinase C in mediating these effects were examined. In a cell‐free cytosolic system derived from human platelets, arachidonic, oleic, and other cis ‐unsaturated fatty acids induced a dose‐dependent phosphorylation of several endogenous substrates. These substrates form a subset of phorbol ester‐induced phosphorylations. Multiple lines of evidence suggested the direct involvement of protein kinase C in mediating fatty acid‐induced phosphorylations. These observations suggest that arachidonic acid and other unsaturated fatty acids are capable of activating protein kinase C in a physiologic environment resulting in the phosphorylation of multiple endogenous substrates.