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Unravelling the different functions of protein kinase C isoforms in platelets
Author(s) -
Heemskerk Johan W.M.,
Harper Matthew T.,
Cosemans Judith M.E.M.,
Poole Alastair W.
Publication year - 2011
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/j.febslet.2011.05.017
Subject(s) - gene isoform , protein kinase c , platelet , microbiology and biotechnology , kinase , phosphorylation , platelet activation , thrombus , biology , biochemistry , chemistry , gene , immunology , medicine
Platelets tightly regulate haemostasis and arterial thrombosis. Protein kinase C (PKC) is involved in most platelet responses implicated in thrombus formation. Recent pharmacological and mouse gene knockout approaches show that the conventional PKC isoforms and the novel PKC isoforms contribute in distinct ways to these platelet responses. We hypothesize that, in platelets and other cells, the characteristic functions of PKC isoforms are established through unique activation mechanisms and unique interacting protein partners, which result in isoform‐specific patterns of substrate phosphorylation. For identifying the substrate proteins in a living cell, new methodology is available and discussed.