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Prepublished online as a Blood First Edition Paper on October 10, 2002; DOI 10.1182/blood-2002-08-2384.
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Blood, 15 February 2003, Vol. 101, No. 4, pp. 1392-1399
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
PKD: a new protein kinase C-dependent pathway in
platelets
Margaret J. Stafford,
Steve P. Watson, and
Catherine
J. Pears
From the Department of Biochemistry, University of
Oxford, Oxford, United Kingdom, and the Department of
Pharmacology, University of Oxford, Oxford, United
Kingdom.
Protein kinase D (PKD, also known as PKCµ) is closely related to
the protein kinase C superfamily but is differentially regulated and
has a distinct catalytic domain that shares homology with Ca2+-dependent protein kinases. PKD is highly expressed in
hematopoietic cells and undergoes rapid and sustained activation upon
stimulation of immune receptors. PKD is regulated through
phosphorylation by protein kinase C (PKC). In the present study, we
show that PKD is expressed in human platelets and that it is
rapidly activated by receptors coupled to heterotrimeric G-proteins or
tyrosine kinases. Activation of PKD is mediated downstream of PKC.
Strong agonists such as convulxin, which acts on GPVI, and thrombin
cause sustained activation of PKC and PKD, whereas the thromboxane
mimetic U46619 gives rise to transient activation of PKC and PKD.
Activation of PKD by submaximal concentrations of phospholipase
C-coupled receptor agonists is potentiated by
Gi-coupled receptors (eg, adenosine diphosphate
and epinephrine). This study shows that PKD is rapidly activated by a
wide variety of platelet agonists through a PKC-dependent pathway.
Activation of PKD enables phosphorylation of a distinct set of
substrates to those targeted by PKC in platelets.
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