Phosphorylation of protein S by platelet kinases enhances its activated protein C cofactor activity
نویسندگان
چکیده
منابع مشابه
Dissociation of activated protein C functions by elimination of protein S cofactor enhancement.
Activated protein C (APC) plays a critical anticoagulant role in vivo by inactivating procoagulant factor Va and factor VIIIa and thus down-regulating thrombin generation. In addition, APC bound to the endothelial cell protein C receptor can initiate protease-activated receptor-1 (PAR-1)-mediated cytoprotective signaling. Protein S constitutes a critical cofactor for the anticoagulant function ...
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Among the drugs that are known to relax the vascular smooth muscle and regulate other cellular functions, beta-adrenergic agonists and nitric oxide-containing compounds are some of the most effective ones. The mechanisms of these drugs are thought to lower agonist-induced intracellular [Ca(2+)] by increasing intracellular cAMP and cGMP, activating their respective protein kinases. However, the ...
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متن کاملRegulation of factor VIIIa by human activated protein C and protein S: inactivation of cofactor in the intrinsic factor Xase.
Factor VIIIa is a trimer of A1, A2, and A3-C1-C2 subunits. Inactivation of the cofactor by human activated protein C (APC) results from preferential cleavage at Arg336 within the A1 subunit, followed by cleavage at Arg562 bisecting the A2 subunit. In the presence of human protein S, the rate of APC-dependent factor VIIIa inactivation increased several-fold and correlated with an increased rate ...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2013
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fj.12-225961