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Platelet coagulation factor Va: the major secretory platelet phosphoprotein
MD Rand, M Kalafatis and KG Mann
Department of Biochemistry, University of Vermont College of Medicine,
Burlington 05405-0068.
Platelet-derived coagulation factor Va is the primary secreted substrate
for a thrombin-stimulation-dependent platelet kinase. Human platelet factor
Va, consisting of a molecular weight (M(r)) 105,000 heavy chain and an M(r)
74,000 light chain, incorporates phosphate in at least two sites on the
light chain. Phosphorylated factor Va represents 50% of the secreted
protein-associated phosphate. This modification occurs exclusively at
serine residues and is inhibited by H-7 and staurosporine, which suggests a
protein kinase C (PKC)-mediated event. Purified plasma factor V and Va are
phosphorylated in the light chain region by rat brain PKC. The activity of
platelet factor Va in prothrombinase on platelets is not altered when
phosphorylation is inhibited by staurosporine. Plasma-derived factor Va in
the presence of thrombin stimulated platelets is phosphorylated on both the
heavy chain and the light chain. Plasma factor V and factor Va heavy chain
phosphorylation occurs without light chain phosphorylation in the presence
of added 32P gamma-ATP and non-stimulated or collagen- stimulated platelets
or casein kinase II. This differential phosphorylation of factor Va heavy
and light chain shows two independent platelet kinase activities that act
on factor Va. The heavy chain factor V/Va kinase activity is similar to
casein kinase II, which we have demonstrated previously to act on factor Va
and accelerate activated protein C inactivation of the cofactor. Our data
show platelet-dependent phosphorylation of platelet and plasma factor V and
Va resulting in significant covalent modifications of the cofactor. These
modifications may play a role in directing the extracellular distribution
of factor V and factor Va.
Volume 83,
Issue 8,
pp. 2180-2190,
04/15/1994
Copyright © 1994 by The American Society of Hematology
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