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J. Biol. Chem., Vol. 256, Issue 11, 5532-5535, Jun, 1981
WG Owen and CT Esmon
Thrombin-catalyzed activation of Protein C is accelerated by a human
endothelial cell surface cofactor. The cofactor occurs also on mouse
hemangioma cells (a transformed endothelial cell line), but not on cultured
human smooth muscle cells or fibroblasts. The cofactor remains bound to the
cell surface during Protein C activation. The cofactor is saturable with
respect to both Protein C (Km = 0.72 +/- 0.07 microM) and thrombin (Km =
0.48 +/- 0.05 nM). Diisopropylphosphoryl-thrombin is a competitive
inhibitor of the cofactor-dependent reaction with Ki = 0.56 +/- 0.1 nM.
Prothrombin Fragment 1, the peptide derived from prothrombin that retains
phospholipid binding capacity, does not inhibit activation of Protein C
when present in a 7:1 molar excess over Protein C. Platelet Factor 4 (20
microgram/ml) also fails to inhibit Protein C activation. It is concluded
that the endothelial cell provides a surface on which Protein C can be
activated under physiological conditions.
Functional properties of an endothelial cell cofactor for thrombin- catalyzed activation of protein C
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