NDLI: Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va.

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Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va.

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Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Griffin, J. H. Hackeng, T. M. Heeb, M. J. Kojima, Y.
Description	Country affiliation: United States Author Affiliation: Heeb MJ ( Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, California 92037, USA. heeb@scripps.edu)
Abstract	Inactivation due to cleavage of Factor Va (FVa) at Arg 506 by activated protein C (APC) helps to downregulate blood coagulation. To identify potential functional roles of amino acids near Arg 506, synthetic overlapping pentadecapeptides comprising FVa heavy chain residues 481-525 were tested for their ability to inhibit prothrombin activation by prothrombinase complexes [Factor Xa (FXa):FVa:phospholipids:Ca2+]. The most potent inhibition was observed for peptide VP493 (residues 493-506), with 50% inhibition at 2.5 microM. VP493 also inhibited FXa in plasma in FXa-1-stage clotting assays by 50% at 3 microM. When the C-terminal carboxamide group of VP493 was replaced by a carboxyl group, most prothrombinase inhibitory activity was lost. VP493 preincubated with FXa inhibited prothrombinase with a pattern of mixed inhibition. Homologous peptides from Factor VIII sequences did not inhibit prothrombinase. Affinity-purified antibodies to VP493 inhibited prothrombinase activity and prolonged FXa-1-stage clotting times. VP493 also blocked the ability of protein S to inhibit prothrombinase independently of APC. Immobilized VP493 bound specifically with similar affinity to both FXa and protein S (Kd approximately 40 nM), but did not measurably bind prothrombin or APC. These studies suggest that FVa residues 493-506 contribute to binding sites for both FXa and protein S, providing a rationale for the ability of protein S to negate the protective effect of FXa toward APC cleavage of FVa. Possible loss of this FVa binding site for FXa due to cleavage at Arg 506 by APC may help explain why this cleavage causes 40% decrease in FVa activity and facilitates inactivation of FVa.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Factor Va Chemistry Metabolism Factor Xa Peptide Fragments Protein S Amino Acid Sequence Antibodies Pharmacology Anticoagulants Binding Sites Enzyme Inhibitors Factor Xa Inhibitors Molecular Sequence Data Antagonists & Inhibitors Thromboplastin Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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