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Article

Enhanced rate of cleavage at Arg-306 and Arg-506 in coagulation factor Va by Gla domain-mutated human-activated protein C.

The Journal of biological chemistry - 12 Nov 2004

Sun Yong-Hui, Tran Sinh, Norstrøm Eva A, Dahlbäck Björn

Abstract excerpt

A Gla domain-mutated protein C variant, QGNSEDY, modified at positions 10-12, 23, 32-33, and 44, having enhanced affinity for negatively charged phospholipid and increased anticoagulant potential, was used to elucidate the importance of the interaction between the Gla domain and the phospholipid for the ability of activated protein C (APC) to inactivate factor Va (FVa). FVa degradation by wild type (WT)-APC and...

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Identifiers

PMID: 15337738
DOI: 10.1074/jbc.M407366200

Genes

APC

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Enhanced rate of cleavage at Arg-306 and Arg-506 in coagulation factor Va by Gla domain-mutated human-activated protein C.PMID 15337738Read ↗

Factor Va is inactivated by activated protein C in the absence of cleavage sites at Arg-306, Arg-506, and Arg-679.Semantic proximity Read ↗

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Novel APC-cleavage sites in FVa provide insights into mechanisms of action of APC and its cofactor protein S.Semantic proximity Read ↗

The R306G and R506Q mutations in coagulation Factor V reveals additional cleavage sites for Activated Protein C in the R313-R321 region and at R505.Semantic proximity Read ↗

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