Heparin cofactor 2 (SERPIND1) binds activated thrombin (factor IIa)

Stable Identifier
Reaction [binding]
Homo sapiens
SERPIND1 binds activated thrombin (factor IIa)
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SERPIND1 (Heparin cofactor 2) is a serine endopeptidase inhibitor (SERPIN) that acts as a pseudosubstrate for activated thrombin, forming a stable complex which has the effect of inactivating thrombin protease activity (Church et al. 1985), although with slower kinetics than SERPINC1 (antithrombin-III). The presence of the glycosaminoglycans heparin or dermatan sulphate increases thrombin inactivation 1000-fold (Van Deerlin & Tollefsen 199) by facilitating the interaction between the active site of thrombin and the reactive site of SERPIND1. Thrombin specificity is conferred by a 90-residue N-terminal extension that contains two acidic motifs containing sulphated Tyr residues, resembling the C-terminus of hirudin (Tollefsen et al. 1997). SERPIND1 also inhibits chymotrypsin and neutrophil cathepsin G, but in a glycosaminoglycan independent manner (Church et al. 1985). In contrast to SERPINC1 deficiency, SERPIND1 deficiency is not associated with venous thrombosis (Corral et al. 2004).

Literature References
PubMed ID Title Journal Year
3863104 Inhibition of chymotrypsin by heparin cofactor II

Church, FC, Griffith, MJ, Noyes, CM

Proc. Natl. Acad. Sci. U.S.A. 1985
This event is regulated
Positively by
Orthologous Events
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