factor IXa associates with cell membrane

Stable Identifier
Reaction [transition]
Homo sapiens
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Membrane-bound thrombin-activated factor VIII (fVIIIa) functions as a cofactor for factor IXa in the factor Xase complex. Factors VIIIa and IXa associate with anionic phospholipid surfaces with high affinity (Gilbert et al. 1990, Mertens & Bertina 1984, Mertens et al. 1984; Greengard et al. 1986). Studies using physiologic surfaces provide evidence for coordinated binding interactions of the enzyme, cofactor and substrate to discrete surface structures. For example, the presence of both (active site-modified) factor IXa and factor X increased both the number and the affinity of binding sites on activated platelets for factor VIIIa (Ahmad et al. 2000). However classical receptors for the constituents of factor Xase have not been identified (Fay 2004).

Literature References
PubMed ID Title Journal Year
6334516 Binding of human blood-coagulation Factors IXa and X to phospholipid membranes

Bertina, RM, Cupers, R, Van Wijngaarden, A, Mertens, K

Biochem. J. 1984
3017409 Binding of coagulation factor XI to washed human platelets

Heeb, MJ, Griffin, JH, Ersdal, E, Greengard, JS, Walsh, PN

Biochemistry 1986
Orthologous Events
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