factor IXa associates with cell membrane

Stable Identifier
R-HSA-5607023
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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 (Respective Kd values ?1 nM and ~15nM, Gilbert et al. 1990, Mertens & Bertina 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
3017409 Binding of coagulation factor XI to washed human platelets

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

Biochemistry 1986
6334516 Binding of human blood-coagulation Factors IXa and X to phospholipid membranes

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

Biochem. J. 1984
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