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Phosphatidylserine Regulation of Coagulation Proteins Factor IXa and Factor VIIIa.

Abstract
Blood coagulation is an intricate process, and it requires precise control of the activities of pro- and anticoagulant factors and sensitive signaling systems to monitor and respond to blood vessel insults. These requirements are fulfilled by phosphatidylserine, a relatively miniscule-sized lipid molecule amid the myriad of large coagulation proteins. This review limelight the role of platelet membrane phosphatidylserine (PS) in regulating a key enzymatic reaction of blood coagulation; conversion of factor X to factor Xa by the enzyme factor IXa and its cofactor factor VIIIa. PS is normally located on the inner leaflet of the resting platelet membrane but appears on the outer leaflet surface of the membrane surface after an injury happens. Human platelet activation leads to exposure of buried PS molecules on the surface of the platelet-derived membranes and the exposed PS binds to discrete and specific sites on factors IXa and VIIIa. PS binding to these sites allosterically regulates both factors IXa and VIIIa. The exposure of PS and its binding to factors IXa/VIIIa is a vital step during clotting. Insufficient exposure or a defective binding of PS to these clotting proteins is responsible for various hematologic diseases which are discussed in this review.
AuthorsRinku Majumder
JournalThe Journal of membrane biology (J Membr Biol) Vol. 255 Issue 6 Pg. 733-737 (12 2022) ISSN: 1432-1424 [Electronic] United States
PMID36098799 (Publication Type: Journal Article, Review, Research Support, N.I.H., Extramural)
Copyright© 2022. This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply.
Chemical References
  • Factor VIIIa
  • Factor IXa
  • Phosphatidylserines
  • Factor X
  • Factor Xa
Topics
  • Humans
  • Factor VIIIa (chemistry, metabolism)
  • Factor IXa (chemistry, metabolism)
  • Phosphatidylserines (chemistry)
  • Factor X (metabolism)
  • Factor Xa (metabolism)
  • Kinetics
  • Binding Sites

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