Publication . Peres dos Santos, R.; Bensimon-Brito, A.; Gavaia, Paulo J.; Cancela, Leonor
Vitamin K-dependent gamma carboxylation (VKGC) is crucial for posttranslational modification of glutamate residues to form α-carboxy glutamic
acid (Gla) in the presence of reduced vitamin K, molecular oxygen, and carbon dioxide (1). This modification has important implications, mainly
physiological, like homeostasis, signal transduction and bone calcification. This mechanism ensures complete carboxylation of coagulation factors,
and proteins like bone Gla protein (BGP) and matrix Gla protein (MGP), being essential for their biological activity. Warfarin is a known
anticoagulant that inhibits the action of VKGC (2), inhibiting consequently the activity of the referred proteins.
