Disease relevance of Ggcx

• Combined with the reported presence of vitamin K dependent carboxylase in B16 cells and the cytotoxicity of warfarin towards B16 cells this suggests an active vitamin K cycle in these melanoma cells that may be essential for survival [1].
• The presence of gamma-glutamyl carboxylase was also described in several murine tumors including both carcinomas and fibrosarcomas [2].

High impact information on Ggcx

• The vitamin K-dependent gamma-glutamyl carboxylase catalyzes the posttranslational conversion of glutamic acid to gamma-carboxyglutamic acid, an amino acid critical to the function of the vitamin K-dependent blood coagulation proteins [3].
• Vitamin K-dependent carboxylase is demonstrated in skin microsomes from humans, rats, rabbits, and mice [4].
• The marine snail Conus is the sole invertebrate wherein both the vitamin K-dependent carboxylase and its product, gamma-carboxyglutamic acid, have been identified [5].
• Expression of this cDNA in COS cells or insect cells yielded vitamin K-dependent carboxylase activity and vitamin K-dependent epoxidase activity [5].
• Since matrix GLA protein function requires gamma-carboxylation of its glutamate residues by a vitamin K dependent carboxylase, warfarin treatment may affect vascular calcification by blocking vitamin K and hence matrix GLA protein activity [6].

Enzymatic interactions of Ggcx

• The liver microsomal vitamin K-dependent carboxylase catalyzes the post-translational conversion of specific glutamyl to gamma-carboxyglutamyl (Gla) residues in precursor forms of a limited number of proteins [7].

References