Blood: Different mutations in GGCX have different effects on the biological function of vitamin K-dependent proteins.

GLUT is a complete membrane protein that catalyzes the translation of multivitamin K-dependent (VKD) proteins and participates in a variety of physiological processes, including clotting, vascular calcification, and bone metabolism.
naturally occurring GGCX mutations are associated with a number of different clinical esolyses.
, however, the genotype-esotypic correlation of GGCX remains elusive.
study, the researchers systematically studied the effects of all naturally occurring GGCX mutations on the carbaboxing of three structural-functional VKD proteins.
GGCX mutations were instantaneously imported into GGCX defective human embryo 293 cells with stable expression of chimic coagulation factors, substrate GLA protein (MGP) or osteocalcin as VKD reporting proteins to evaluate the effergization efficiency of these reported proteins.
results show that GGCX mutations have different effects on the efflurgization of these reported proteins and the efficiency of vitamin K as a cofactor.
these reported proteins are ionized by the C-end truncation mutation (R704X), indicating that the C-end of GGCX plays a key role in the binding of osteocalcin, but not in the binding of clotting factors and MGP.
protein-protein interactions between GGCX and its protein substrates in living cells were detected using dual-molecule fluorescence complementarities and chemical cross-linking experiments.
addition, using microgene shearing experiments, the researchers demonstrated that several GGCX misalignment mutations affected the cutting of GGCX mRNA pregenitors, rather than altering the corresponding amino acid residues.
, the results of this study illustrate the correlation between GGCX genotypes and their clinical esotypes, and explain the reasons why vitamin K therapy can correct hemorrhagic diseases but are ineffective for non-hemorrhagic diseases.
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