{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMatrix Gla protein (MGP) is a small, vitamin K–dependent extracellular protein that plays a critical role in regulating mineral metabolism primarily by inhibiting vascular calcification. It exerts its inhibitory effect by binding calcium ions, calcium crystals, and bone morphogenetic proteins (BMPs)—a process that depends on vitamin K–mediated post‐translational modifications (e.g. γ‐carboxylation and phosphorylation). Several in vitro and in vivo studies have demonstrated the potency of MGP as a calcification inhibitor, emphasizing its essential function in maintaining vascular health."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinically, circulating species of MGP—in particular its inactive form, dephosphorylated‐uncarboxylated MGP (dp-ucMGP)—have emerged as valuable biomarkers reflecting vitamin K status and vascular calcification burden. Multiple studies in patients with chronic kidney disease, coronary artery and aortic valve calcification, diabetes, and heart failure have shown that lower concentrations of the biologically active form of MGP (or conversely, elevated dp-ucMGP levels) are associated with increased arterial calcification, vascular stiffness, and adverse cardiovascular events. These observations underscore the potential of MGP measurements for risk stratification and for monitoring the efficacy of vitamin K–based interventions aimed at preventing or retarding calcific progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular level, genetic variations as well as finely tuned post‐translational modifications of MGP govern its functional potency. Experimental work has revealed that under different local microenvironments MGP may exhibit dual modulatory effects on vascular calcification—largely by regulating BMP signaling pathways that control the osteogenic differentiation of vascular smooth muscle cells. Several polymorphisms in the MGP gene have been linked to increased susceptibility to myocardial infarction, aortic valve calcification, and other cardiovascular disorders, thus highlighting how genotype–phenotype correlations can impact MGP bioactivity and calcification outcomes. Detailed structure–function analyses have further identified critical residues required for optimal binding to BMPs and for maintaining the inhibitory capacity of MGP."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in vascular calcification inhibition, MGP is increasingly recognized for its broader involvement in extracellular matrix remodeling, regulation of cell–matrix interactions, and even tumor biology. Notably, MGP has been shown to bind extracellular matrix proteins such as vitronectin, suggesting a potential role in modulating cellular adhesion and migratory behavior. Moreover, aberrant MGP expression has been documented in several malignancies—including ovarian cancer, osteosarcoma, and triple‐negative breast cancer—and may contribute to disease progression by influencing tissue remodeling and metastatic potential."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "33", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Benjamin D Parker, Leon J Schurgers, Vincent M Brandenburg, et al. 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