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Overview
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Background
Matrix Gla protein, or MGP, is involved in regulating calcification in the extracellular matrix, in particular in cartilage and arteries. MGP is a vitamin K-dependent protein containing five to six residues of g-carboxy-glutamic acid (Gla), a Ca2+ binding amino acid requiring vitamin K-dependent g carboxylase for its formation. In humans MGP is an 84 residue protein along with a 19 amino acid transmembrane signal peptide. A shortened 77 residue form of MGP is found in human bone extracts, likely formed by COOH-terminal processing by carboxypeptidase B-like enzymatic activity. High levels of ex-pression occur in heart, kidney and lung, and over-expression of MGP occurs in the breast cancer cell line 600 PEI. Retinoic acid induces MGP expression in chondrocytes, fibroblasts and osteoblasts. Mutations in the gene coding for MGP can cause Keutel syndrome (KS), associated with abnormal cartilage calcification, substantiating the role of MGP in extracellular matrix calcification regulation. MGP can bind Vitronectin and Fibronectin via its C-terminus; phosphorlyation of MGP occurs near the N-terminus at three serine residues, which are part of a tandemly repeated Ser-X-Glu sequence.
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