Matrix Gla protein (MGP) is member of a family of vitamin K2 dependent, Gla-containing proteins. MGP has a high affinity binding to calcium ions, similar to other Gla-containing proteins. The protein acts as an inhibitor of vascular mineralization and plays a role in bone organization.[5][6]
MGP | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | MGP, MGLAP, NTI, GIG36, matrix Gla protein | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 154870 MGI: 96976 HomoloGene: 693 GeneCards: MGP | ||||||||||||||||||||||||||||||||||||||||||||||||||
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MGP is found in a number of body tissues in mammals, birds, and fish. Its mRNA is present in bone, cartilage, heart, and kidney.[7]
It is present in bone together with the related vitamin K2-dependent protein osteocalcin. In bone, its production is increased by vitamin D.
The MGP was linked to the short arm of chromosome 12 in 1990.[8] Its mRNA sequence length is 585 bases long in humans.[9]
MGP and osteocalcin are both calcium-binding proteins that may participate in the organisation of bone tissue. Both have glutamate residues that are post-translationally carboxylated by the enzyme gamma-glutamyl carboxylase in a reaction that requires Vitamin K hydroquinone.
Abnormalities in the MGP gene have been linked with Keutel syndrome, a rare condition characterised by abnormal calcium deposition in cartilage, peripheral stenosis of the pulmonary artery, and midfacial hypoplasia.[10]
Mice that lack MGP develop to term but die within two months as a result of arterial calcification which leads to blood-vessel rupture.[6]