Matrix gla protein

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Matrix gla protein (MGP) is member of a family of vitamin-K 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.[1][2]

MGP is found in number body tissues in mammals, birds, and fish. Its mRNA is present in bone, cartilage, heart, and kidney.[3]

It is present in bone together with the related vitamin K-dependent protein osteocalcin. In bone, its production is increased by vitamin D.

Genetics

The MGP was linked to the short arm of chromosome 12 in 1990.[4] Its mRNA sequence length is 585 bases long in humans.[5]

Physiology

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.

This process also occurs with a number of proteins involved in coagulation: prothrombin, factor VII, factor IX and factor X, protein C, protein S and protein Z.

Role in disease

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.[6]

Mice that lack MGP develop to term but die within two months as a result of arterial calcification which leads to blood-vessel rupture.[2]

References

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