Matrix Gla Protein (MGP) in Axial Skeletal Formation of Lizard Tail

Matrix Gla protein (MGP) is a member of the mineral-binding Gla protein family with the molecular weight of 10-kD and known to be involved in cartilage mineralization during development. MGP is expressed in chondrocytes, endothelial cells and vascular smooth muscle cells (Dan et al., 2012; Yao et al., 2009). The five γ-carboxyglutamic acid (Gla) residues of this protein possess high affinity for ions such as calcium and phosphate (Newman et al., 2001; Beazley et al., 2013) which enable it to prevent extracellular matrix calcification by binding the minerals thus limiting the amount of free calcium ions available to initiate calcification (Yagami et al., 1999; Dan et al., 2012). It has been reported that MGP does not only inhibit cartilage mineralization, but it also blocks chondrocyte maturation and both types of ossification (Yagami et al., 1999).

Mineralization begins in matrix vesicles which is associated with MGP and at sites with accumulated proteoglycan. MGP inhibits calcium influx into matrix vesicles, preventing the vesicles to initiate calcification. MGP expression in chick growth plates is low in the proliferative zone, strong in pre-hypertrophic zone, low again in the hypertrophic zone and strong again in the posthypertrophic mineralizing zone demonstrating that MGP is not only involved in mineralization (Yagami et al., 1999), but might also have roles in chondrocyte and cartilage development (Newman et al., 2001). It is still unclear how MGP affects chondrocytes and cartilage maturation but there is possibility that it is related to its calcium binding ability (Yagami et al., 1999). MGP is also known to bind BMP2 and BMP4 forming an inactive complex which might inhibit calcification. MGP influences the delivery of BMP to target cells through the formation of a MGP-Ca2+-BMP aggregate (Yao et al., 2009; Dan et al., 2012; Beazley et al., 2013).

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