IMR Press / FBL / Volume 16 / Issue 8 / DOI: 10.2741/3887

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Matrix vesicles: structure, composition, formation and function in calcification
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1 Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208 , USA
Academic Editor:Ermanno Bonucci
Front. Biosci. (Landmark Ed) 2011, 16(8), 2812–2902; https://doi.org/10.2741/3887
Published: 1 June 2011
(This article belongs to the Special Issue The biomineralization process: mechanism, problems, perspectives)
Abstract

Matrix vesicles (MVs) induce calcification during endochondral bone formation. Experimental methods for structural, compositional, and functional analysis of MVs are reviewed. MV proteins, enzymes, receptors, transporters, regulators, lipids and electrolytes are detailed. MV formation is considered from both structural and biochemical perspectives. Confocal imaging of Ca2+ and H+ were used to depict how living chondrocytes form MVs. Biochemical studies revealed that coordinated mitochondrial Ca2+ and Pi metabolism produce MVs containing a nucleational complex (NC) of amorphous calcium phosphate, phosphatidylserine and annexin A5 – all critical to the mechanism of mineral nucleation. Reconstitution of the NC and modeling with unilamellar vesicles reveal how the NC transforms into octacalcium phosphate, regulated by Mg2+, Zn2+ and annexin A5. Extravasation of intravesicular mineral is mediated by phospholipases and tissue-nonspecific alkaline phosphatase (TNAP). In the extravesicular matrix, hydroxyapatite crystal propagation is enhanced by cartilage collagens and TNAP, which destroys inhibitory PPi, and by metalloproteases that degrade proteoglycans. Other proteins also modulate mineral formation. Recent findings from single and multiple gene knockouts of TNAP, NPP1, ANK, PHOSPHO1, and Annexin A5 are reviewed.

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