Biochemical characterization of matrix vesicles from bone and cartilage

Mühlrád, András; Setton, Adrianne; Sela, J.; I, Bab; Deutsch, D.

doi:10.1016/0221-8747(83)90008-5

Cited by 10 publications

(2 citation statements)

References 29 publications

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“…Since the primary Ca phosphate crystallites exhibit a chain-like character these matrix molecules should also be strands inside the MVs with a fibril-like character. Up to now only F-actin (Muhlrad et al, 1981(Muhlrad et al, , 1982(Muhlrad et al, , 1984Stein et al, 1981;Morris et al, 1983;Oosawa, 1993) and Annexin V seem to appear in the interior part of the MVs with a fibrous character (Morris et al, 1992). According to our knowledge it is mainly F-actin which represents fibrous strands.…”

Section: Discussionmentioning

confidence: 80%

Early mineralization of matrix vesicles in the epiphyseal growth plate

Plate

Tkotz

Wiesmann

et al. 1996

Journal of Microscopy

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Matrix vesicles (MVs) induce the primary mineralization in collagen-rich hard tissues such as bone, mineralizing cartilage and dentine. Calcium and phosphate ions accumulate at the inner MV membrane. This accumulation takes place in association with phospholipids alone and/or in association with Annexin V, which displays Ca ion channel activity when inserted in membranes; consequently, Annexin V may be involved in Ca uptake by matrix vesicles. The first crystal nuclei are formed at these macromolecules of the MV inner membrane. They grow to stable nanometre-sized particles, dots, which coalesce to form chains of dots along the macromolecules of the MV inner membrane. At the same time, or shortly afterwards, chains of these Ca phosphate dots also develop inside the MVs. The measured centre-to-centre distances between these dots represent approximately the distances between the nucleating sites, called active sites, along the MV matrix molecules. The mineralization does not stop at the MV membrane but expands continuously into the extravesicular region in radial directions to form nodules. These radiating Ca phosphate chains, which coalesce to form needles, are composed of such primary dots, which have developed at the nucleating sites of the corresponding macromolecules.

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Section: Discussionmentioning

confidence: 80%

Early mineralization of matrix vesicles in the epiphyseal growth plate

Plate

Tkotz

Wiesmann

et al. 1996

Journal of Microscopy

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“…Several early studies explored the sodium dodecyl sulfate -polyacrylamide gel electrophoresis (SDS-PAGE) patterns of proteins present in MV using crude collagenase digestion (88)(89)(90), as well as MVEM (55-57, 65, 68) and culture media vesicles (58,69,70,91). While there was considerable variability in the patterns of MV proteins from the various tissues, animal species, and MV preparations, certain protein bands nevertheless were consistently observed; these include two or three intensely staining bands in the 30-38 kDa range, two strongly staining bands at 40-48 kDa, and bands frequently appearing in the 55 kDa, 90-100 kDa and 130-150 kDa range.…”

Section: Early Sds-page Studiesmentioning

confidence: 99%

Matrix vesicles: structure, composition, formation and function in calcification

Wuthier

Lipscomb²

2011

Front Biosci

160

230

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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 Ca(2+) and H(+) were used to depict how living chondrocytes form MVs. Biochemical studies revealed that coordinated mitochondrial Ca(2+) 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 Mg(2+), Zn(2+) 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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Primary Mineralization

Sela¹

2012

Principles of Bone Regeneration

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Biochemical characterization of matrix vesicles from bone and cartilage

Cited by 10 publications

References 29 publications

Early mineralization of matrix vesicles in the epiphyseal growth plate

Early mineralization of matrix vesicles in the epiphyseal growth plate

Matrix vesicles: structure, composition, formation and function in calcification

Primary Mineralization

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