Vertebrate mineralized matrix proteins: structure and function.

Abstract:

:The mineralized matrices of enamel, cementum, dentin, calcified cartilage and bone are similar in their ability to form a microenvironment that facilitates deposition of hydroxyapatite. However, they are not identical, as witnessed by the nature of apatite crystals that are formed. Enamel is devoid of collagen; and is composed of enamelins, amelogenins, tuftelin and ameloblastin, first described at this meeting. Cementum, dentin and bone matrices are composed primarily of type I collagen, however, each matrix may also contain unique moieties. The exact composition of cementum is not fully known, but in dentin there are unique matrix proteins, phosphophoryn (dentin phosphoprotein, DPP), a distinctive dentin matrix protein (DMP-1), and dentin sialoprotein (DSP). In bone, dentin and cementum, the matrix proteins include proteoglycans (versican, decorin, biglycan) and hyaluronan, glycoproteins which are often phosphorylated and sulfated (osteonectin, RGD-containing proteins) and gla-containing proteins (matrix gla protein, protein S, osteocalcin). The exact nature of all the non-collagenous proteins of calcified cartilage is not yet fully known. While there are no definitive functions for any of the mineralized matrix proteins to date, they most likely participate in regulation of cell metabolism, matrix deposition and mineralization, and bone turnover.

journal_name

Connect Tissue Res

authors

Robey PG

doi

10.3109/03008209609029183

subject

Has Abstract

pub_date

1996-01-01 00:00:00

pages

131-6

issue

1-4

eissn

0300-8207

issn

1607-8438

journal_volume

35

pub_type

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