Matrix metalloproteinases and bone remodeling.doc

 PAGE \* MERGEFORMAT 14 Matrix metalloproteinases and bone remodeling Keywords:: matrix metalloproteinase; bone remodeling Matrix metalloproteinase (matrix metalloproteinase, MMPs) are involved in degradation of the body, including bones, including a variety of extracellular matrix (extracellular matrix, ECM) protease family. Since 1962, Gross and Lapie re the first report of collagenase (Collagenase) has been applied to other components of the ECM matrix metalloproteinase been reported. To date, and purified MMPs have been found at least 20 species of MMPs have been confirmed in almost all organizations, development and body repair, tumor, inflammation, etc. played an important role, has increasingly attracted attention. In this paper, MMPs in bone development, metabolism and regeneration of the reconstruction process of the latest developments are reviewed. 1 MMPs the general characteristics of MMPs are a group containing Zn2 that can degrade extracellular matrix protease, usually in the neutral condition to play activity, there are ca2 when the activity involved in the greatest. Its activity inhibited by the chelating agents, but not by serine, cysteine, aspartic protease inhibitor class. With the cDNA predicted amino acid sequence, suggesting that some mammalian MMPs between the various types of enzyme, its structure has a high degree of constancy. All members of the MMPs family have some common amino acid sequence and structure of the domain. These structural domains are: pre-peptide domain, signal peptide, catalytic domain, rennet-like domain, transmembrane domain and so on. Through the modification of one of these areas increase or decrease in the formation of different MMPs. As in the catalytic domain of gelatinase a period of fibronectin-like insert, MMP-7 lack of rennet-like domain, while the membrane-type MMPs contains a transmembrane domain, and so on. Zymogen forms of MMPs are secreted, its activation requires protein hydrol