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Secondary treatment of external hydrocephalus baby
PAGE \* MERGEFORMAT 17
Secondary treatment of external hydrocephalus baby
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. So far, MMPs have been found and purified at least 20 species of MMPs have been confirmed in almost all organizations, development of body and repair, tumor development, inflammatory reaction played an important role, has become increasingly a cause for attention. In this paper, MMPs in bone development, metabolism and regeneration of the reconstruction process of the latest research advances 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 inhibitors studied. 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 hydrolysis, the former peptide loss, mole
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