Collagenases and tissue inhibitors of metalloproteinases: a functional balance in tissue degradation

Oral Diseases
J J Reynolds

Abstract

Members of the family of matrix metalloproteinases (MMPs; also called collagenases or matrixins) are key enzymes in matrix degradation. They function at neutral pH and can digest synergistically all the matrix macromolecules. Biochemical and clonal studies indicate that there are three major groups: the specific collagenases cleave interstitial collagens; the gelatinases degrade types IV, V, VII and XI collagens and act synergistically with collagenases by degrading denatured collagens (gelatins); and the stromelysins have broader specificity and can degrade basement membrane collagens as well as proteoglycans and matrix glycoproteins. Others not in these groups are matrilysin, metalloelastase and a recently cloned membrane-bound metalloproteinase. MMPs are Zn(2+)- and Ca(2+)-requiring endopeptidases and are secreted in a latent proform: activation involves the loss of a propeptide. Naturally occurring inhibitors, TIMPs (Tissue Inhibitors of MetalloProteinases), are important controlling factors in the actions of MMPs, and tissue destruction in disease processes often correlates with an imbalance of MMPs over TIMPs. The major inhibitor is TIMP-1 (or TIMP), a 30-kDa glycoprotein that is synthesised by most cells. A second unglyc...Continue Reading

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