alexa Role of matrix metalloproteinases

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Role of matrix metalloproteinases

Proteases are enzymes that catalyze proteins by hydrolyzing peptide bonds that link the amino acids. Metzincins are a universally expressed family of multidomain zinc (II)-dependent endopeptidases, which includes metalloproteases such as matrix metalloproteinases (MMPs). A highly conserved motif containing 3 histidines that bind to zinc at the catalytic site and a conserved methionine that sits beneath the active site distinguishes the metzincin super family from others. Metzincins, apart from participating in the digestion of proteins, tissue development, maintenance and remodelling, are also involved in highly specific cleavage events to activate or inactivate themselves or other proenzymes or active enzymes and bioactive peptides. The MMPs dependence on metal ions as cofactors, their ability to degrade extracellular matrix and their specific evolutionary DNA sequence distinguish them from other endopeptidases. High levels of MMPs are usually observed in disease state and pathological processes involved in connective tissue degradation such as inflammation. Timely degradation of extracellular matrix (ECM) is an important feature of tissue repair and modelling and is precisely regulated under normal physiological conditions, but when dysregulated, it is the cause of many diseases such as cancer, fibrosis in pancreatitis, etc. Various types of proteinases are known to be implicated in ECM degradation, however, the major enzymes are MMPs also known as matrixins.

 
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