Proteinase activity regulation by glycosaminoglycans

Abstract

There are few reports concerning the biological role and the mechanisms of interaction between proteinases and carbohydrates other than those involved in clotting. It has been shown that the interplay of enzymes and glycosaminoglycans is able to modulate the activity of different proteases and also to affect their structures. From the large number of proteases belonging to the well-known protease families and also the variety of carbohydrates described as widely distributed, only few events have been analyzed more deeply. The term "family" is used to describe a group of proteases in which every member shows an evolutionary relationship to at least one other protease. This relationship may be evident throughout the entire sequence, or at least in that part of the sequence responsible for catalytic activity. The majority of proteases belong to the serine, cysteine, aspartic or metalloprotease families. By considering the existing limited proteolysis process, in addition to the initial idea that the proteinases participate only in digestive processes, it is possible to conclude that the function of the enzymes is strictly limited to the cleavage of intended substrates since the destruction of functional proteins would result in normal tissue damage. In addition, the location as well as the eventual regulation of protease activity promoted by glycosaminoglycans can play an essential role in the development of several physiopathological conditions.

Dentin Adhesion and MMPs: A Comprehensive Review

“…Cathepsin activities are regulated by chondroitin sulphate. 91 For example, the collagenolytic activity of cathepsin K requires the formation of a complex between this protease and chondroitin sulfate. In the absence of chondroitin sulfate, which is a major component of ECM including dentin, monomeric cathepsin K does not degrade the triple helical collagen.…”

“…In the absence of chondroitin sulfate, which is a major component of ECM including dentin, monomeric cathepsin K does not degrade the triple helical collagen. 91 The relationship between the activities of MMPs and cysteine cathepsin in intact or carious dentin has been recently reported. 92,93 The activities of MMPs and cysteine cathepsin in carious lesions showed a tenfold increase compared with those of intact dentin.…”

“…Proteoglycans have attached one or more glycosaminoglycan chains, among which is chondroitin sulfate. Cathepsin activities are regulated by chondroitin sulphate . For example, the collagenolytic activity of cathepsin K requires the formation of a complex between this protease and chondroitin sulfate.…”

Atypical EnteropathogenicEscherichia coliSecretes Plasmid Encoded Toxin

“…As a consequence, many of these proteases are involved in the pathogenic processes associated with a number of infections and are, thus, considered important virulence factors [2, 3]. For instance, members of the family of the serine protease autotransporters of the Enterobacteriaceae (SPATE) have been associated with pathogenic strains and are among the virulence proteins predominantly secreted by the pathogens of this family [4].…”

In Situ Zymography: A Molecular Pathology Technique to Localize Endogenous Protease Activity in Tissue Sections

“…7 In addition to their involvement in the pathogenesis of various diseases, proteases play critical roles in normal physiology. 41,50 In this respect, ISZ has been very useful to gain a better understanding of the role of various MMPs in various physiologic processes. In particular, ISZ has been used in several studies to establish the exact contribution of MMPs during the ovarian cycle.…”