Artigo
Proteinase activity regulation by glycosaminoglycans
Fecha
2002-02-01Registro en:
Brazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 35, n. 2, p. 135-144, 2002.
0100-879X
S0100-879X2002000200001.pdf
S0100-879X2002000200001
10.1590/S0100-879X2002000200001
WOS:000174281400001
Autor
Tersariol, Ivarne Luis dos Santos [UNIFESP]
Pimenta, D.c. [UNIFESP]
Chagas, Jair Ribeiro [UNIFESP]
Almeida, P.c.
Institución
Resumen
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.