Proteinase activity regulation by glycosaminoglycans
Braz. j. med. biol. res
;
35(2): 135-144, Feb. 2002. tab
Article
in English
| LILACS, SES-SP
| ID: lil-303555
RESUMO
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
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Endopeptidases
/
Glycosaminoglycans
Limits:
Animals
/
Humans
Language:
English
Journal:
Braz. j. med. biol. res
Year:
2002
Type:
Article
/
Congress and conference
Institution/Affiliation country:
Universidade Federal de Säo Paulo/BR
/
Universidade de Mogi das Cruzes/BR
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