Matrix remodelling enzymes, the protease cascade and glycosylation

Citation
Pe. Van Den Steen et al., Matrix remodelling enzymes, the protease cascade and glycosylation, BBA-GEN SUB, 1528(2-3), 2001, pp. 61-73
Citations number
60
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
ISSN journal
03044165 → ACNP
Volume
1528
Issue
2-3
Year of publication
2001
Pages
61 - 73
Database
ISI
SICI code
0304-4165(20011003)1528:2-3<61:MRETPC>2.0.ZU;2-8
Abstract
Glycosylation influences the specific activities of serine proteases includ ing tissue-type plasminogen activator and plasmin which act together in a t ernary complex with fibrin. Serine proteases and matrix metalloproteinases (MMPs), including gelatinase B, participate in a protease cascade to remode l the extracellular matrix. In addition to the recognition and targeting fu nctions of carbohydrates and the fact that they confer protease resistance on glycoproteins, oligosaccharides may extend particular protein domains of matrix remodelling enzymes and fine-control their activities within the co ntext of the extracellular matrix. For example. the sialic acids of gelatin ase B influence the catalytic activity of this enzyme in a complex with the tissue inhibitor of metalloproteinases-1 (TIMP-1). (C) 2001 Elsevier Scien ce B.V. All rights reserved.