Matrix remodelling enzymes, the protease cascade and glycosylation.

Glycosylation influences the specific activities of serine proteases including tissue-type plasminogen activator and plasmin which act together in a ternary complex with fibrin. Serine proteases and matrix metalloproteinases (MMPs), including gelatinase B, participate in a protease cascade to remode...

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Main Authors: Van den Steen, P, Opdenakker, G, Wormald, M, Dwek, R, Rudd, P
Format: Journal article
Language:English
Published: 2001
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author Van den Steen, P
Opdenakker, G
Wormald, M
Dwek, R
Rudd, P
author_facet Van den Steen, P
Opdenakker, G
Wormald, M
Dwek, R
Rudd, P
author_sort Van den Steen, P
collection OXFORD
description Glycosylation influences the specific activities of serine proteases including tissue-type plasminogen activator and plasmin which act together in a ternary complex with fibrin. Serine proteases and matrix metalloproteinases (MMPs), including gelatinase B, participate in a protease cascade to remodel the extracellular matrix. In addition to the recognition and targeting functions 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 context of the extracellular matrix. For example, the sialic acids of gelatinase B influence the catalytic activity of this enzyme in a complex with the tissue inhibitor of metalloproteinases-1 (TIMP-1).
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spelling oxford-uuid:69f6e30c-c3a5-433c-b618-1c5005736d9e2022-03-26T18:54:24ZMatrix remodelling enzymes, the protease cascade and glycosylation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:69f6e30c-c3a5-433c-b618-1c5005736d9eEnglishSymplectic Elements at Oxford2001Van den Steen, POpdenakker, GWormald, MDwek, RRudd, PGlycosylation influences the specific activities of serine proteases including tissue-type plasminogen activator and plasmin which act together in a ternary complex with fibrin. Serine proteases and matrix metalloproteinases (MMPs), including gelatinase B, participate in a protease cascade to remodel the extracellular matrix. In addition to the recognition and targeting functions 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 context of the extracellular matrix. For example, the sialic acids of gelatinase B influence the catalytic activity of this enzyme in a complex with the tissue inhibitor of metalloproteinases-1 (TIMP-1).
spellingShingle Van den Steen, P
Opdenakker, G
Wormald, M
Dwek, R
Rudd, P
Matrix remodelling enzymes, the protease cascade and glycosylation.
title Matrix remodelling enzymes, the protease cascade and glycosylation.
title_full Matrix remodelling enzymes, the protease cascade and glycosylation.
title_fullStr Matrix remodelling enzymes, the protease cascade and glycosylation.
title_full_unstemmed Matrix remodelling enzymes, the protease cascade and glycosylation.
title_short Matrix remodelling enzymes, the protease cascade and glycosylation.
title_sort matrix remodelling enzymes the protease cascade and glycosylation
work_keys_str_mv AT vandensteenp matrixremodellingenzymestheproteasecascadeandglycosylation
AT opdenakkerg matrixremodellingenzymestheproteasecascadeandglycosylation
AT wormaldm matrixremodellingenzymestheproteasecascadeandglycosylation
AT dwekr matrixremodellingenzymestheproteasecascadeandglycosylation
AT ruddp matrixremodellingenzymestheproteasecascadeandglycosylation