Document Detail


Functional interactions between matrix metalloproteinases and glycosaminoglycans.
MedLine Citation:
PMID:  23421805     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Similar to most proteinases, matrix metalloproteinases (MMP) do not recognize a consensus cleavage site. Thus, it is not surprising that, in a defined in vitro reaction, most MMPs can act on a wide range of proteins, including many extracellular matrix proteins. However, the findings obtained from in vivo studies with genetic models have demonstrated that individual MMPs act on just a few extracellular protein substrates, typically not matrix proteins. The limited, precise functions of an MMP imply that mechanisms have evolved to control the specificity of proteinase:substrate interactions. We discuss the possibility that interactions with the glycosaminoglycan chains of proteoglycans may function as allosteric regulators or accessory factors directing MMP catalysis to specific substrates. We propose that understanding how the activity of specific MMPs is confined to discreet compartments and targeted to defined substrates via interactions with other macromolecules may provide a means of blocking potentially deleterious MMP-mediated processes at the same time as sparing any beneficial functions.
Authors:
Autumn Tocchi; William C Parks
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Publication Detail:
Type:  Journal Article; Review     Date:  2013-03-08
Journal Detail:
Title:  The FEBS journal     Volume:  280     ISSN:  1742-4658     ISO Abbreviation:  FEBS J.     Publication Date:  2013 May 
Date Detail:
Created Date:  2013-05-10     Completed Date:  2013-07-02     Revised Date:  2013-10-24    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  2332-41     Citation Subset:  IM    
Copyright Information:
© 2013 The Authors Journal compilation © 2013 FEBS.
Affiliation:
Department of Medicine (Pulmonary and Critical Care Medicine), Center for Lung Biology, University of Washington, Seattle, WA 98109, USA.
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MeSH Terms
Descriptor/Qualifier:
Allosteric Regulation
Animals
Catalytic Domain
Consensus Sequence
Enzyme Activation
Glycosaminoglycans / metabolism*
Humans
Matrix Metalloproteinase 7 / metabolism*
Protein Binding
Protein Interaction Mapping*
Protein Structure, Tertiary
Proteolysis
Substrate Specificity
Zinc / metabolism
Grant Support
ID/Acronym/Agency:
P01 HL029594/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Glycosaminoglycans; 7440-66-6/Zinc; EC 3.4.24.23/Matrix Metalloproteinase 7

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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