Document Detail

Tales from the crypt[ic] sites of the extracellular matrix.
MedLine Citation:
PMID:  12837607     Owner:  NLM     Status:  MEDLINE    
Proteolytic cleavage of extracellular matrix (ECM) proteins by matrix metalloproteinases and/or conformational changes unmask "cryptic" sites and liberate fragments with biological activities that are not observed in the intact molecule. Cryptic sites and fragments of ECM macromolecules have been implicated in many events governed by cell-ECM interactions, such as migration, invasion, adhesion and differentiation. The unmasking of cryptic sites is a tightly controlled process, reflecting the importance of cryptic ECM functions. This review summarizes and evaluates the current developments regarding cryptic regulatory ECM signals found as ECM-tethered protein epitopes or fragments.
Susann Schenk; Vito Quaranta
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Trends in cell biology     Volume:  13     ISSN:  0962-8924     ISO Abbreviation:  Trends Cell Biol.     Publication Date:  2003 Jul 
Date Detail:
Created Date:  2003-07-02     Completed Date:  2003-09-05     Revised Date:  2005-11-16    
Medline Journal Info:
Nlm Unique ID:  9200566     Medline TA:  Trends Cell Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  366-75     Citation Subset:  IM    
The Scripps Research Institute, Department of Cell Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
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MeSH Terms
Binding Sites / physiology
Eukaryotic Cells / metabolism*,  ultrastructure
Extracellular Matrix / metabolism*,  ultrastructure
Extracellular Matrix Proteins / metabolism*
Peptide Fragments / physiology
Peptide Hydrolases / metabolism
Protein Structure, Tertiary / physiology
Reg. No./Substance:
0/Extracellular Matrix Proteins; 0/Peptide Fragments; EC 3.4.-/Peptide Hydrolases

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