Tales from the crypt[ic] sites of the extracellular matrix.

Schenk S, Quaranta V
Trends Cell Biol. 2003 13 (7): 366-75

PMID: 12837607

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.

MeSH Terms (9)

Animals Binding Sites Eukaryotic Cells Extracellular Matrix Extracellular Matrix Proteins Humans Peptide Fragments Peptide Hydrolases Protein Structure, Tertiary

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