Tales from the crypt[ic] sites of the extracellular matrix.
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.
Schenk
Susann
S
The Scripps Research Institute, Department of Cell Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. sschenk@scripps.edu
Quaranta
Vito
V
D000818:Animals; D001665:Binding Sites / Q000502:physiology; D005057:Eukaryotic Cells / Q000378:metabolism* / Q000648:ultrastructure; D005109:Extracellular Matrix / Q000378:metabolism* / Q000648:ultrastructure; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006801:Humans; D010446:Peptide Fragments / Q000502:physiology; D010447:Peptide Hydrolases / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000502:physiology
D016326:Extracellular Matrix Proteins; D010446:Peptide Fragments; D010447:Peptide Hydrolases