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

Trends Cell Biol. 2003 Jul;13(7):366-75. doi: 10.1016/s0962-8924(03)00129-6.


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.

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites / physiology
  • Eukaryotic Cells / metabolism*
  • Eukaryotic Cells / ultrastructure
  • Extracellular Matrix / metabolism*
  • Extracellular Matrix / ultrastructure
  • Extracellular Matrix Proteins / metabolism*
  • Humans
  • Peptide Fragments / physiology
  • Peptide Hydrolases / metabolism
  • Protein Structure, Tertiary / physiology


  • Extracellular Matrix Proteins
  • Peptide Fragments
  • Peptide Hydrolases