Interstitial collagen catabolism

J Biol Chem. 2013 Mar 29;288(13):8785-93. doi: 10.1074/jbc.R113.451211. Epub 2013 Feb 19.

Abstract

Interstitial collagen mechanical and biological properties are altered by proteases that catalyze the hydrolysis of the collagen triple-helical structure. Collagenolysis is critical in development and homeostasis but also contributes to numerous pathologies. Mammalian collagenolytic enzymes include matrix metalloproteinases, cathepsin K, and neutrophil elastase, and a variety of invertebrates and pathogens possess collagenolytic enzymes. Components of the mechanism of action for the collagenolytic enzyme MMP-1 have been defined experimentally, and insights into other collagenolytic mechanisms have been provided. Ancillary biomolecules may modulate the action of collagenolytic enzymes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Arthritis / metabolism
  • Binding Sites
  • Catalysis
  • Cathepsin K / metabolism*
  • Collagen / chemistry
  • Collagen / metabolism*
  • Gene Expression Regulation, Enzymologic*
  • Humans
  • Leukocyte Elastase / metabolism*
  • Matrix Metalloproteinase 1 / metabolism
  • Matrix Metalloproteinases / metabolism*
  • Metabolism
  • Molecular Conformation
  • Neoplasms / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Serine / chemistry
  • Substrate Specificity

Substances

  • Serine
  • Collagen
  • Leukocyte Elastase
  • Cathepsin K
  • Matrix Metalloproteinases
  • Matrix Metalloproteinase 1