The cell-elastin-elastase(s) interacting triade directs elastolysis

Front Biosci (Landmark Ed). 2011 Jan 1;16:707-22. doi: 10.2741/3714.

Abstract

Human elastases have been identified within serine, cysteine and metallopeptidase families. These enzymes are able to adsorb rapidly onto elastin, but they can also bind onto cell surface-associated proteins such as heparan sulfate proteoglycans, both interactions involving enzyme exosites distinct form active site. Immobilization of elastin at the cell surface will create a sequestered microenvironment and will favour elastolysis. Generated elastin peptides are potent matrikines displaying dual biological functions in physiopathology that are described in this review. Among properties, they are potent inducers of protease expression catalyzing collagenolysis or amplifying elastin degradation. The ability of unsaturated fatty acids and heparin(s) to control elastases action are delineated.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adsorption
  • Animals
  • Connective Tissue Diseases / drug therapy
  • Cysteine Endopeptidases / metabolism
  • Elastic Tissue / physiopathology
  • Elastin / metabolism*
  • Fatty Acids, Unsaturated / pharmacology
  • Humans
  • Leukocyte Elastase / metabolism
  • Macrophages / metabolism
  • Metalloendopeptidases / metabolism
  • Neutrophils / enzymology
  • Pancreatic Elastase / metabolism*
  • Receptors, Cell Surface / metabolism*
  • Serine Endopeptidases / metabolism

Substances

  • Fatty Acids, Unsaturated
  • Receptors, Cell Surface
  • Elastin
  • Serine Endopeptidases
  • Pancreatic Elastase
  • Leukocyte Elastase
  • Cysteine Endopeptidases
  • Metalloendopeptidases