Open Access
Article
The cell-elastin-elastase(s) interacting triade directs elastolysis
William Hornebeck1,Herve Emonard1
1
Universite de Reims Champagne-Ardenne, UMR 6237 CNRS, Faculte de Medecine, 51 rue Cognacq Jay, 51095 Reims Cedex, France. william.hornebeck@univ-reims.fr
DOI: 10.2741/3714 Volume 16 Issue 2, pp.707-722
Published: 01 January 2011
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.

Share and Cite
William Hornebeck, Herve Emonard. The cell-elastin-elastase(s) interacting triade directs elastolysis. Frontiers in Bioscience-Landmark. 2011. 16(2); 707-722.