Degradation of tropoelastin and elastin substrates by human neutrophil elastase, free and bound to alpha2-macroglobulin in serum of the M and Z (Pi) phenotypes for alpha1-antitrypsin

Am Rev Respir Dis. 1979 Mar;119(3):435-41. doi: 10.1164/arrd.1979.119.3.435.


Human neutrophil elastase degraded tropoelastin approximately 9 times faster than it did solubilized elastin and approximately 19 times faster than it did lung elastin. When bound to alpha2-M, the enzyme retained approximately 6 per cent of its activity toward tropoelastin and solubilized latter observations suggest that alpha2-M--bound elastase, cleared slowly from lung extracellular tissue space, may participate normally in the turnover of soluble precursor (s) of elastin and may contribute to the development of emphysema in alpha1-antitrypsin deficiency.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Dogs
  • Elastin* / analogs & derivatives
  • Humans
  • Immunoelectrophoresis, Two-Dimensional
  • Kinetics
  • Pancreatic Elastase / blood*
  • Pulmonary Emphysema / blood
  • Pulmonary Emphysema / enzymology*
  • Rabbits
  • Substrate Specificity
  • Swine
  • Tropoelastin*
  • alpha 1-Antitrypsin Deficiency*
  • alpha-Macroglobulins*


  • Tropoelastin
  • alpha-Macroglobulins
  • Elastin
  • Pancreatic Elastase