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Liberation of desmosine and isodesmosine as amino acids from insoluble elastin by elastolytic proteases.

Abstract
The development of atherosclerotic lesions and abdominal aortic aneurysms involves degradation and loss of extracellular matrix components, such as collagen and elastin. Releases of the elastin cross-links desmosine (DES) and isodesmosine (IDE) may reflect elastin degradation in cardiovascular diseases. This study investigated the production of soluble elastin cross-linking structures by proteinases implicated in arterial diseases. Recombinant MMP-12 and neutrophil elastase liberated DES and IDE as amino acids from insoluble elastin. DES and IDE were also released from insoluble elastin exposed to monocyte/macrophage cell lines or human primary macrophages derived from peripheral blood monocytes. Elastin oxidized by reactive oxygen species (ROS) liberated more unconjugated DES and IDE than did non-oxidized elastin when incubated with MMP-12 or neutrophil elastase. These results support the exploration of free DES and IDE as biomarkers of elastin degradation.
AuthorsHideyuki Umeda, Masanori Aikawa, Peter Libby
JournalBiochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 411 Issue 2 Pg. 281-6 (Jul 29 2011) ISSN: 1090-2104 [Electronic] United States
PMID21726534 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2011 Elsevier Inc. All rights reserved.
Chemical References
  • Biomarkers
  • Reactive Oxygen Species
  • Recombinant Proteins
  • Desmosine
  • Elastin
  • Isodesmosine
  • Leukocyte Elastase
  • Matrix Metalloproteinase 12
Topics
  • Animals
  • Biomarkers (metabolism)
  • Cardiovascular Diseases (metabolism)
  • Cell Line
  • Desmosine (metabolism)
  • Elastin (metabolism)
  • Humans
  • Isodesmosine (metabolism)
  • Leukocyte Elastase (chemistry, genetics, metabolism)
  • Matrix Metalloproteinase 12 (chemistry, genetics, metabolism)
  • Mice
  • Reactive Oxygen Species (metabolism)
  • Recombinant Proteins (chemistry, genetics, metabolism)

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