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Literature DB >> 21726534

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

Hideyuki Umeda¹, Masanori Aikawa, Peter Libby.

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.

Entities: CellLine Chemical Disease Gene Species

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Year: 2011 PMID： 21726534 PMCID： PMC3148299 DOI： 10.1016/j.bbrc.2011.06.124

Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575

30 in total

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12 in total

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