Degradation of relaxin family peptides by insulin-degrading enzyme

Research output: Chapter in Book/Report/Conference proceedingConference contribution

10 Scopus citations

Abstract

Insulin-degrading enzyme (IDE) is a ubiquitously expressed metalloproteinase responsible for the intracellular degradation of insulin. IDE also interacts with other members of the insulin superfamily, including relaxin, but no studies have been reported regarding the interaction of other relaxin-like peptides with IDE. In this study, we determined that relaxin, relaxin-3, and InsL3 all competitively inhibited the degradation of insulin by IDE to different degrees, and all inhibited covalent cross-linking of insulin to IDE. Each of the peptides was degraded by IDE to various degrees (insulin > relaxin > InsL3 = relaxin-3). In summary, relaxin, InsL3, and relaxin-3 all bound to IDE, competed for the binding and degradation of insulin, and were all substrates for the proteolytic activity of IDE. Therefore, it is possible that in addition to insulin, IDE may be important for the cellular proteolysis of relaxin, InsL3, and relaxin-3.

Original languageEnglish (US)
Title of host publicationRelaxin and Related Peptides Fifth International Conference
PublisherBlackwell Publishing Inc.
Pages38-41
Number of pages4
ISBN (Print)9781573317214
DOIs
Publication statusPublished - Apr 2009

Publication series

NameAnnals of the New York Academy of Sciences
Volume1160
ISSN (Print)0077-8923
ISSN (Electronic)1749-6632

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Keywords

  • InsL3
  • Insulin-degrading enzyme
  • Insulysin
  • Relaxin
  • Relaxin-3
  • Relaxin-like factor

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • History and Philosophy of Science

Cite this

Bennett, R. G., Heimann, D. G., & Hamel, F. G. (2009). Degradation of relaxin family peptides by insulin-degrading enzyme. In Relaxin and Related Peptides Fifth International Conference (pp. 38-41). (Annals of the New York Academy of Sciences; Vol. 1160). Blackwell Publishing Inc.. https://doi.org/10.1111/j.1749-6632.2008.03782.x