Regulation of the calpain and ubiquitin-proteasome systems in a canine model of muscular dystrophy

Kristine M. Wadosky, Luge Li, Jessica E. RodríGuez, Jin Na Min, Dan Bogan, Jason Gonzalez, Cam Patterson, Joe N. Kornegay, Monte Willis

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Introduction: Previous studies have tested the hypothesis that calpain and/or proteasome inhibition is beneficial in Duchenne muscular dystrophy, based largely on evidence that calpain and proteasome activities are enhanced in the mdx mouse. Methods: mRNA expression of ubiquitin-proteasome and calpain system components were determined using real-time polymerase chain reaction in skeletal muscle and heart in the golden retriever muscular dystrophy model. Similarly, calpain 1 and 2 and proteasome activities were determined using fluorometric activity assays. Results: We found that less than half of the muscles tested had increases in proteasome activity, and only half had increased calpain activity. In addition, transcriptional regulation of the ubiquitin-proteasome system was most pronounced in the heart, where numerous components were significantly decreased. Conclusion: This study illustrates the diversity of expression and activities of the ubiquitin-proteasome and calpain systems, which may lead to unexpected consequences in response to pharmacological inhibition.

Original languageEnglish (US)
Pages (from-to)553-562
Number of pages10
JournalMuscle and Nerve
Volume44
Issue number4
DOIs
StatePublished - Oct 1 2011

Keywords

  • Calpain
  • Heart
  • Muscular dystrophy
  • Proteasome
  • Skeletal muscle

ASJC Scopus subject areas

  • Physiology
  • Clinical Neurology
  • Cellular and Molecular Neuroscience
  • Physiology (medical)

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    Wadosky, K. M., Li, L., RodríGuez, J. E., Min, J. N., Bogan, D., Gonzalez, J., Patterson, C., Kornegay, J. N., & Willis, M. (2011). Regulation of the calpain and ubiquitin-proteasome systems in a canine model of muscular dystrophy. Muscle and Nerve, 44(4), 553-562. https://doi.org/10.1002/mus.22125