Implication of altered ubiquitin-proteasome system and ER stress in the muscle atrophy of diabetic rats

Arch Biochem Biophys. 2018 Feb 1:639:16-25. doi: 10.1016/j.abb.2017.12.015. Epub 2017 Dec 24.

Abstract

Background: Skeletal muscle is adversely affected in type-1 diabetes, and excessively stimulated ubiquitin-proteasome system (UPS) was found to be a leading cause of muscle wasting or atrophy. The role of endoplasmic reticulum (ER) stress in muscle atrophy of type-1 diabetes is not known. Hence, we investigated the role of UPS and ER stress in the muscle atrophy of chronic diabetes rat model.

Methods: Diabetes was induced with streptozotocin (STZ) in male Sprague-Dawley rats and were sacrificed 2- and 4-months thereafter to collect gastrocnemius muscle. In another experiment, 2-months post-STZ-injection diabetic rats were treated with MG132, a proteasome inhibitor, for the next 2-months and gastrocnemius muscle was collected.

Results: The muscle fiber cross-sectional area was diminished in diabetic rats. The expression of UPS components: E1, MURF1, TRIM72, UCHL1, UCHL5, ubiquitinated proteins, and proteasome activity were elevated in the diabetic rats indicating activated UPS. Altered expression of ER-associated degradation (ERAD) components and increased ER stress markers were detected in 4-months diabetic rats. Proteasome inhibition by MG132 alleviated alterations in the UPS and ER stress in diabetic rat muscle.

Conclusion: Increased UPS activity and ER stress were implicated in the muscle atrophy of diabetic rats and proteasome inhibition exhibited beneficiary outcome.

Keywords: ERAD; MG132; Muscle wasting; Proteasome inhibitor; Type 1 diabetes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Diabetes Mellitus, Experimental / drug therapy
  • Diabetes Mellitus, Experimental / metabolism*
  • Diabetes Mellitus, Experimental / pathology
  • Endoplasmic Reticulum Stress*
  • Leupeptins / pharmacology
  • Male
  • Muscle Proteins / metabolism
  • Muscle, Skeletal / metabolism*
  • Muscle, Skeletal / pathology
  • Muscular Atrophy / chemically induced
  • Muscular Atrophy / drug therapy
  • Muscular Atrophy / metabolism*
  • Muscular Atrophy / pathology
  • Proteasome Endopeptidase Complex / metabolism*
  • Proteasome Inhibitors / pharmacology
  • Rats
  • Rats, Sprague-Dawley
  • Tripartite Motif Proteins / metabolism
  • Ubiquitin / metabolism*
  • Ubiquitin Thiolesterase / metabolism
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitinated Proteins / metabolism
  • Vesicular Transport Proteins / metabolism

Substances

  • Leupeptins
  • Muscle Proteins
  • Proteasome Inhibitors
  • TRIM72 protein, rat
  • Tripartite Motif Proteins
  • Ubiquitin
  • Ubiquitinated Proteins
  • Vesicular Transport Proteins
  • Trim63 protein, rat
  • Ubiquitin-Protein Ligases
  • UCHL1 protein, rat
  • Ubiquitin Thiolesterase
  • Proteasome Endopeptidase Complex
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde