The role of αB-crystallin in skeletal and cardiac muscle tissues

Cell Stress Chaperones. 2018 Jul;23(4):491-505. doi: 10.1007/s12192-017-0866-x. Epub 2017 Nov 30.

Abstract

All organisms and cells respond to various stress conditions such as environmental, metabolic, or pathophysiological stress by generally upregulating, among others, the expression and/or activation of a group of proteins called heat shock proteins (HSPs). Among the HSPs, special attention has been devoted to the mutations affecting the function of the αB-crystallin (HSPB5), a small heat shock protein (sHsp) playing a critical role in the modulation of several cellular processes related to survival and stress recovery, such as protein degradation, cytoskeletal stabilization, and apoptosis. Because of the emerging role in general health and disease conditions, the main objective of this mini-review is to provide a brief account on the role of HSPB5 in mammalian muscle physiopathology. Here, we report the current known state of the regulation and localization of HSPB5 in skeletal and cardiac tissue, making also a critical summary of all human HSPB5 mutations known to be strictly associated to specific skeletal and cardiac diseases, such as desmin-related myopathies (DRM), dilated (DCM) and restrictive (RCM) cardiomyopathy. Finally, pointing to putative strategies for HSPB5-based therapy to prevent or counteract these forms of human muscular disorders.

Keywords: Chaperones; Crystallinopathies; Disease; Heat shock proteins; Physical activity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Autophagy
  • Humans
  • Muscle, Skeletal / metabolism*
  • Myocardium / metabolism*
  • Oxidation-Reduction
  • Proteasome Endopeptidase Complex / metabolism
  • alpha-Crystallin B Chain / chemistry
  • alpha-Crystallin B Chain / metabolism*

Substances

  • alpha-Crystallin B Chain
  • Proteasome Endopeptidase Complex