Small heat shock protein alphaB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis

Biochem Biophys Res Commun. 2007 Mar 2;354(1):109-14. doi: 10.1016/j.bbrc.2006.12.152. Epub 2006 Dec 28.

Abstract

Apoptosis is a highly conserved procedure of cell death and occurs under various stimuli, including oxidative stress. A small heat shock protein, alphaB-crystallin, is found to process resistance to apoptosis in some cells and tissues. But the mechanisms under this protective role are not fully understood. In the present study, we reported the early protective role of alphaB-crystallin against hydrogen peroxide-induced apoptosis in mice myogenic C(2)C(12) cells. alphaB-Crystallin interacted with p53, a proapoptotic protein, during cell apoptosis and such protein interaction mainly occurred in the cytoplasm of the cells, suggesting that the interaction of alphaB-crystallin with p53 might prevent the translocation of p53 from cytoplasm to mitochondria. Hence, this study provides a hint that alphaB-crystallin affects on p53 mitochondrial translocation during oxidative stress-induced apoptosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis / drug effects*
  • Cell Line
  • Dose-Response Relationship, Drug
  • Heat-Shock Proteins, Small / metabolism*
  • Hydrogen Peroxide / administration & dosage*
  • Mice
  • Mitochondria / drug effects
  • Mitochondria / metabolism*
  • Myoblasts / drug effects
  • Myoblasts / metabolism*
  • Myoblasts / ultrastructure
  • Oxidative Stress / drug effects
  • Oxidative Stress / physiology
  • Protein Binding
  • Protein Transport / drug effects
  • Protein Transport / physiology
  • Tumor Suppressor Protein p53 / metabolism*
  • alpha-Crystallin B Chain / metabolism*

Substances

  • Heat-Shock Proteins, Small
  • Tumor Suppressor Protein p53
  • alpha-Crystallin B Chain
  • Hydrogen Peroxide