Roles of heat-shock protein 70 in protecting against intestinal mucosal damage

Front Biosci (Landmark Ed). 2013 Jan 1;18(1):356-65. doi: 10.2741/4106.

Abstract

Heat shock proteins (HSPs) are remarkably conserved in all living organisms. The upregulation of expression of HSPs is triggered by a variety of physiological and environmental insults. HSPs play an important role in protecting against protein denaturation and subsequent celluar stress, which damages the intestinal mucosa and reduces the protective function of the mucosal barrier, resulting in the formation of stress ulcers. Heat shock protein 70 (HSP70) is the most widely studied of all HSPs and has numerous important chaperoning functions. Stress accelerates the synthesis of HSP70, which in turn inhibits the apoptosis of intestinal mucosal cells. In this article, we review the main classification of HSPs, the expression and regulation of HSPs and their roles in stress ulcers. We also discuss the role of functional amino acids in regulating the expression of HSPs (particularly HSP70) and protecting the intestinal mucosa and other tissues.

Publication types

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

MeSH terms

  • Animals
  • Apoptosis / drug effects
  • Arginine / metabolism
  • Arginine / pharmacology
  • Glutamine / metabolism
  • Glutamine / pharmacology
  • HSP70 Heat-Shock Proteins / biosynthesis
  • HSP70 Heat-Shock Proteins / physiology*
  • Intestinal Mucosa / drug effects*
  • Intestinal Mucosa / physiology
  • Peptic Ulcer / genetics
  • Stress, Physiological / physiology

Substances

  • HSP70 Heat-Shock Proteins
  • Glutamine
  • Arginine