Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.
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.