Document Detail

Roles of heat-shock protein 70 in protecting against intestinal mucosal damage.
MedLine Citation:
PMID:  23276928     Owner:  NLM     Status:  MEDLINE    
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.
Xin Wu; Yuzhe Zhang; Yulong Yin; Zheng Ruan; Humin Yu; Zhenlong Wu; Guoyao Wu
Related Documents :
6526128 - Modification of membrane protein organization during in vitro aging of human erythrocytes.
1493178 - Purification and characterization of a human follicular fluid lipid transfer protein th...
9639148 - Binding of seminal vesicle proteins to the plasma membrane of rat spermatozoa in vivo a...
22585498 - Two-dimensional blue native/sds gel electrophoresis of multiprotein complexes.
10461858 - The effect of tryptophan plus methionine, 5-azacytidine, and methotrexate on adjuvant a...
3391168 - A photo-chemically induced dynamic nuclear polarization nmr study on rabbit and bovine ...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2013-01-01
Journal Detail:
Title:  Frontiers in bioscience (Landmark edition)     Volume:  18     ISSN:  1093-4715     ISO Abbreviation:  Front Biosci (Landmark Ed)     Publication Date:  2013  
Date Detail:
Created Date:  2013-01-01     Completed Date:  2013-06-12     Revised Date:  2013-07-29    
Medline Journal Info:
Nlm Unique ID:  101612996     Medline TA:  Front Biosci (Landmark Ed)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  356-65     Citation Subset:  IM    
Hunan Engineering and Research Center of Animal and Poultry Science and Key Laboratory for Agro-ecological Processes in Subtropical Region, Institute of Subtropical Agriculture, Chinese Academy of Sciences, Hunan, China.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Apoptosis / drug effects
Arginine / metabolism,  pharmacology
Glutamine / metabolism,  pharmacology
HSP70 Heat-Shock Proteins / biosynthesis,  physiology*
Intestinal Mucosa / drug effects*,  physiology
Peptic Ulcer / genetics
Stress, Physiological / physiology
Reg. No./Substance:
0/HSP70 Heat-Shock Proteins; 56-85-9/Glutamine; 74-79-3/Arginine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Towards elucidating the role of SirT1 in osteoarthritis.
Next Document:  Prevalence and risk factor for MDR-GNB infection in liver transplantation.