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International Journal of Proteomics
Volume 2010 (2010), Article ID 259163, 11 pages
http://dx.doi.org/10.1155/2010/259163
Review Article

Heat Shock Protein: Hard Worker or Bad Offender for Gastric Diseases

1Laboratory of Chemoprevention, Lee Gil Ya Cancer and Diabetes Institute, Gachon University of Medicine and Science, Incheon, Republic of Korea
2Laboratory of Translational Medicine, Lee Gil Ya Cancer and Diabetes Institute, Gachon University of Medicine and Science, Incheon, Republic of Korea
3Laboratory of Cell Regulation and Carcinogenesis, Lee Gil Ya Cancer and Diabetes Institute, Gachon University of Medicine and Science, Incheon, Republic of Korea
4Department of Gastroenterology, Gachon Graduate School of Medicine Gil Medical Center, Songdo-dong 7-45, Yeonsu-gu, Incheon, 406-840, Republic of Korea

Received 28 June 2010; Accepted 5 September 2010

Academic Editor: Ho Jeong Kwon

Copyright © 2010 Ho-Jae Lee et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Heat shock proteins (HSPs) have core housekeeping functions in the cells where they are built-in components of folding, signal transduction pathways, and quality control functions for which they proofread the structure of proteins and repair misfolded conformers. Helicobacter pylori (H. pylori) infection leads to significant inflammations in the gastric mucosa, which is closely associated with development of either precancerous lesion including chronic atrophic gastritis or gastric cancer in addition to, peptic ulcer disease, and mucosa-associated lymphoid tissue (MALT) lymphoma. Therefore, the association between H. pylori infection and role of HSP has been focused as an important issue because there had been rather conflicting publications showing that HSPs as a good worker for defense against H. pylori infection, whereas HSPs as a bad offender contributing to the progression of H. pylori-associated gastric carcinogenesis in addition to aggravation of gastric inflammation. In this paper regarding proteomic discovery of HSPs related to H. pylori-associated gastric diseases, we introduce several evidences obtained from proteomic analysis dealing with friend or foe role of HSP in H. pylori infection from a cellular level to human diseases. The implication of HSPs in alcoholic or NSAIDs-induced gastritis and the intervening of HSPs in biological changes exemplified with TGF- 𝛽 signaling, key tumor suppressor growth factors regulating inflammation, immune function, and carcinogenesis were further introduced.