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

摘要

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 betweenH. pyloriinfection 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 againstH. pyloriinfection, whereas HSPs as a bad offender contributing to the progression ofH. pylori-associated gastric carcinogenesis in addition to aggravation of gastric inflammation. In this paper regarding proteomic discovery of HSPs related toH. pylori-associated gastric diseases, we introduce several evidences obtained from proteomic analysis dealing with friend or foe role of HSP inH. pyloriinfection 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-βsignaling, key tumor suppressor growth factors regulating inflammation, immune function, and carcinogenesis were further introduced.