Histidine-rich protein Hpn from Helicobacter pylori forms amyloid-like fibrils in vitro and inhibits the proliferation of gastric epithelial AGS cells |
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Authors: | Ruiguang Ge Xuesong SunDongxian Wang Qinglu ZhouHongzhe Sun |
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Institution: | a The laboratory of Integrative Biosciences, College of Life Sciences, Sun Yat-Sen University, Guangzhou 510275, Chinab Institute of Life and Health Engineering and National Engineering Research Center for Genetic Medicine, Jinan University, Guangzhou 510632, Chinac Department of Chemistry and Open Laboratory of Chemical Biology, The University of Hong Kong, Pokfulam Road, Hong Kong, China |
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Abstract: | Helicobacter pylori causes various gastric diseases, such as gastritis, peptic ulcerations, gastric cancer and mucosa-associated lymphoid tissue lymphoma. Hpn is a histidine-rich protein abundant in this bacterium and forms oligomers in physiologically relevant conditions. In this present study, Hpn oligomers were found to develop amyloid-like fibrils as confirmed by negative stain transition electron microscopy, thioflavin T and Congo red binding assays. The amyloid-like fibrils of Hpn inhibit the proliferation of gastric epithelial AGS cells through cell cycle arrest in the G2/M phase, which may be closely related to the disruption of mitochondrial bioenergetics as reflected by the significant depletion of intracellular ATP levels and the mitochondrial membrane potential. The collective data presented here shed some light on the pathologic mechanisms of H. pylori infections. |
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Keywords: | Aβ β-amyloid AD Alzheimer's disease ΔΨm mitochondrial transmembrane potential FBS fetal bovine serum H pylori Helicobacter pylori HRC histidine-rich Ca2+ binding protein IAPP islet amyloid polypeptide JC-1 5 5&prime 6 6&prime -tetrachloro-1 1&prime 3 3&prime -tetraethylbenzimidazolylcarbocyanine iodide LUV large unilamellar vesicle MALT mucosa-associated lymphoid tissue PBS phosphate-buffered saline PI propidium iodide polyQ poly(glutamine) PrP prion protein ThT thioflavin T TOM translocase of the outer membrane |
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