Characterizing the polymeric status of Helicobacter pylori heat shock protein 60

Ching Yi Lin, Yu Shan Huang, Chi Han Li, Yuan Ting Hsieh, Nu Man Tsai, Pei Juin He, Wei Tung Hsu, Yi Chen Yeh, Fang Hsing Chiang, Ming Shiang Wu, Chia-Ching Chang, Kuang-Wen Liao*


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20 引文 斯高帕斯(Scopus)


Helicobacter pylori heat shock protein 60 (HpHsp60) was first identified as an adhesion molecule associated with H. pylori infection. Here we have analyzed the structure of HpHsp60 via amino acid BLAST, circular dichroism, and electrophoresis and the results indicate that most recombinant HpHsp60 molecules exist as dimers or tetramers, which is quite different from Escherichia coli Hsp60. Treatment of human monocytic cells THP-1 with HpHsp60 was found to up-regulate a panel of cytokines including IL-1α, IL-8, IL-10, IFN-γ, TNF-α, TGF-β, GRO, and RANTES. Carboxymethylated HpHsp60 molecules with a switched oligomeric status were able to further enhance NF-κB-mediated IL-8 and TNF-α secretion in THP-1 cells compared to unmodified HpHsp60 molecules. These results indicated that the oligomeric status of HpHsp60s might have an important role in regulating host inflammation and thus help facilitate H. pylori persistent infection.

頁(從 - 到)283-289
期刊Biochemical and Biophysical Research Communications
出版狀態Published - 16 10月 2009


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