標題: Characterizing the polymeric status of Helicobacter pylori heat shock protein 60
作者: Lin, Ching-Yi
Huang, Yu-Shan
Li, Chi-Han
Hsieh, Yuan-Ting
Tsai, Nu-Man
He, Pei-Juin
Hsu, Wei-Tung
Yeh, Yi-Chen
Chiang, Fang-Hsing
Wu, Ming-Shiang
Chang, Chia-Ching
Liao, Kuang-Wen
生物科技學系
Department of Biological Science and Technology
關鍵字: Helicobacter pylori;Heat shock protein 60;Inflammation
公開日期: 16-Oct-2009
摘要: 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-1 alpha, IL-8, IL-10, IFN-gamma, TNF-alpha, TGF-beta, GRO, and RANTES. Carboxymethylated HpHsp60 molecules with a switched oligomeric status were able to further enhance NF-kappa B-mediated IL-8 and TNF-alpha 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. (C) 2009 Elsevier Inc. All rights reserved.
URI: http://dx.doi.org/10.1016/j.bbrc.2009.07.159
http://hdl.handle.net/11536/6561
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2009.07.159
期刊: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume: 388
Issue: 2
起始頁: 283
結束頁: 289
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