期刊
WORLD JOURNAL OF GASTROENTEROLOGY
卷 17, 期 28, 页码 3300-3309出版社
BAISHIDENG PUBLISHING GROUP INC
DOI: 10.3748/wjg.v17.i28.3300
关键词
Arginase; Helicobacter pylori; S-(2-boronoethyl)-L-cysteine; Urease; Mice
资金
- Public Health Service, National Institutes of Health [R01-CA101931]
AIM: To investigate the role of host and bacterial arginases in the colonization of mice by Helicobacter pylori (H. pylon). METHODS: H. pylon produces a very powerful urease that hydrolyzes urea to carbon dioxide and ammonium, which neutralizes acid. Urease is absolutely essential to H. pylori pathogenesis; therefore, the urea substrate must be in ample supply for urease to work efficiently. The urea substrate is most likely provided by arginase activity, which hydrolyzes L-arginine to L-ornithine and urea. Previous work has demonstrated that H. pylon arginase is surprisingly not required for colonization of wild-type mice. Hence, another in vivo source of the critical urea substrate must exist. We hypothesized that the urea source was provided by host arginase since this enzyme is expressed in the stomach, and H. pylon has previously been shown to induce the expression of murine gastric arginase II. To test this hypothesis, wild-type and arginase (rocF) mutant H. pylori strain SS1 were inoculated into arginase H knockout mice. RESULTS: Surprisingly, both the wild-type and rocF mutant bacteria still colonized arginase H knockout mice. Moreover, feeding arginase II knockout mice the host arginase inhibitor S-(2-boronoethyl)-L-cysteine (BEC), while inhibiting > 50% of the host arginase I activity in several tissues, did not block the ability of the rocF mutant H. pylori to colonize. In contrast, BEC poorly inhibited H. pylori arginase activity. CONCLUSION: The in vivo source for the essential urea utilized by H. pylori urease is neither bacterial arginase nor host arginase II; instead, either residual host arginase I or agmatinase is probably responsible. (C) 2011 Baishideng. All rights reserved.
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