Identification of neutral and acidic sphingomyelinases in Helicobacter pylori

Yuh Ling Lin, Jai Shin Liu, Kuei Tian Chen, Chien Tsu Chen, Err Cheng Chan

研究成果: 雜誌貢獻文章同行評審

15 引文 斯高帕斯(Scopus)

摘要

We demonstrated for the first time the presence of sphingomyelinase (SMase) in Helicobacter pylori. Activation of SMase has been implicated as the cause of elevation of cellular ceramide levels and consequently of apoptosis. The data indicate that there are two classes of SMase, defined by their optimal pHs and cellular locations, existing in H. pylori. One is an Mg2+-dependent membrane-bound enzyme with an optimal activity at pH 7, and the other is an Mg2+-independent cytosolic enzyme with an optimal activity at pH 5. Bisalumin, a bismuth salt, was found to inhibit the activities of both forms of SMase regardless of the presence of Mg2+. By Western blot analysis, the membrane-bound SMases of H. pylori and Bacillus cereus were shown to be antigenically related and to have a similar denatured molecular mass of 28 kDa.

原文英語
頁(從 - 到)249-253
頁數5
期刊FEBS Letters
423
發行號2
DOIs
出版狀態已發佈 - 二月 20 1998

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 分子生物學
  • 遺傳學
  • 細胞生物學

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