Identification of neutral and acidic sphingomyelinases in Helicobacter pylori

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

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

15 Scopus citations


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.

Original languageEnglish
Pages (from-to)249-253
Number of pages5
JournalFEBS Letters
Issue number2
StatePublished - 20 02 1998


  • Bacillus cereus
  • Helicobacter pylori
  • N-ω-Trinitrophenylaminolauryl- sphingomyelin
  • Phospholipase
  • Sphingomyelinase


Dive into the research topics of 'Identification of neutral and acidic sphingomyelinases in Helicobacter pylori'. Together they form a unique fingerprint.

Cite this