Identification of neutral and acidic sphingomyelinases in Helicobacter pylori

FEBS Letters

Lin, Yuh-Ling¹  Liu, Jai-Shin¹  Chen, Kuei-Tian¹  Chan, Err-Cheng¹  Chen, Chien-Tsu² 

[1] School of Medical Technology, Chang Gung University, 259 Wen-Hua 1st Road, Taoyuan, Taiwan;Department of Biochemistry, Taipei Medical College, Taipei, Taiwan

关键词: Sphingomyelinase;    Phospholipase;    Bacillus cereus;    Helicobacter pylori;    N-ω-Trinitrophenylaminolauryl-sphingomyelin;   

DOI  :  10.1016/S0014-5793(98)00087-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown