Preferential inhibition of phorbol ester‐induced hydrolysis of phosphatidylethanolamine by N‐acetylsphingosine in NIH 3T3 fibroblasts

FEBS Letters

Deli, Eva¹  Kiss, Zoltan¹ 

[1] Hormel Institute, University of Minnesota, 801 16th Avenue NE, Austin, MN 55912, USA

关键词: N-Acetylsphingosine;    Phospholipase D;    Phosphatidylethanolamine;    Phosphatidylcholine;    NIH 3T3 fibroblast;    PLD;    phospholipase D;    PtdCho;    phosphatidylcholine;    PtdEtn;    phosphatidylethanolamine;    PMA;    phorbol 12-myristate 13-acetate;    C2-ceramide;    N-acetylsphingosine;    PtdEtOH;    phosphatidylethanol;    SMase;    sphingomyelinase;   

DOI  :  10.1016/0014-5793(95)00445-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It has been reported that in rat fibroblasts cell-permeable ceramide analogs inhibit agonist-induced phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho). Here we demonstrate that relatively short (30 min) treatments of NIH 3T3 fibroblasts with 15–60 μM concentrations of N-acetylsphingosine result in preferential, although not exclusive, inhibition of phorbol 12-myristate 13-acetate-induced PLD-mediated hydrolysis of phosphatidylethanolamine (PtdEtn). The results suggest that in different cell types the PtdEtn- and PtdCho-hydrolyzing PLD activities are differentially sensitive to the inhibitory effect of ceramide.

【 授权许可】

Unknown