Premium
Acute activation of acid ceramidase affects cytokine‐induced cytotoxicity in rat islet β‐cells
Author(s) -
Zhu Qun,
Shan Xiaohong,
Miao Heng,
Lu Yibing,
Xu Jiarong,
You Na,
Liu Chao,
Liao Duan-fang,
Jin Junfei
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.05.047
Subject(s) - sphingosine , ceramide , sphingosine kinase , sphingosine 1 phosphate , sphingosine kinase 1 , sphingolipid , lipid signaling , chemistry , cytokine , biochemistry , biology , microbiology and biotechnology , medicine , enzyme , immunology , apoptosis , receptor
Ceramidase hydrolyzes ceramide and produces sphingosine as a substrate of sphingosine kinase (SPHK), which transforms sphingosine to sphingosine‐1‐phosphate. It has been reported that cytokines elicit SPHK activation in rat β‐cells. As a sphingosine provider, ceramidase should also be activated. In our previous work, we showed that the increase in mRNA and protein levels in cytokine‐treated INS‐1 rat β‐cells resulted in chronic activation of neutral ceramidase. Here we found that acid ceramidase (AC) is activated by cytokines at an early stage via tyrosine phosphorylation. In addition, basal AC activity was first detected in INS‐1 cells and isolated rat islets, and cytokine‐induced cell growth was significantly repressed when AC was pharmacologically inhibited.