Autor: |
T, Levade, N, Andrieu-Abadie, B, Ségui, N, Augé, M, Chatelut, J P, Jaffrézou, R, Salvayre |
Rok vydání: |
2000 |
Předmět: |
|
Zdroj: |
Chemistry and physics of lipids. 102(1-2) |
ISSN: |
0009-3084 |
Popis: |
The ubiquitous sphingophospholipid sphingomyelin (SM) can be hydrolysed in human cells to ceramide by different sphingomyelinases (SMases). These enzymes exert a dual role, enabling not only the turnover of membrane SM and the degradation of exogenous (lipoprotein) SM, but also the signal-induced generation of the lipid second messenger ceramide. This review focuses on the function(s) of the different SMases in living cells. While both lysosomal and non-lysosomal pathways that ensure SM hydrolysis in intact cells can be distinguished, the precise contribution of each of these SM-cleaving enzymes to the production of ceramide as a signalling molecule remains to be clarified. |
Databáze: |
OpenAIRE |
Externí odkaz: |
|