Sphingomyelin-degrading pathways in human cells

Autor: Robert Salvayre, Thierry Levade, Nathalie Andrieu-Abadie, Nathalie Augé, Jean-Pierre Jaffrézou, Bruno Ségui, Martine Chatelut
Rok vydání: 1999
Předmět:
Zdroj: Chemistry and Physics of Lipids. 102:167-178
ISSN: 0009-3084
DOI: 10.1016/s0009-3084(99)00085-7
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