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C 2 -ceramide ( N -acetyl-sphingenine) is often used as an analog to study ceramide-mediated cellular processes. According to Lee et al. [J. Biol. Chem.  271  (1996), 209–217], C 2 -ceramide is formed by an acetyl transfer from platelet-activating factor (PAF, 1- O -alkyl-2-acetyl- sn -glycero-3-phosphocholine) to sphingenine. To substantiate these unconfirmed findings, we (i) developed a method to quantify C 2 -ceramide and (ii) analyzed C 2 -ceramide levels in  Pex5   -/-   mice, a model for Zellweger syndrome, in which the synthesis of ether lipids such as PAF is impaired. The presence of C 2 -ceramide could be established in brain (±10 pmol/g) and liver (±25 pmol/g) from control mice, and was approximately 5000-fold less than the main long-chain ceramide species. In  Pex5   -/-   mice, C 2 -ceramide levels did not differ significantly compared to control tissues. Given the presence of a ceramide kinase in mammals, phosphorylation of C 2 -ceramide by human ceramide kinase ( Hs CERK) was tested. C 2 -ceramide appears to be a good substrate when albumin is used as carrier. In CHO cells overexpressing  Hs CERK, phosphorylation of exogenously added C 2 -ceramide could also be demonstrated. Our data indicate that C 2 -ceramide is present in mammalian tissues and can be converted to C 2 -ceramide-1-phosphate, in addition to other documented metabolic alterations, but does not seem to be linked to ether lipid metabolism.

On the presence of C 2 -ceramide in mammalian tissues: possible relationship to etherphospholipids and phosphorylation by ceramide kinase