Abstract
The effects of a series of ceramide analogs with acyl chain lengths of 2, 6, 8 and 16 on the structure of dipalmitoylphosphatidylcholine (DPPC) bilayers and cobra venom phospholipase A2 (PL-A2) activity were studied using 2H-NMR and specific enzymatic assays. C2-ceramide did not induce a significant effect on the structure of DPPC bilayers and did not alter PL-A2 activity. C6- and C8-ceramides increased the ordering of the DPPC acyl chains, correlating with the inhibition of PL-A2 activity which was probably due to the increased lateral surface pressure. The long-chain C16-ceramide induced lateral phase separation of the bilayers into gel and liquid crystalline domains and activated PL-A2, as does natural ceramide (Huang et al. 1996). Taken together, the results strongly suggest a correlation between membrane defects induced by ceramide analogs and their effects on phospholipase A2 activity. Furthermore, the effects of short-chain ceramides on PL-A2 are different from those of natural ceramide, indicating that the cell-permeable short-chain ceramide analogs, widely used to study the sphingomyelin-dependent cellular signal transduction pathway, may not completely mimic the natural product.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
Author information
Authors and Affiliations
Additional information
Received: 8 July 1997 / Accepted: 19 January 1998
Rights and permissions
About this article
Cite this article
Huang, Hw., Goldberg, E. & Zidovetzki, R. Ceramides perturb the structure of phosphatidylcholine bilayers and modulate the activity of phospholipase A2 . Eur Biophys J 27, 361–366 (1998). https://doi.org/10.1007/s002490050143
Issue Date:
DOI: https://doi.org/10.1007/s002490050143