Journal article
Effect of ceramide structure on membrane biophysical properties: The role of acyl chain length and unsaturation
Biochimica Et Biophysica Acta-Biomembranes, Vol.1808(11), pp.2753-2760
Nov/2011
Abstract
Ceramide is an important bioactive sphingolipid involved in a variety of biological processes. The mechanisms by which ceramide regulates biological events are not fully understood, but may involve alterations in the biophysical properties of membranes. We now examine the properties of ceramide with different acyl chains including long chain (C16- and C18-), very long chain (C24-) and unsaturated (C18:1- and C24:1-) ceramides, in phosphatidylcholine model membranes. Our results show that i) saturated ceramides have a stronger impact on the fluid membrane, increasing its order and promoting gel/fluid phase separation, while their unsaturated counterparts have a lower (C24:1-) or no (C18:1-) ability to form gel domains at 37 degrees C; ii) differences between saturated species are smaller and are mainly related to the morphology and size of the gel domains, and iii) very long chain ceramides form tubular structures likely due to their ability to form interdigitated phases. These results suggest that generation of different ceramide species in cell membranes has a distinct biophysical impact with acyl chain saturation dictating membrane lateral organization, and chain asymmetry governing interdigitation and membrane morphology. (C) 2011 Elsevier B.V. All rights reserved.
Details
- Title
- Effect of ceramide structure on membrane biophysical properties; The role of acyl chain length and unsaturation
- Creators
- Sandra N. Pinto (null)Liana C. Silva (null)Anthony H. Futerman (null) - 972WIS_INST___112Manuel Prieto (null)
- Resource Type
- Journal article
- Publication Details
- Biochimica Et Biophysica Acta-Biomembranes, Vol.1808(11), pp.2753-2760; Nov/2011
- Number of pages
- 8
- Language
- English
- DOI
- https://doi.org/10.1016/j.bbamem.2011.07.023
- Grant note
- Fundacao para a Ciencia e Tecnologia (FCT), Portugal [PTDC/QUI-BIQ/111411/2009]; Israel Science Foundation [1735/07]; FCT [SFRH/BD/46296/2008]The authors thank Alexander Fedorov for assistance with time-resolved fluorescence measurements. A.H. Futerman is The Joseph Meyerhoff Professor of Biochemistry at the Weizmann Institute of Science. This work was supported by Fundacao para a Ciencia e Tecnologia (FCT), Portugal (PTDC/QUI-BIQ/111411/2009) and Israel Science Foundation grant number 1735/07. FCT provided a research grant to S.N.P. (SFRH/BD/46296/2008)._ALMAME_DELIMITER_
- Record Identifier
- 993264513803596
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