Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1808, Issue 11, Pages 2753-2760Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.07.023
Keywords
Ceramide gel domains; Ceramide synthases; Ceramide tubules; Interdigitation; Lipid domain morphology
Categories
Funding
- Fundacao para a Ciencia e Tecnologia (FCT), Portugal [PTDC/QUI-BIQ/111411/2009]
- Israel Science Foundation [1735/07]
- FCT [SFRH/BD/46296/2008]
- Fundação para a Ciência e a Tecnologia [PTDC/QUI-BIQ/111411/2009, SFRH/BD/46296/2008] Funding Source: FCT
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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.
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