Journal article
A combined fluorescence spectroscopy, confocal and 2-photon microscopy approach to re-evaluate the properties of sphingolipid domains
Biochimica Et Biophysica Acta-Biomembranes, Vol.1828(9), pp.2099-2110
Sep/2013
Abstract
The aim of this study is to provide further insight about the interplay between important signaling lipids and to characterize the properties of the lipid domains formed by those lipids in membranes containing distinct composition. To this end, we have used a combination of fluorescence spectroscopy, confocal and two-photon microscopy and a stepwise approach to re-evaluate the biophysical properties of sphingolipid domains, particularly lipid rafts and ceramide (Cer)-platforms. By using this strategy we were able to show that, in binary mixtures, sphingolipids (Cer and sphingomyelin, SM) form more tightly packed gel domains than those formed by phospholipids with similar acyl chain length. In more complex lipid mixtures, the interaction between the different lipids is intricate and is strongly dictated by the Cer-to-Chol ratio. The results show that in quaternary phospholipid/SM/Chol/Cer mixtures, Cer forms gel domains that become less packed as Chol is increased. Moreover, the extent of gel phase formation is strongly reduced in these mixtures, even though Cer molar fraction is increased. These results suggest that in biological membranes, lipid domains such as rafts and ceramide platforms, might display distinctive biophysical properties depending on the local lipid composition at the site of the membrane where they are formed, further highlighting the potential role of membrane biophysical properties as an underlying mechanism for mediating specific biological processes. (C) 2013 Elsevier B.V. All rights reserved.
Details
- Title
- A combined fluorescence spectroscopy, confocal and 2-photon microscopy approach to re-evaluate the properties of sphingolipid domains
- Creators
- Sandra N. Pinto (null)Fabio Fernandes (null)Alexander Fedorov (null)Anthony H. Futerman (null) - 972WIS_INST___112Liana C. Silva (null)Manuel Prieto (null)
- Resource Type
- Journal article
- Publication Details
- Biochimica Et Biophysica Acta-Biomembranes, Vol.1828(9), pp.2099-2110; Sep/2013
- Number of pages
- 12
- Language
- English
- DOI
- https://doi.org/10.1016/j.bbamem.2013.05.011
- Grant note
- Fundacao para a Ciencia e Tecnologia (FCT), Portugal [PTDC/QUI-BIQ/111411/2009]; Compromisso para a Ciencia from FCT; [SFRH/BD/46296/2008]; [SFRH/BPD/64320/2009]This work was supported by PTDC/QUI-BIQ/111411/2009 from Fundacao para a Ciencia e Tecnologia (FCT), Portugal. FCT provided a research grant to S.N. Pinto (SFRH/BD/46296/2008) and F. Fernandes (SFRH/BPD/64320/2009). Alexander Fedorov and L.C. Silva acknowledge funding from Compromisso para a Ciencia 2007 and 2008 from FCT. A. H. Futerman is The Joseph Meyerhoff Professor of Biochemistry at the Weizmann Institute of Science._ALMAME_DELIMITER_
- Record Identifier
- 993263173903596
Metrics
6 Record Views