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Biophys J, March 2001, p. 1417-1428, Vol. 80, No. 3
*Department of Cell Biology and Anatomy, Department
of Chemistry, and ¶Lineberger Comprehensive Cancer Center,
University of North Carolina at Chapel Hill, Chapel Hill, North
Carolina 27599, Laboratory for Fluorescence Dynamics,
Department of Physics, University of Illinois at Urbana-Champaign,
Urbana, Illinois 61801, and §Department of Medicine,
University of Texas Southwestern Medical Center at Dallas and Veterans
Administration Medical Center, Dallas, Texas 75216 USA
One key tenet of the raft hypothesis is that the
formation of glycosphingolipid- and cholesterol-rich lipid domains can
be driven solely by characteristic lipid-lipid interactions, suggesting that rafts ought to form in model membranes composed of appropriate lipids. In fact, domains with raft-like properties were found to
coexist with fluid lipid regions in both planar supported lipid layers
and in giant unilamellar vesicles (GUVs) formed from 1) equimolar
mixtures of phospholipid-cholesterol-sphingomyelin or 2) natural lipids
extracted from brush border membranes that are rich in sphingomyelin
and cholesterol. Employing headgroup-labeled fluorescent phospholipid
analogs in planar supported lipid layers, domains typically several
microns in diameter were observed by fluorescence microscopy at room
temperature (24°C) whereas non-raft mixtures (PC-cholesterol)
appeared homogeneous. Both raft and non-raft domains were fluid-like,
although diffusion was slower in raft domains, and the probe could
exchange between the two phases. Consistent with the raft hypothesis,
GM1, a glycosphingolipid (GSL), was highly enriched in the more ordered
domains and resistant to detergent extraction, which disrupted the
GSL-depleted phase. To exclude the possibility that the domain
structure was an artifact caused by the lipid layer support, GUVs were
formed from the synthetic and natural lipid mixtures, in which the
probe, LAURDAN, was incorporated. The emission spectrum of LAURDAN was
examined by two-photon fluorescence microscopy, which allowed
identification of regions with high or low order of lipid acyl chain
alignment. In GUVs formed from the raft lipid mixture or from brush
border membrane lipids an array of more ordered and less ordered
domains that were in register in both monolayers could reversibly be
formed and disrupted upon cooling and heating. Overall, the notion that
in biomembranes selected lipids could laterally aggregate to form more
ordered, detergent-resistant lipid rafts into which glycosphingolipids partition is strongly supported by this study.
Biophys J, March 2001, p. 1417-1428, Vol. 80, No. 3
© 2001 by the Biophysical Society 0006-3495/01/03/1417/12 $2.00
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