The preferential interactions of cholesterol with different classes of phospholipids

Demel, R.A.; Jansen, Joachim; Dijck, P.W.M. Van; Deenen, L.L.M. Van

doi:10.1016/0005-2736(77)90350-9

Cited by 366 publications

(111 citation statements)

References 29 publications

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“…Previous studies showed that feeding dietary SM in rat inhibited cholesterol absorption [6,7] by a mechanism related to the decreased thermodynamic activity of cholesterol in micelles by SM [8], due to close interaction between SM and cholesterol [25,26]. The present study showed that not only SM but also ceramide, the hydrolytic product of SM in the micelles, inhibited cholesterol uptake.…”

Section: Discussionsupporting

confidence: 60%

Generating Ceramide from Sphingomyelin by Alkaline Sphingomyelinase in the Gut Enhances Sphingomyelin-Induced Inhibition of Cholesterol Uptake in Caco-2 Cells

et al. 2010

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Section: Discussionsupporting

confidence: 60%

Generating Ceramide from Sphingomyelin by Alkaline Sphingomyelinase in the Gut Enhances Sphingomyelin-Induced Inhibition of Cholesterol Uptake in Caco-2 Cells

et al. 2010

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“…Separation into SM-rich and PUFA-rich phases is further demonstrated by the presence of two endotherms in DSC scans for 16:0-22:6PE/egg SM (1:1 mol), and the introduction of cholesterol first affects the higher temperature endotherm attributed to the SM-rich phase [58]. This approach, of course, is the same methodology Demel et al used to demonstrate cholesterol-SM affinity in the 1970s [22] [59] establishes the presence of motionally distinct SM-rich (more ordered) and PUFA-rich (less ordered) domains that are o20 nm in size, an acceptable size for lipid rafts. Order in the SM-rich (raft) domain is increased more than the PUFArich (non-raft) domain when cholesterol (1:1:1 mol) is added.…”

Section: Pufa's Aversion To Cholesterolmentioning

confidence: 85%

“…Particularly noteworthy were cholesterol-and sphingolipid-enriched domains studied in model bilayer membranes in the 1970s by Biltonen and Thompson [21]. An early differential scanning calorimetry (DSC) study by Demel et al [22] that established differential affinity for cholesterol was based on preferential obliteration by the sterol of melting transitions between two component monotectic lipids. This investigation showed that cholesterol association follows the sequence: sphingomyelin4 phosphatidylserine, phosphatidylglycerol4phosphatidyl-choline4phosphatidylethanolamine (SM4PS, PG4PC4 PE).…”

Section: Role Of Cholesterol In Lipid Raftsmentioning

confidence: 99%

The location and behavior of α‐tocopherol in membranes

Atkinson

Harroun

Wassall

et al. 2010

Molecular Nutrition Food Res

168

128

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Vitamin E (a-tocopherol) has long been recognized as the major antioxidant in biological membranes, and yet many structurally related questions persist of how the vitamin functions. For example, the very low levels of a-tocopherol reported for whole cell extracts question how this molecule can successfully protect the comparatively enormous quantities of PUFAcontaining phospholipids found in membranes that are highly susceptible to oxidative attack. The contemporary realization that membranes laterally segregate into regions of distinct lipid composition (domains), we propose, provides the answer. We hypothesize a-tocopherol partitions into domains that are enriched in polyunsaturated phospholipids, amplifying the concentration of the vitamin in the place where it is most needed. These highly disordered domains depleted in cholesterol are analogous, but organizationally antithetical, to the wellstudied lipid rafts. We review here the ideas that led to our hypothesis. Experimental evidence in support of the formation of PUFA-rich domains in model membranes is presented, focusing upon docosahexaenoic acid that is the most unsaturated fatty acid commonly found. Physical methodologies are then described to elucidate the nature of the interaction of a-tocopherol with PUFA and to establish that the vitamin and PUFA-containing phospholipids co-localize in non-raft domains.

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“…Although we do not know why discrete, low-cholesterol membrane regions are formed, there is a possibility that these regions might have different phospholipid compositions, because Demel et al . (15) reported that cholesterol has a preferential affinity for certain kinds of phospholipids such as sphingomyelin .…”

Section: Discussionmentioning

confidence: 99%

Absence of filipin-sterol complexes from the membranes of active zones and acetylcholine receptor aggregates at frog neuromuscular junctions.

Nakajima¹,

Bridgman²

1981

The Journal of Cell Biology

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The polyene antibiotic filipin reacts specifically with membrane cholesterol and produces distinctive membrane lesions. We treated frog cutaneous and sartorius muscles with 0.04% filipin in a glutaraldehyde solution with or without prefixation with glutaraldehyde. Freeze-fracture of these muscles revealed numerous 19 to 38-nm protuberances and depressions (filipin-sterol complexes) in most areas of muscle, axon, and Schwann cell membranes. In the presynaptic membrane, however, these filipin-sterol complexes were absent from active zones consisting of ridges bordered with double rows of particles. In the postsynaptic membrane, filipin-sterol complexes were also virtually absent from the areas occupied by aggregates of large particles representing acetylcholine receptors. These results suggest that the membrane regions of active zones and acetylcholine receptor aggregates have a low cholesterol content.

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The preferential interactions of cholesterol with different classes of phospholipids

Cited by 366 publications

References 29 publications

Generating Ceramide from Sphingomyelin by Alkaline Sphingomyelinase in the Gut Enhances Sphingomyelin-Induced Inhibition of Cholesterol Uptake in Caco-2 Cells

Generating Ceramide from Sphingomyelin by Alkaline Sphingomyelinase in the Gut Enhances Sphingomyelin-Induced Inhibition of Cholesterol Uptake in Caco-2 Cells

The location and behavior of α‐tocopherol in membranes

Absence of filipin-sterol complexes from the membranes of active zones and acetylcholine receptor aggregates at frog neuromuscular junctions.

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