Effect of the structure of lipids favoring disordered domain formation on the stability of cholesterol-containing ordered domains (lipid rafts): identification of multiple raft-stabilization mechanisms.

Effect of the structure of lipids favoring disordered domain formation on the stability of cholesterol-containing ordered domains (lipid rafts): identification of multiple raft-stabilization mechanisms. Research Abstract Details 

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Effect of the structure of lipids favoring disordered domain formation on the stability of cholesterol-containing ordered domains (lipid rafts): identification of multiple raft-stabilization mechanisms. Abstract Text:

Omar Bakht,Priyadarshini Pathak,Erwin London,Omar Bakht,Priyadarshini Pathak,Erwin London,Omar Bakht,Priyadarshini Pathak,Erwin London,Omar Bakht,Priyadarshini Pathak,Erwin London,

Despite the importance of lipid rafts, commonly defined as liquid-ordered domains rich in cholesterol and in lipids with high gel-to-fluid melting temperatures (T(m)), the rules for raft formation in membranes are not completely understood. Here, a fluorescence-quenching strategy was used to define how lipids with low T(m), which tend to form disordered fluid domains at physiological temperatures, can stabilize ordered domain formation by cholesterol and high-T(m) lipids (either sphingomyelin or dipalmitoylphosphatidylcholine). In bilayers containing mixtures of low-T(m) phosphatidylcholines, cholesterol, and high-T(m) lipid, the thermal stability of ordered domains decreased with the acyl-chain structure of low-T(m) lipids in the following order: diarachadonyl > diphytanoyl > 1-palmitoyl 2-docosahexenoyl = 1,2 dioleoyl = dimyristoleoyl = 1-palmitoyl, 2-oleoyl (PO). This shows that low-T(m) lipids with two acyl chains having very poor tight-packing propensities can stabilize ordered domain formation by high-T(m) lipids and cholesterol. The effect of headgroup structure was also studied. We found that even in the absence of high-T(m) lipids, mixtures of cholesterol with PO phosphatidylethanolamine (POPE) and PO phosphatidylserine (POPS) or with brain PE and brain PS showed a (borderline) tendency to form ordered domains. Because these lipids are abundant in the inner (cytofacial) leaflet of mammalian membranes, this raises the possibility that PE and PS could participate in inner-leaflet raft formation or stabilization. In bilayers containing ternary mixtures of PO lipids, cholesterol, and high-T(m) lipids, the thermal stability of ordered domains decreased with the polar headgroup structure of PO lipids in the order PE > PS > phosphatidylcholine (PC). Analogous experiments using diphytanoyl acyl chain lipids in place of PO acyl chain lipids showed that the stabilization of ordered lipid domains by acyl chain and headgroup structure was not additive. This implies that it is likely that there are two largely mutually exclusive mechanisms by which low-T(m) lipids can stabilize ordered domain formation by high-T(m) lipids and cholesterol: 1), by having structures resulting in immiscibility of low-T(m) and high-T(m) lipids, and 2), by having structures allowing them to pack tightly within ordered domains to a significant degree.

Effect of the structure of lipids favoring disordered domain formation on the stability of cholesterol-containing ordered domains (lipid rafts): identification of multiple raft-stabilization mechanisms. Publishing Authors By Initials

O Bakht,P Pathak,E London,O Bakht,P Pathak,E London,O Bakht,P Pathak,E London,O Bakht,P Pathak,E London,

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Effect of the structure of lipids favoring disordered domain formation on the stability of cholesterol-containing ordered domains (lipid rafts): identification of multiple raft-stabilization mechanisms. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biophysical journal

VOLUME: 93

Page Numbers: 4307-18

Journal Abbreviation: Biophys. J.

ISSN: 0006-3495

DAY: 31

MONTH: 08

YEAR: 2007

Effect of the structure of lipids favoring disordered domain formation on the stability of cholesterol-containing ordered domains (lipid rafts): identification of multiple raft-stabilization mechanisms. Information

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LANGUAGE: eng

NlmUniqueID: 370626

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AFFILIATION: Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York.

Country: United States

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MEDLINETA: Biophys J

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