A comparative study of the phase transitions of phospholipid bilayers and monolayers

Blume, Alfred

doi:10.1016/0005-2736(79)90087-7

Cited by 401 publications

(228 citation statements)

References 38 publications

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“…In general, ⌬ is inversely proportional to 0 of the phospholipid monolayer, and an extrapolation of ⌬ versus 0 yields c , which specifies an upper limit of 0 that a protein can penetrate (56). The surface pressure of cell membranes and large unilamellar vesicles has been estimated to be 31-35 dynes/cm (63)(64)(65). Thus, for a protein to effectively penetrate a particular cell membrane (or large vesicles), it should have the c value above this range for the monolayer whose lipid composition mimics that of the cell membrane.…”

Section: Resultsmentioning

confidence: 99%

Mechanistic Basis of Differential Cellular Responses of Phosphatidylinositol 3,4-Bisphosphate- and Phosphatidylinositol 3,4,5-Trisphosphate-binding Pleckstrin Homology Domains

Manna

Albanese

Park

et al. 2007

Journal of Biological Chemistry

125

150

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Phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P 2 ) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P 3 ) are lipid second messengers that regulate various cellular processes by recruiting a wide range of downstream effector proteins to membranes. Several pleckstrin homology (PH) domains have been reported to interact with PtdIns(3,4)P 2 and PtdIns(3,4,5)P 3 . To understand how these PH domains differentially respond to PtdIns(3,4)P 2 and PtdIns(3,4,5)P 3 signals, we quantitatively determined the PtdIns(3,4)P 2 and PtdIns(3,4,5)P 3 binding properties of several PH domains, including Akt, ARNO, Btk, DAPP1, Grp1, and C-terminal TAPP1 PH domains by surface plasmon resonance and monolayer penetration analyses. The measurements revealed that these PH domains have significant different phosphoinositide specificities and affinities. Btk-PH and TAPP1-PH showed genuine PtdIns(3,4,5)P 3 and PtdIns(3,4)P 2 specificities, respectively, whereas other PH domains exhibited less pronounced specificities. Also, the PH domains showed different degrees of membrane penetration, which greatly affected the kinetics of their membrane dissociation. Mutational studies showed that the presence of two proximal hydrophobic residues on the membrane-binding surface of the PH domain is important for membrane penetration and sustained membrane residence. When NIH 3T3 cells were stimulated with platelet-derived growth factor to generate PtdIns(3,4,5)P 3 , reversible translocation of Btk-PH, Grp1-PH, ARNO-PH, DAPP1-PH, and its L177A mutant to the plasma membrane was consistent with their in vitro membrane binding properties. Collectively, these studies provide new insight into how various PH domains would differentially respond to cellular PtdIns(3,4)P 2 and PtdIns(3,4,5)P 3 signals. Phosphoinositides (PIs)2 are mono-and polyphosphorylated derivatives of phosphatidylinositol (PtdIns) (1-3). AlthoughPIs are minor components of membrane lipids, they regulate a wide range of biological processes, including cell proliferation, cell survival, differentiation, signal transduction, cytoskeleton organization, and membrane trafficking (1-3). PIs regulate these cellular processes primarily by serving as site-specific membrane signals that mediate the membrane recruitment and regulation of effector proteins. The PI-mediated cellular processes allow exceptional spatiotemporal specificity because the spatial and temporal distribution of various PIs is dynamically and tightly regulated by a series of PI-modifying enzymes, such as phospholipases, lipid kinases, and lipid phosphatases, located in different cell membranes (1-3). For instance, phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2 ) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P 3 ) are mainly found in the plasma membrane, whereas phosphatidylinositol 3-phosphate (PtdIns3P), phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 5-phosphate (PtdIns5P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P 2 ) are primarily present in endosomes, Golgi, nucl...

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Section: Resultsmentioning

confidence: 99%

Mechanistic Basis of Differential Cellular Responses of Phosphatidylinositol 3,4-Bisphosphate- and Phosphatidylinositol 3,4,5-Trisphosphate-binding Pleckstrin Homology Domains

Manna

Albanese

Park

et al. 2007

Journal of Biological Chemistry

125

150

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“…Figure 6 depicts the crosssectional molecular areas of the various sphingolipids at 30 mN/m in the absence and presence of cholesterol. Data obtained at 30 mN/m were of particular interest because there is much evidence indicating that surface pressures in the 30-35 mN/m range approximate those found in each half of bilayer membranes (Phillips & Chapman, 1968;Demel et al, 1975;Evans & Waugh, 1977;Blume, 1979;Cevc & Marsh, 1987). In Figure 6, each horizontal line corresponds to a different sphingolipid derivative with GalCer derivatives having filled symbols and SMs having unfilled symbols at the ends of their lines.…”

Section: What Effect Does Cholesterol Have On Sphingolipid-packing Dementioning

confidence: 99%

Cholesterol-Induced Interfacial Area Condensations of Galactosylceramides and Sphingomyelins with Identical Acyl Chains

et al. 1996

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The interfacial interactions occurring between cholesterol and either galactosylceramides (GalCers) or sphingomyelins (SMs) with identical acyl chains have been investigated using Langmuir film balance techniques. Included among the synthesized GalCers and SMs were species containing palmitoyl (16:0), stearoyl (18:0), oleoyl [18:1 ∆9(c) ], nervonoyl [24:1 ∆15(c) ], or linoleoyl [18:2 ∆9,12(c) ] acyl residues. The cholesterol-induced condensations in the average molecular areas of the monolayers were determined by classic mean molecular area vs composition plots as well as by expressing the changes in terms of sphingolipid cross-sectional area reduction over the surface pressure range from 1 to 40 mN/m (at 1 mN/m intervals). The results show that, at surface pressures approximating bilayer conditions (30 mN/m), acyl heterogeneity in naturally occurring SMs (bovine or egg SM) enhanced the area condensation induced by cholesterol compared to their predominant molecular species (e.g. 18:0 SM in bovine SM; 16:0 SM in egg SM). Nonetheless, cholesterol always had a greater condensing effect on SM compared to GalCer when these sphingolipids were acyl chain matched and in similar phase states (prior to mixing with cholesterol). Also, the cholesterol-induced area changes for a given sphingolipid type (e.g. SM or GalCer) were similar whether the acyl chains were saturated, cis-∆9-monounsaturated, or cis-∆9,12-diunsaturated if the sphingolipids were in similar phase states (prior to mixing with cholesterol) and compared at equivalent surface pressures. These results indicate that, under conditions where hydrocarbon structure is matched, the sphingolipid head group plays a dominant role in determining the extent to which cholesterol reduces sphingolipid cross-sectional area. Despite the larger cholesterol-induced area condensations observed in SMs compared to those in GalCers, the molecular-packing densities showed that equimolar GalCercholesterol films were generally packed as tight as or slightly tighter than those of the SMcholesterol films. The results are discussed in terms of a molecular model for sphingolipidcholesterol interactions. Our findings also not only raise questions as to whether cholesterolinduced condensation data provide a reliable measure of the affinity, i.e. interaction strength, between cholesterol and different lipids but also provide insight regarding the stability of sterol/ sphingolipid-rich microdomains thought to exist in caveolae and other cell membrane regions. † This investigation was supported by USPHS Grant GM45928 (R.E.B.) and the Hormel Foundation. The automated Langmuir film balance used in this study receives major support from USPHS Grants HL49180 and HL17371 (H. L. Brockman, P. I.).

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“…to examine whether the DHE separation into crystalline form in membrane lipids reflects that of cholesterol, force-area isotherms of DHE and cholesterol in POPC monolayers were compared (Table II) at a surface compression of 35 mN/m, in the range of that typical of lipid bilayers (44,50). Increasing the mol % of either DHE or cholesterol in the monolayer reduced the mean molecular area (Å 2 ), due to the condensing effect of sterols on phospholipid membranes.…”

Section: Force-area Isotherms Of Monolayers Formed From Dhe or Cholesmentioning

confidence: 99%

Fluorescence and Multiphoton Imaging Resolve Unique Structural Forms of Sterol in Membranes of Living Cells

McIntosh¹,

Gallegos²,

Atshaves³

et al. 2003

Journal of Biological Chemistry

113

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Although cholesterol is an essential component of mammalian membranes, resolution of cholesterol organization in membranes and organelles (i.e. lysosomes) of living cells is hampered by the paucity of nondestructive, nonperturbing methods providing real time structural information. Advantage was taken of the fact that the emission maxima of a naturally occurring fluorescent sterol (dehydroergosterol) were resolvable into two structural forms, monomeric (356 and 375 nm) and crystalline (403 and 426 nm). Model membranes (sterol:phospholipid ratios in the physiological range, e.g. 0.5-1.0), subcellular membrane fractions (plasma membranes, lysosomal membranes, microsomes, and mitochondrial membranes), and lipid rafts/caveolae (plasma membrane cholesterol-rich microdomain purified by a nondetergent method) contained primarily monomeric sterol and only small quantities (i.e. 1-5%) of the crystalline form. In contrast, the majority of sterol in isolated lysosomes was crystalline. However, addition of sterol carrier protein-2 in vitro significantly reduced the proportion of crystalline dehydroergosterol in the isolated lysosomes. Multiphoton laser scanning microscopy (MPLSM) of living L-cell fibroblasts cultured with dehydroergosterol for the first time provided real time images showing the presence of monomeric sterol in plasma membranes, as well as other intracellular membrane structures of living cells. Furthermore, MPLSM confirmed that crystalline sterol colocalized in highest amounts with LysoTracker Green, a lysosomal marker dye. Although crystalline sterol was also detected in the cytoplasm, the extralysosomal crystalline sterol did not colocalize with BODIPY FL C 5 -ceramide, a Golgi marker, and crystals were not associated with the cell surface membrane. These noninvasive, nonperturbing methods demonstrated for the first time that multiple structural forms of sterol normally occurred within membranes, membrane microdomains (lipid rafts/ caveolae), and intracellular organelles of living cells, both in vitro and visualized in real time by MPLSM.Cholesterol is essential for optimal membrane transport, receptor-effector coupling, cell recognition, and other eukaryotic cellular processes (reviewed in Ref. 1). Increasing evidence indicates that plasma membrane cholesterol is organized into lateral and transbilayer cholesterol-rich microdomains (reviewed in Ref.2) such as lipid rafts and caveolae (reviewed in Refs. 2-6). These domains contain proteins involved in multiple cellular functions including signaling and cholesterol transport. For example, overexpression of caveolin-1 in mice stimulates high density lipoprotein uptake via plasma membrane caveolae and markedly increases plasma high density lipoprotein-cholesterol (8). In contrast, caveolin-1-deficient mice are lean and resistant to diet-induced obesity but show hypertriglyceridemia and exhibit vascular abnormalities (9 -11). There is a strong association of cholesterol abnormalities with cytotoxicity, sickle cell acanthacytosis, Niemann-Pick C disease, Alzhe...

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A comparative study of the phase transitions of phospholipid bilayers and monolayers

Cited by 401 publications

References 38 publications

Mechanistic Basis of Differential Cellular Responses of Phosphatidylinositol 3,4-Bisphosphate- and Phosphatidylinositol 3,4,5-Trisphosphate-binding Pleckstrin Homology Domains

Mechanistic Basis of Differential Cellular Responses of Phosphatidylinositol 3,4-Bisphosphate- and Phosphatidylinositol 3,4,5-Trisphosphate-binding Pleckstrin Homology Domains

Cholesterol-Induced Interfacial Area Condensations of Galactosylceramides and Sphingomyelins with Identical Acyl Chains

Fluorescence and Multiphoton Imaging Resolve Unique Structural Forms of Sterol in Membranes of Living Cells

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