Transmembrane Dynamics of Lipids

Devaux, Philippe F.; Herrmann, Andreas

doi:10.1002/9781118120118

Cited by 5 publications

(2 citation statements)

References 34 publications

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“…A detailed analysis of plasma membrane asymmetry in physiological context requires a methodology that can probe dynamics and organization of both leaflets of an intact cell membrane separately with sufficient spatiotemporal resolution. In addition to the quantitative nature of the method, the other key points necessary to analyze the transbilayer membrane organization are 15 : (1) There should be a way of separating the information originating from the two leaflets. This can be achieved by using lipid probes that confine themselves predominantly to one particular leaflet or by selectively quenching the fluorescence signal from one leaflet using a membrane impermeable agent, e.g.…”

Section: Introductionmentioning

confidence: 99%

Analysing plasma membrane asymmetry of lipid organisation by fluorescence lifetime and correlation spectroscopy

Gupta

Korte

Herrmann

et al. 2019

Preprint

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Asymmetric organization of plasma membrane lipids 2 ABSTRACT A fundamental feature of a eukaryotic cell membrane is the asymmetric arrangement of lipids in the two leaflets. A cell invests significant energy to maintain this asymmetry and utilizes it to regulate important biological processes such as apoptosis and vesiculation. Here, we employ fluorescence lifetime imaging microscopy (FLIM) and imaging total internal reflection fluorescence correlation spectroscopy (ITIR-FCS) to differentiate the dynamics and organization of the exofacial and cytoplasmic leaflet of live mammalian cells. We characterize the biophysical properties of fluorescent analogues of phosphatidylcholine (PC), sphingomyelin (SM) and phosphatidylserine (PS) in two mammalian cell membranes. Due to their specific transverse membrane distribution, these probes allow leaflet specific investigation of the plasma membrane. We compare the results with regard to the different temporal and spatial resolution of the methods. Fluorescence lifetimes of fluorescent lipid analogues were found to be in a characteristic range for the liquid ordered phase in the outer leaflet and liquid disordered phase in the inner leaflet. The observation of a more fluid inner leaflet is supported by free diffusion in the inner leaflet with high average diffusion coefficients. The liquid ordered phase in the outer leaflet is accompanied by slower diffusion and diffusion with intermittent transient trapping.Our results show that the combination of FLIM and ITIR-FCS with specific fluorescent lipid analogues provides a powerful tool to investigate lateral and trans-bilayer characteristics of plasma membrane in live cells.

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Section: Introductionmentioning

confidence: 99%

Analysing plasma membrane asymmetry of lipid organisation by fluorescence lifetime and correlation spectroscopy

Gupta

Korte

Herrmann

et al. 2019

Preprint

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“…The asymmetry of lens membranes is not well characterized, but it is expected that the younger cells in the outer part of the cortex retain the leaflet asymmetry typical of most mammalian plasma membranes, with phosphatidylethanolmine (PE), phosphatidylserine (PS) and phosphatidylinositol (PI) lipids enriched in the cytoplasmic leaflet and phosphatidylcholine (PC) and sphingolipids such as sphingomyelin (SM) enriched in the exoplasmic leaflet [18,19]. As a consequence, acyl transfer from the membrane to AQP0 would be expected produce a distribution of acyl groups that reflects the acyl composition of PE and PS, and to a lesser extent (due to their low abundance), PI lipids.…”

Section: Discussionmentioning

confidence: 99%

The lipidation profile of aquaporin-0 correlates with the acyl composition of phosphoethanolamine lipids in lens membranes

Ismail¹,

Mosely²,

Tapodi³

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT AbstractThe lens fiber major intrinsic protein (otherwise known as aquaporin-0 (AQP0), MIP26 and MP26) has been examined by mass spectrometry (MS) in order to determine the speciation of acyl modifications to the side chains of lysine residues and the N-terminal amino group. The speciation of acyl modifications to the side chain of one specific, highly conserved lysine residue (K238) and the N-terminal amino group of human and bovine AQP0 revealed, in decreasing order of abundance, oleoyl, palmitoyl, stearoyl, eicosenoyl, dihomo--linolenoyl, palmitoleoyl and eicosadienoyl modifications. In the case of human AQP0, an arachidonoyl modification was also found at the N-terminus. The relative abundances of these modifications mirror the fatty acid composition of lens phosphatidylethanolamine lipids. This lipid class would be expected to be concentrated in the inner leaflet of the lens fiber membrane to which each of the potential AQP0 lipidation sites is proximal. Our data evidence a broad lipidation profile that is both species and site independent, suggesting a chemical-based ester aminolysis mechanism to explain such modifications.

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The Chemical Reactivity of Membrane Lipids

Duché,

Sanderson

2024

Chem. Rev.

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It is well-known that aqueous dispersions of phospholipids spontaneously assemble into bilayer structures. These structures have numerous applications across chemistry and materials science and form the fundamental structural unit of the biological membrane. The particular environment of the lipid bilayer, with a water-poor low dielectric core surrounded by a more polar and better hydrated interfacial region, gives the membrane particular biophysical and physicochemical properties and presents a unique environment for chemical reactions to occur. Many different types of molecule spanning a range of sizes, from dissolved gases through small organics to proteins, are able to interact with membranes and promote chemical changes to lipids that subsequently affect the physicochemical properties of the bilayer. This Review describes the chemical reactivity exhibited by lipids in their membrane form, with an emphasis on conditions where the lipids are well hydrated in the form of bilayers. Key topics include the following: lytic reactions of glyceryl esters, including hydrolysis, aminolysis, and transesterification; oxidation reactions of alkenes in unsaturated fatty acids and sterols, including autoxidation and oxidation by singlet oxygen; reactivity of headgroups, particularly with reactive carbonyl species; and E/Z isomerization of alkenes. The consequences of reactivity for biological activity and biophysical properties are also discussed. CONTENTS

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Transmembrane Dynamics of Lipids

Cited by 5 publications

References 34 publications

Analysing plasma membrane asymmetry of lipid organisation by fluorescence lifetime and correlation spectroscopy

Analysing plasma membrane asymmetry of lipid organisation by fluorescence lifetime and correlation spectroscopy

The lipidation profile of aquaporin-0 correlates with the acyl composition of phosphoethanolamine lipids in lens membranes

The Chemical Reactivity of Membrane Lipids

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