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Article: Regulation of Gramicidin Channel Function Solely by Changes in Lipid Intrinsic Curvature.

Maer, Andreia M / Rusinova, Radda / Providence, Lyndon L / Ingólfsson, Helgi I / Collingwood, Shemille A / Lundbæk, Jens A / Andersen, Olaf S

Frontiers in physiology

2022 Volume 13, Page(s) 836789

Abstract: Membrane protein function is regulated by the lipid bilayer composition. In many cases the changes in function correlate with changes in the lipid intrinsic curvature ( ...

Abstract	Membrane protein function is regulated by the lipid bilayer composition. In many cases the changes in function correlate with changes in the lipid intrinsic curvature (
Language	English
Publishing date	2022-03-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2564217-0
ISSN	1664-042X
ISSN	1664-042X
DOI	10.3389/fphys.2022.836789
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Article ; Online: Lipid bilayer-mediated regulation of ion channel function by amphiphilic drugs.

Lundbaek, Jens A

The Journal of general physiology

2008 Volume 131, Issue 5, Page(s) 421–429

MeSH term(s)	Animals ; Biomarkers, Pharmacological ; Biomechanical Phenomena ; Cell Membrane/chemistry ; Cell Membrane/drug effects ; Dose-Response Relationship, Drug ; Energy Transfer/drug effects ; Gramicidin/chemistry ; Humans ; Hydrophobic and Hydrophilic Interactions ; Ion Channels/chemistry ; Ion Channels/drug effects ; Lipid Bilayers/chemistry ; Pharmaceutical Preparations/chemistry ; Surface-Active Agents/chemistry ; Surface-Active Agents/pharmacology
Chemical Substances	Biomarkers, Pharmacological ; Ion Channels ; Lipid Bilayers ; Pharmaceutical Preparations ; Surface-Active Agents ; Gramicidin (1405-97-6)
Language	English
Publishing date	2008-04-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3118-5
ISSN	1540-7748 ; 0022-1295
ISSN (online)	1540-7748
ISSN	0022-1295
DOI	10.1085/jgp.200709948
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Article: Regulation of membrane protein function by lipid bilayer elasticity-a single molecule technology to measure the bilayer properties experienced by an embedded protein.

Lundbæk, Jens August

Journal of physics. Condensed matter : an Institute of Physics journal

2006 Volume 18, Issue 28, Page(s) S1305–44

Abstract: Membrane protein function is generally regulated by the molecular composition of the host lipid bilayer. The underlying mechanisms have long remained enigmatic. Some cases involve specific molecular interactions, but very often lipids and other ... ...

Abstract	Membrane protein function is generally regulated by the molecular composition of the host lipid bilayer. The underlying mechanisms have long remained enigmatic. Some cases involve specific molecular interactions, but very often lipids and other amphiphiles, which are adsorbed to lipid bilayers, regulate a number of structurally unrelated proteins in an apparently non-specific manner. It is well known that changes in the physical properties of a lipid bilayer (e.g., thickness or monolayer spontaneous curvature) can affect the function of an embedded protein. However, the role of such changes, in the general regulation of membrane protein function, is unclear. This is to a large extent due to lack of a generally accepted framework in which to understand the many observations. The present review summarizes studies which have demonstrated that the hydrophobic interactions between a membrane protein and the host lipid bilayer provide an energetic coupling, whereby protein function can be regulated by the bilayer elasticity. The feasibility of this 'hydrophobic coupling mechanism' has been demonstrated using the gramicidin channel, a model membrane protein, in planar lipid bilayers. Using voltage-dependent sodium channels, N-type calcium channels and GABA(A) receptors, it has been shown that membrane protein function in living cells can be regulated by amphiphile induced changes in bilayer elasticity. Using the gramicidin channel as a molecular force transducer, a nanotechnology to measure the elastic properties experienced by an embedded protein has been developed. A theoretical and technological framework, to study the regulation of membrane protein function by lipid bilayer elasticity, has been established.
Language	English
Publishing date	2006-07-19
Publishing country	England
Document type	Journal Article
ZDB-ID	1472968-4
ISSN	1361-648X ; 0953-8984
ISSN (online)	1361-648X
ISSN	0953-8984
DOI	10.1088/0953-8984/18/28/S13
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Article ; Online: Linear rate-equilibrium relations arising from ion channel-bilayer energetic coupling.

Greisen, Per / Lum, Kevin / Ashrafuzzaman, Md / Greathouse, Denise V / Andersen, Olaf S / Lundbæk, Jens A

Proceedings of the National Academy of Sciences of the United States of America

2011 Volume 108, Issue 31, Page(s) 12717–12722

Abstract: Linear rate-equilibrium (RE) relations, also known as linear free energy relations, are widely observed in chemical reactions, including protein folding, enzymatic catalysis, and channel gating. Despite the widespread occurrence of linear RE relations, ... ...

Abstract	Linear rate-equilibrium (RE) relations, also known as linear free energy relations, are widely observed in chemical reactions, including protein folding, enzymatic catalysis, and channel gating. Despite the widespread occurrence of linear RE relations, the principles underlying the linear relation between changes in activation and equilibrium energy in macromolecular reactions remain enigmatic. When examining amphiphile regulation of gramicidin channel gating in lipid bilayers, we noted that the gating process could be described by a linear RE relation with a simple geometric interpretation. This description is possible because the gating process provides a well-understood reaction, in which structural changes in a bilayer-embedded model protein can be studied at the single-molecule level. It is thus possible to obtain quantitative information about the energetics of the reaction transition state and its position on a spatial coordinate. It turns out that the linear RE relation for the gramicidin monomer-dimer reaction can be understood, and the quantitative relation between changes in activation energy and equilibrium energy can be interpreted, by considering the effects of amphiphiles on the changes in bilayer elastic energy associated with channel gating. We are not aware that a similar simple mechanistic explanation of a linear RE relation has been provided for a chemical reaction in a macromolecule. RE relations generally should be useful for examining how amphiphile-induced changes in bilayer properties modulate membrane protein folding and function, and for distinguishing between direct (e.g., due to binding) and indirect (bilayer-mediated) effects.
MeSH term(s)	Algorithms ; Capsaicin/pharmacology ; Chromans/pharmacology ; Energy Transfer/drug effects ; Genistein/pharmacology ; Gramicidin/chemistry ; Hydrophobic and Hydrophilic Interactions ; Ion Channel Gating/drug effects ; Ion Channels/chemistry ; Kinetics ; Lipid Bilayers/chemistry ; Membrane Lipids/chemistry ; Models, Chemical ; Octoxynol/pharmacology ; Phosphatidylcholines/chemistry ; Protein Folding ; Rosiglitazone ; Thiazolidinediones/pharmacology ; Troglitazone
Chemical Substances	Chromans ; Ion Channels ; Lipid Bilayers ; Membrane Lipids ; Phosphatidylcholines ; Thiazolidinediones ; Rosiglitazone (05V02F2KDG) ; Gramicidin (1405-97-6) ; 1,2-diphytanoylphosphatidylcholine (32448-32-1) ; Octoxynol (9002-93-1) ; Genistein (DH2M523P0H) ; 1,2-oleoylphosphatidylcholine (EDS2L3ODLV) ; Troglitazone (I66ZZ0ZN0E) ; Capsaicin (S07O44R1ZM)
Language	English
Publishing date	2011-07-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1103192108
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Article: Amphiphile regulation of ion channel function by changes in the bilayer spring constant

Lundbæk, Jens A / Koeppe, Roger E. II / Andersen, Olaf S

Proceedings of the National Academy of Sciences of the United States of America. 2010 Aug. 31, v. 107, no. 35

2010

Abstract: Many drugs are amphiphiles that, in addition to binding to a particular target protein, adsorb to cell membrane lipid bilayers and alter intrinsic bilayer physical properties (e.g., bilayer thickness, monolayer curvature, and elastic moduli). Such ... ...

Abstract	Many drugs are amphiphiles that, in addition to binding to a particular target protein, adsorb to cell membrane lipid bilayers and alter intrinsic bilayer physical properties (e.g., bilayer thickness, monolayer curvature, and elastic moduli). Such changes can modulate membrane protein function by altering the energetic cost (ΔGbilayer) of bilayer deformations associated with protein conformational changes that involve the protein-bilayer interface. But amphiphiles have complex effects on the physical properties of lipid bilayers, meaning that the net change in ΔGbilayer cannot be predicted from measurements of isolated changes in such properties. Thus, the bilayer contribution to the promiscuous regulation of membrane proteins by drugs and other amphiphiles remains unknown. To overcome this problem, we use gramicidin A (gA) channels as molecular force probes to measure the net effect of amphiphiles, at concentrations often used in biological research, on the bilayer elastic response to a change in the hydrophobic length of an embedded protein. The effects of structurally diverse amphiphiles can be described by changes in a phenomenological bilayer spring constant (HB) that summarizes the bilayer elastic properties, as sensed by a bilayer-spanning protein. Amphiphile-induced changes in HB, measured using gA channels of a particular length, quantitatively predict changes in lifetime for channels of a different length--as well as changes in the inactivation of voltage-dependent sodium channels in living cells. The use of gA channels as molecular force probes provides a tool for quantitative, predictive studies of bilayer-mediated regulation of membrane protein function by amphiphiles.
Keywords	deformation ; drugs ; gramicidin ; hydrophobicity ; lipid bilayers ; modulus of elasticity ; sodium channels
Language	English
Dates of publication	2010-0831
Size	p. 15427-15430.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1007455107
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Article ; Online: Amphiphile regulation of ion channel function by changes in the bilayer spring constant.

Lundbaek, Jens A / Koeppe, Roger E / Andersen, Olaf S

Proceedings of the National Academy of Sciences of the United States of America

2010 Volume 107, Issue 35, Page(s) 15427–15430

Abstract	Many drugs are amphiphiles that, in addition to binding to a particular target protein, adsorb to cell membrane lipid bilayers and alter intrinsic bilayer physical properties (e.g., bilayer thickness, monolayer curvature, and elastic moduli). Such changes can modulate membrane protein function by altering the energetic cost (DeltaG(bilayer)) of bilayer deformations associated with protein conformational changes that involve the protein-bilayer interface. But amphiphiles have complex effects on the physical properties of lipid bilayers, meaning that the net change in DeltaG(bilayer) cannot be predicted from measurements of isolated changes in such properties. Thus, the bilayer contribution to the promiscuous regulation of membrane proteins by drugs and other amphiphiles remains unknown. To overcome this problem, we use gramicidin A (gA) channels as molecular force probes to measure the net effect of amphiphiles, at concentrations often used in biological research, on the bilayer elastic response to a change in the hydrophobic length of an embedded protein. The effects of structurally diverse amphiphiles can be described by changes in a phenomenological bilayer spring constant (H(B)) that summarizes the bilayer elastic properties, as sensed by a bilayer-spanning protein. Amphiphile-induced changes in H(B), measured using gA channels of a particular length, quantitatively predict changes in lifetime for channels of a different length--as well as changes in the inactivation of voltage-dependent sodium channels in living cells. The use of gA channels as molecular force probes provides a tool for quantitative, predictive studies of bilayer-mediated regulation of membrane protein function by amphiphiles.
MeSH term(s)	Algorithms ; Capsaicin/analogs & derivatives ; Capsaicin/chemistry ; Capsaicin/pharmacology ; Cell Line ; Cell Membrane/chemistry ; Cell Membrane/drug effects ; Cell Membrane/physiology ; Genistein/chemistry ; Genistein/pharmacology ; Gramicidin/chemistry ; Gramicidin/pharmacology ; Humans ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Ion Channel Gating/drug effects ; Ion Channel Gating/physiology ; Ion Channels/chemistry ; Ion Channels/physiology ; Isoflavones/chemistry ; Isoflavones/pharmacology ; Kinetics ; Lipid Bilayers/chemistry ; Membrane Potentials/drug effects ; Membrane Proteins/chemistry ; Octoxynol/chemistry ; Octoxynol/pharmacology ; Phloretin/chemistry ; Phloretin/pharmacology ; Phosphatidylcholines/chemistry ; Protein Conformation/drug effects
Chemical Substances	Ion Channels ; Isoflavones ; Lipid Bilayers ; Membrane Proteins ; Phosphatidylcholines ; Gramicidin (1405-97-6) ; 1,2-diphytanoylphosphatidylcholine (32448-32-1) ; daidzein (6287WC5J2L) ; Octoxynol (9002-93-1) ; Genistein (DH2M523P0H) ; 1,2-oleoylphosphatidylcholine (EDS2L3ODLV) ; capsazepine (LFW48MY844) ; Capsaicin (S07O44R1ZM) ; Phloretin (S5J5OE47MK)
Language	English
Publishing date	2010-08-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1007455107
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Regulation of endothelial cell migration by amphiphiles - are changes in cell membrane physical properties involved?

Jensen, Lasse D E / Hansen, Anker J / Lundbaek, Jens A

Angiogenesis

2007 Volume 10, Issue 1, Page(s) 13–22

Abstract: Endothelial cell (EC) migration is an integral part of angiogenesis and a prerequisite for malignant tumor growth. Recent studies suggest that amphiphilic compounds can regulate migration of bovine aortic ECs by altering the physical properties of the ... ...

Abstract	Endothelial cell (EC) migration is an integral part of angiogenesis and a prerequisite for malignant tumor growth. Recent studies suggest that amphiphilic compounds can regulate migration of bovine aortic ECs by altering the physical properties of the cell membrane lipid bilayers. A number of structurally different amphiphiles thus regulate the migration in quantitative correlation with their effects on the plasma membrane microviscosity. Many amphiphiles that affect EC migration and angiogenesis alter the physical properties of lipid bilayers, suggesting that such a regulatory mechanism may be of general importance. To investigate this notion, we studied the effects of lysophospholipids that inhibit migration of bovine aortic ECs and decrease cell membrane microviscosity, and of other amphiphiles that decrease membrane microviscosity (Triton X-100, octyl-beta-glucoside, arachidonic acid, docosahexaenoic acid, ETYA, capsaicin) on the migration of porcine aortic ECs. We further studied whether the enzyme secretory phospholipase A(2) (sPLA(2)) would affect migration in accordance with the changes in membrane microviscosity induced by its hydrolysis products lysophospholipids and polyunsaturated fatty acids. Arachidonic acid, at low concentrations, promoted cell migration by a mechanism involving metabolic products of this compound. Apart from this effect, all the amphiphiles, as well as sPLA(2), inhibited cell migration. A semi-quantitative analysis found a similar correlation between the effects on migration and on lipid bilayer stiffness measured using gramicidin channels as molecular force transducers. These results suggest that changes in cell membrane physical properties may generally contribute to the effects of amphiphiles on EC migration.
MeSH term(s)	Animals ; Arachidonic Acid/metabolism ; Cell Culture Techniques/methods ; Cell Membrane/drug effects ; Cell Membrane/physiology ; Cell Movement/drug effects ; Cell Movement/physiology ; Docosahexaenoic Acids/metabolism ; Endothelial Cells/physiology ; Glucosides/chemistry ; Glucosides/pharmacology ; Lipid Bilayers/chemistry ; Lysophospholipids/metabolism ; Membrane Fluidity/drug effects ; Membrane Fluidity/physiology ; Membrane Lipids/metabolism ; Octoxynol/chemistry ; Octoxynol/pharmacology ; Surface-Active Agents/chemistry ; Surface-Active Agents/pharmacology ; Swine
Chemical Substances	Glucosides ; Lipid Bilayers ; Lysophospholipids ; Membrane Lipids ; Surface-Active Agents ; Docosahexaenoic Acids (25167-62-8) ; Arachidonic Acid (27YG812J1I) ; octyl-beta-D-glucoside (29836-26-8) ; Octoxynol (9002-93-1)
Language	English
Publishing date	2007
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1484717-6
ISSN	0969-6970
ISSN	0969-6970
DOI	10.1007/s10456-006-9060-y
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Article: Vitamin D enhanced pork from pigs exposed to artificial UVB light in indoor facilities

Barnkob, Line Lundbaek / Paul Michael Petersen / Jens Peter Nielsen / Jette Jakobsen

European food research & technology. 2019 Feb., v. 245, no. 2

2019

Abstract: Vitamin D deficiency is a recognized problem in Europe; this can be minimized by fortifying a broader range of foods. Our aim was to investigate the potential for enhancing the vitamin D content of pork from pigs raised in indoor facilities, by exposing ... ...

Abstract	Vitamin D deficiency is a recognized problem in Europe; this can be minimized by fortifying a broader range of foods. Our aim was to investigate the potential for enhancing the vitamin D content of pork from pigs raised in indoor facilities, by exposing the pigs to UVB for a period just before slaughter. Three groups of six pigs were exposed to 0, 0.7 or 1 SED/day for 28 days. A fourth group was exposed to 2 SED; this treatment was not completed due to mild erythema. The highest increase of vitamin D₃ was achieved with 1 SED; the vitamin D₃ content in loin was 3.7 ng/g; more than a factor of 2 higher compared to previously reported results from studies using 2000 IU/kg feed, the maximum allowed level in Europe. This is the first time an increase in the vitamin D content of pork has been reported as a result of using artificial UVB exposure of slaughter pigs in indoor facilities. However, the maximum production of vitamin D was probably not reached as a linear relationship between UVB dose and vitamin D content was found; therefore, the UVB-lighting method described still calls for further investigation to realise its full potential to enhance vitamin D in pork.
Keywords	cholecalciferol ; erythema ; food research ; pork ; slaughter ; swine ; ultraviolet radiation ; vitamin D deficiency ; Europe
Language	English
Dates of publication	2019-02
Size	p. 411-418.
Publishing place	Springer Berlin Heidelberg
Document type	Article
ZDB-ID	1359456-4
ISSN	1431-4630 ; 1438-2377
ISSN	1431-4630 ; 1438-2377
DOI	10.1007/s00217-018-3173-6
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes.

Lundbaek, Jens A / Collingwood, Shemille A / Ingólfsson, Helgi I / Kapoor, Ruchi / Andersen, Olaf S

Journal of the Royal Society, Interface

2009 Volume 7, Issue 44, Page(s) 373–395

Abstract: Membrane protein function is regulated by the host lipid bilayer composition. This regulation may depend on specific chemical interactions between proteins and individual molecules in the bilayer, as well as on non-specific interactions between proteins ... ...

Abstract	Membrane protein function is regulated by the host lipid bilayer composition. This regulation may depend on specific chemical interactions between proteins and individual molecules in the bilayer, as well as on non-specific interactions between proteins and the bilayer behaving as a physical entity with collective physical properties (e.g. thickness, intrinsic monolayer curvature or elastic moduli). Studies in physico-chemical model systems have demonstrated that changes in bilayer physical properties can regulate membrane protein function by altering the energetic cost of the bilayer deformation associated with a protein conformational change. This type of regulation is well characterized, and its mechanistic elucidation is an interdisciplinary field bordering on physics, chemistry and biology. Changes in lipid composition that alter bilayer physical properties (including cholesterol, polyunsaturated fatty acids, other lipid metabolites and amphiphiles) regulate a wide range of membrane proteins in a seemingly non-specific manner. The commonality of the changes in protein function suggests an underlying physical mechanism, and recent studies show that at least some of the changes are caused by altered bilayer physical properties. This advance is because of the introduction of new tools for studying lipid bilayer regulation of protein function. The present review provides an introduction to the regulation of membrane protein function by the bilayer physical properties. We further describe the use of gramicidin channels as molecular force probes for studying this mechanism, with a unique ability to discriminate between consequences of changes in monolayer curvature and bilayer elastic moduli.
MeSH term(s)	Gramicidin/metabolism ; Hydrophobic and Hydrophilic Interactions ; Kinetics ; Lipid Bilayers/chemistry ; Membrane Fluidity ; Membrane Proteins/chemistry ; Membrane Proteins/physiology ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/physiology ; Models, Biological ; Molecular Probes/chemistry ; Molecular Probes/metabolism ; Molecular Probes/physiology
Chemical Substances	Lipid Bilayers ; Membrane Proteins ; Membrane Transport Proteins ; Molecular Probes ; Gramicidin (1405-97-6)
Language	English
Publishing date	2009-11-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2156283-0
ISSN	1742-5662 ; 1742-5689
ISSN (online)	1742-5662
ISSN	1742-5689
DOI	10.1098/rsif.2009.0443
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Article: GABA(A) receptor function is regulated by lipid bilayer elasticity.

Søgaard, Rikke / Werge, Thomas M / Bertelsen, Camilla / Lundbye, Camilla / Madsen, Kenneth L / Nielsen, Claus H / Lundbaek, Jens A

Biochemistry

2006 Volume 45, Issue 43, Page(s) 13118–13129

Abstract: Docosahexaenoic acid (DHA) and other polyunsaturated fatty acids (PUFAs) promote GABA(A) receptor [(3)H]-muscimol binding, and DHA increases the rate of GABA(A) receptor desensitization. Triton X-100, a structurally unrelated amphiphile, similarly ... ...

Abstract	Docosahexaenoic acid (DHA) and other polyunsaturated fatty acids (PUFAs) promote GABA(A) receptor [(3)H]-muscimol binding, and DHA increases the rate of GABA(A) receptor desensitization. Triton X-100, a structurally unrelated amphiphile, similarly promotes [(3)H]-muscimol binding. The mechanism(s) underlying these effects are poorly understood. DHA and Triton X-100, at concentrations that affect GABA(A) receptor function, increase the elasticity of lipid bilayers measured as decreased bilayer stiffness using gramicidin channels as molecular force transducers. We have previously shown that membrane protein function can be regulated by amphiphile-induced changes in bilayer elasticity and hypothesized that GABA(A) receptors could be similarly regulated. We therefore studied the effects of four structurally unrelated amphiphiles that decrease bilayer stiffness (Triton X-100, octyl-beta-glucoside, capsaicin, and DHA) on GABA(A) receptor function in mammalian cells. All the compounds promoted GABA(A) receptor [(3)H]-muscimol binding by increasing the binding capacity of high-affinity binding without affecting the associated equilibrium binding constant. A semiquantitative analysis found a similar quantitative relation between the effects on bilayer stiffness and [(3)H]-muscimol binding. Membrane cholesterol depletion, which also decreases bilayer stiffness, similarly promoted [(3)H]-muscimol binding. In whole-cell voltage-clamp experiments, Triton X-100, octyl-beta-glucoside, capsaicin, and DHA all reduced the peak amplitude of the GABA-induced currents and increased the rate of receptor desensitization. The effects of the amphiphiles did not correlate with the expected changes in monolayer spontaneous curvature. We conclude that GABA(A) receptor function is regulated by lipid bilayer elasticity. PUFAs may generally regulate membrane protein function by affecting the elasticity of the host lipid bilayer.
MeSH term(s)	Animals ; CHO Cells ; Capsaicin/chemistry ; Capsaicin/pharmacology ; Cell Line ; Cricetinae ; Cricetulus ; Docosahexaenoic Acids/chemistry ; Docosahexaenoic Acids/pharmacology ; Glucosides/chemistry ; Glucosides/pharmacology ; Humans ; Ion Channels/drug effects ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Membrane Fluidity/drug effects ; Membrane Fluidity/physiology ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Muscimol/metabolism ; Octoxynol/chemistry ; Octoxynol/pharmacology ; Protein Binding/drug effects ; Receptors, GABA-A/genetics ; Receptors, GABA-A/metabolism ; Receptors, GABA-A/physiology ; Transfection ; Tritium
Chemical Substances	Glucosides ; Ion Channels ; Lipid Bilayers ; Membrane Proteins ; Receptors, GABA-A ; Tritium (10028-17-8) ; Docosahexaenoic Acids (25167-62-8) ; Muscimol (2763-96-4) ; octyl-beta-D-glucoside (29836-26-8) ; Octoxynol (9002-93-1) ; Capsaicin (S07O44R1ZM)
Language	English
Publishing date	2006-10-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi060734+
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