Non‐uniform distribution of phospholipids in (Na+ + K+‐ATPase‐rich membranes from Torpedo marmorata electric organ evidenced by spin—spin interactions between spin‐labeled phospholipids

Zachowski, Alain; Devaux, Philippe F.

doi:10.1016/0014-5793(83)80828-x

Cited by 15 publications

(7 citation statements)

References 18 publications

(4 reference statements)

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“…Besides no studies have focused on cellular localization of synaptosomal (Na + /K + )ATPase in torpedo electric organ, a clear-cut heterogeneous distribution among different types of membranes have been reported in previous works (Zubler-Faivre and Dunant, 1976;Elfman et al, 1982;Zachowski and Devaux, 1983;Jentsch et al, 1989;Camus et al, 1998;Marchand et al, 2000;Blanton et al, 2001;Lukas et al, 2002). In the electric organ, probably more than 90% of the (Na + /K + )ATPase activity is localized at the non innervated (dorsal) face of electroplaques, in a very dense array of small invaginations (cannaliculi of about 0.1 m in diameter), which form quite dense "bodies" during the preparation of pinchedoff nerve endings.…”

Section: Differential Inhibition Of (Na + /K + )Atpase By Aluminiummentioning

confidence: 90%

Comparative effects of aluminum and ouabain on synaptosomal choline uptake, acetylcholine release and (Na+/K+)ATPase

Silva¹,

Nunes²,

Cordeiro³

et al. 2007

Toxicology

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Section: Differential Inhibition Of (Na + /K + )Atpase By Aluminiummentioning

confidence: 90%

Comparative effects of aluminum and ouabain on synaptosomal choline uptake, acetylcholine release and (Na+/K+)ATPase

Silva¹,

Nunes²,

Cordeiro³

et al. 2007

Toxicology

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“…A selectivity for spin-labeled phosphatidic acid and phosphatidylserine has also been demonstrated by the reduced spinspin interaction in (Na+,K+)-ATPase membranes from Torpedo marmorata (Zachowski & Devaux, 1983). These results are interesting since they also suggest a reduced rate of lipid exchange at the protein interface (cf.…”

Section: Discussionmentioning

confidence: 99%

Spin-label studies of lipid-protein interactions in sodium-potassium ATPase membranes from rectal glands of Squalus acanthias

Esmann¹,

Watts²,

Marsh³

1985

Biochemistry

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Lipid-protein interactions in (Na+,K+)-ATPase-rich membranes from the rectal gland of Squalus acanthias have been studied by using spin-labeled lipids in conjunction with electron spin resonance (ESR) spectroscopy. Lipid-protein associations are revealed by the presence of a second component in the ESR spectra of the membranes in addition to a component which corresponds very closely to the ESR spectra obtained from dispersions of the extracted membrane lipids. This second component corresponds to spin-labeled lipids whose motion is very significantly restricted relative to that of the fluid lipids in the membrane or the lipid extract. A stoichiometry of approximately 66 lipids per 265 000-dalton protein is found for the motionally restricted component of those spin-labeled lipids (e.g., phosphatidylcholine) which show least specificity for the protein. This corresponds approximately to the number of lipids which may be accommodated within the first shell around the alpha 2 beta 2 protein dimer. A selectivity of the various spin-labeled lipids for the motionally restricted component associated with the protein is found in the following order: cardiolipin greater than phosphatidylserine approximately stearic acid greater than or equal to phosphatidic acid greater than phosphatidylglycerol approximately phosphatidylcholine approximately phosphatidylethanolamine approximately androstanol.

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“…Experimentally, domains have been observed using fluorescence digital imaging microscopy (Luan et al, 1995;Denisov et al, 1998), fluorescence recovery after photobleaching (FRAP) (Jovin and Vaz, 1989;Polozova and Litman, 2000), fluorescence spectroscopy (Davenport et al, 1989), fluorescence resonance energy transfer (FRET) (Stillwell et al, 2000), electron spin resonance (ESR) spectroscopy (Zachowski and Devaux, 1983), atomic force microscopy (Gliss et al, 1998), vibrational spectroscopy (Mendelsohn and Moore, 1998), and 2 H NMR spectroscopy (Mitrakos and Macdonald, 1996, 1997Macdonald, 1997, 1998). Few of these techniques are capable of defining domain composition.…”

Section: Introductionmentioning

confidence: 99%

Polylysine-Induced 2H NMR-Observable Domains in Phosphatidylserine/Phosphatidylcholine Lipid Bilayers

Franzin

Macdonald

2001

Biophysical Journal

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The interaction of three polylysines, Lys(5) (N = 5), Lys(30) (N = 30), and Lys(100) (N = 100), where N is the number of lysine residues per chain, with phosphatidylserine-containing lipid bilayer membranes was investigated using 2H NMR spectroscopy. Lys(30) and Lys(100) added to multilamellar vesicles composed of (70:30) (mol:mol) mixtures of choline-deuterated 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) + 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine (POPS) produced two resolvable 2H NMR spectral components under conditions of low ionic strength and for cases where the global anionic lipid charge was in excess over the global cationic polypeptide charge. The intensities and quadrupolar splittings of the two spectral components were consistent with the existence of polylysine-bound domains enriched in POPS, in coexistence with polylysine-free domains depleted in POPS. Lys(5), however, yielded no 2H NMR resolvable domains. Increasing ionic strength caused domains to become diffuse and eventually dissipate entirely. At physiological salt concentrations, only Lys(100) yielded 2H NMR-resolvable domains. Therefore, under physiological conditions of ionic strength, pH, and anionic lipid bilayer content, and in the absence of other, e.g., hydrophobic, contributions to the binding free energy, the minimum number of lysine residues sufficient to produce spectroscopically resolvable POPS-enriched domains on the 2H NMR millisecond timescale may be fewer than 100, but is certainly greater than 30.

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Non‐uniform distribution of phospholipids in (Na⁺ + K⁺‐ATPase‐rich membranes from Torpedo marmorata electric organ evidenced by spin—spin interactions between spin‐labeled phospholipids

Cited by 15 publications

References 18 publications

Comparative effects of aluminum and ouabain on synaptosomal choline uptake, acetylcholine release and (Na+/K+)ATPase

Comparative effects of aluminum and ouabain on synaptosomal choline uptake, acetylcholine release and (Na+/K+)ATPase

Spin-label studies of lipid-protein interactions in sodium-potassium ATPase membranes from rectal glands of Squalus acanthias

Polylysine-Induced 2H NMR-Observable Domains in Phosphatidylserine/Phosphatidylcholine Lipid Bilayers

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