On the microstructure and phase diagram of dimyristoylphosphatidylcholine-glycophorin bilayers. The role of defects and the hydrophilic lipid-protein interaction

Rüppel, D.; Kapitza, H. G.; Galla, Hans‐Joachim; Sixl, F.; Sackmann, E.

doi:10.1016/0005-2736(82)90496-5

Cited by 56 publications

(19 citation statements)

References 18 publications

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“…The data thus far support the concept that GPA is tightly linked to membrane PE and interference with this interaction may expose PE and cause the functional changes induced by antibodies. The external component of GPA lies “pancake‐like” on the external surface in phospholipid vesicles where it interacts with approximately 300 lipid molecules 31 . In PE vesicles, hydrogen bonds between the COOH groups of sialic acid GPA and the amine groups of PE confers stability 32 .…”

Section: Discussionmentioning

confidence: 99%

“…The external component of GPA lies "pancake-like" on the external surface in phospholipid vesicles where it interacts with approximately 300 lipid molecules. 31 In PE vesicles, hydrogen bonds between the COOH groups of sialic acid GPA and the amine groups of PE confers stability. 32 Likewise, in RBCs the external component of GPA lies close to the surface of the membrane and interacts with the phospholipid bilayer, an interaction that diminishes with the age of RBCs.…”

Section: Brain Et Almentioning

confidence: 99%

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Life‐threatening hemolytic anemia due to an autoanti‐Pr cold agglutinin: evidence that glycophorin A antibodies may induce lipid bilayer exposure and cation permeability independent of agglutination

et al. 2010

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Section: Discussionmentioning

confidence: 99%

Section: Brain Et Almentioning

confidence: 99%

Life‐threatening hemolytic anemia due to an autoanti‐Pr cold agglutinin: evidence that glycophorin A antibodies may induce lipid bilayer exposure and cation permeability independent of agglutination

et al. 2010

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“…The trans ‐membrane portion of the molecule is intensely hydrophobic which leads it to exist as a dimer in the bilayer and to migrate as such in sodium dodecyl sulphate polyacrylamide electrophoresis gels, and to interact with the phospholipid fatty chains (Adair & Engelman, 1994). The extracellular domain has contact with the outer surface of the bilayer as, at low concentrations of glycophorin A, it lies as a ‘pancake’ at the aqueous/lipid interface (Ruppel et al , 1982). Nuclear magnetic resonance studies have shown that in this down or ‘D’ state, the effective lateral pressure of the glycophorin A dimer acting on the hydrocarbon chains of the adjacent lipids is reduced.…”

Section: Discussionmentioning

confidence: 99%

Glycophorin A‐mediated haemolysis of normal human erythrocytes: evidence for antigen aggregation in the pathogenesis of immune haemolysis

Brain¹,

Prevost²,

Pihl³

et al. 2002

Br J Haematol

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Summary. The inexplicable severity of anti‐Pr autoimmune haemolytic anaemia led us to test the hypothesis that the haemolysis was primarily due to a change in the function of glycophorin A, on which the Pr antigen is located. The lectins Maclura pomifera and wheat germ agglutinin that bind to glycophorin A induced the haemolysis of normal erythrocytes in vitro. Lectin binding led to an increase in erythrocyte membrane permeability to sodium and potassium, the former resulting in an influx of water and subsequent haemolysis. The response was glycophorin A specific as Concanavalin A, which binds to band 3, did not cause haemolysis and peanut agglutinin only did so after removal of erythrocyte sialic acid. The lectin‐induced cation leak was not mediated by activation of cation channels as the inhibitors, tetrodotoxin, amiloride and 4,4′ diisothiocyanate stilbene 2,2′disulphonate, had no effect, suggesting that the haemolysis was due to exacerbation of the inherent cation permeability of the erythrocyte membrane. A human IgAK anti‐Pr autoantibody and a mouse anti‐human glycophorin A antibody increased erythrocyte permeability to sodium. The role of glycophorin A in stabilizing and, upon aggregation, destabilizing the phospholipid bilayer is discussed. Our findings may help explain the severity of anti‐Pr autoimmune haemolytic anaemia and other pathophysiological changes in human erythrocytes.

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“…By lowering the temperature, the membrane fluidity decreases and counteracts protein incorporation efficiency. Moreover, Ruppel et al (1982) showed that lowering temperature (< 10°C) led to the exclusion of the glycophorin-lipid complex from the dimyristoylglycerophosphocholine bilayers.…”

Section: Discussionmentioning

confidence: 99%

Electropermeabilization mediates a stable insertion of glycophorin A with Chinese hamster ovary cell membranes

Ouagari

Benoist

Sixou

et al. 1994

European Journal of Biochemistry

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Electropulsation allowed us to incorporate glycophorin A, an integral membrane protein, into mammalian nucleated cell membranes (Chinese hamster ovary cells). The induction of stable protein association is effective only when the field intensity is higher than its threshold value, creating membrane permeabilization to small molecules. Under controlled conditions, cell viability was only slightly altered by this treatment. Pulse number and duration controlled both the number of modified cells and incorporated molecules. The phenomena was temperature dependent. An average of 5 X104 moleculeskell was bound. About 80% of cells in the pulsed population were observed to incorporate glycophorin. The protein incorporation was shown to be stable 48 h after electroassociation. Electrically bound proteins were shared between the cells after each division. As enhanced binding is detected if glycophorin is added after the pulses, it is the long-lived alteration of the membrane mediated by the pulses which supports the association.It is commonly accepted that the driving force for the spontaneous incorporation of proteins is hydrophobic effect. However, a number of other effects may support or counteract this hydrophobic effect. Generally, the free energy of protein incorporation includes four contributions which arise from a change of water structure, protein state, lipid state, bonds between protein and water or lipid molecules. Nevertheless, the central questions of how hydrophobic sequences would be transferred from an aqueous to an hydrophobic environment and how the polar regions of protein that span the membrane would be transferred across the hydrocarbon core of the bilayer, have not been emphasized. So, this makes it exceedingly unlikely that insertion of integral protein occurs directly across the lipid bilayer (Singer, 1990;Singer and Yaffe, 1990; Singer et al., 1987a, b). The membrane contribution, which has been neglected until now, necessarily appears important allowing the penetration of macromolecules with strongly polar segments. Thermodynamics of protein insertion in lipid systems imply the occurrence of the lipid matrix perturbation. Thus, protein incorporation thermodynamics ( J i m and Zakim, 1987;Jahnig, 1983) show a favourable contribution of electrostatic forces and hydrophobic forces which occur on the membrane-spanning sequence, whereas hydration forces (Pargesian and Rau, 1984) and hydrophobic forces which occur on the protein polar segments prevent incorporation. Spontaneous insertion takes place if the first component is stronger than the second one. Such a case would occur only if the membrane is in an 'excited' state.Electropulsation can create such an 'excited' state of the membrane. Recent studies reported the so-called 'electroinCorrespondence to J. Teissie,

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On the microstructure and phase diagram of dimyristoylphosphatidylcholine-glycophorin bilayers. The role of defects and the hydrophilic lipid-protein interaction

Cited by 56 publications

References 18 publications

Life‐threatening hemolytic anemia due to an autoanti‐Pr cold agglutinin: evidence that glycophorin A antibodies may induce lipid bilayer exposure and cation permeability independent of agglutination

Life‐threatening hemolytic anemia due to an autoanti‐Pr cold agglutinin: evidence that glycophorin A antibodies may induce lipid bilayer exposure and cation permeability independent of agglutination

Glycophorin A‐mediated haemolysis of normal human erythrocytes: evidence for antigen aggregation in the pathogenesis of immune haemolysis

Electropermeabilization mediates a stable insertion of glycophorin A with Chinese hamster ovary cell membranes

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