Effect of haemoglobin on liposome permeability to Rb+ and other solutes

Calissano, Pietro; Alemà, Stefano; Rusca, Graziella

doi:10.1016/0005-2736(72)90414-2

Cited by 26 publications

(5 citation statements)

References 6 publications

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“…Sickling results in membrane leaks of monovalent cations (18) and calcium accumulation in the sickled cells (19), which exhibit decreased deformability (20). Some ofthese membrane effects are mimicked in model lipid membranes in which Hb A has been intercalated (21)(22)(23). Our present studies suggest that the initial event in sickling may be the irreversible binding ofdeoxyHb S to erythrocyte membranes.…”

Section: Discussionmentioning

confidence: 73%

Interaction of sickle cell hemoglobin with erythrocyte membranes.

Shaklai¹,

Sharma²,

Ranney³

1981

Proc. Natl. Acad. Sci. U.S.A.

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The interactions ofhemoglobin S with the erythrocyte membrane were compared with the corresponding interactions of hemoglobin A by measuring in both steady-state and kinetic experiments the quenching of the fluorescence of a probe embedded in erythrocyte membranes. Whereas hemoglobin A could be dissociated from membranes, a fraction of hemoglobin S was irreversibly bound even in the oxy state. Deoxyhemoglobin S interacted much more strongly with erythrocyte membranes than did deoxyhemoglobin A: a portion of the deoxyhemoglobin S was irreversibly bound, and the reversibly bound fraction ofhemoglobin S dissociated more slowly than did deoxyhemoglobin A. It is suggested that the binding of deoxyhemoglobin S is a two-step reaction in which the first step involves electrostatic interaction with band III erythrocyte membrane protein and the second step involves a hydrophobic interaction with membrane lipids. The latter reaction reflects the greater hydrophobicity ofhemoglobin S. The unique interaction of hemoglobin S with erythrocyte membranes may be important in the formation of irreversibly siclded cells.The decreased erythrocyte flexibility observed in sickled cells reflects changes in the erythrocyte membrane (1). In some cells, irreversible sickling takes place and the erythrocyte does not resume the normal shape on exposure to oxygen. The changes in membrane structure that are responsible for irreversible sickling have not been defined, although loss of sialic acid (2) and possible alterations in membrane proteins (3) have been described, and an increase in membrane-bound hemoglobin has been noted in erythrocytes ofindividuals with sickle cell anemia (4). The erythrocyte membranes ofpatients with sickle cell anemia are initially normal, although they may undergo secondary structural changes as a result of sickle-unsickle cycles. Our observations of the effects of sickle-cell hemoglobin (Hb S) on erythrocyte membranes prepared from normal individuals were designed to ascertain whether the interactions ofHb S with normal erythrocyte membranes differed from such interactions of normal human hemoglobin A (Hb A). Shaklai and Abrahami (5) utilized similar techniques for studies of the interactions of deoxy Hb A, which showed a lower affinity of the unliganded hemoglobin for erythrocyte membranes. The mutational change (normal (36 glutamic acid is replaced by valine) that characterizes Hb S results in a greater positive charge (higher isoelectric point) and greater surface hydrophobicity (6) than in Hb A. Hb A2, the minor basic component of hemoglobin obtained from normal adults, has a higher isoelectric point than does Hb S, but does not share its greater surface hydrophobicity. In the present studies, the interactions ofthese three hemoglobins with erythrocyte membranes were compared in steady-state and kinetic observations. MATERIALS AND METHODSAll chemicals used were reagent grade. Anthroyl stearic acid was a product of Molecular Probes (Plano, TX); glyceraldehyde-3-phosphate dehydrogenase was purchased fr...

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Section: Discussionmentioning

confidence: 73%

Interaction of sickle cell hemoglobin with erythrocyte membranes.

Shaklai¹,

Sharma²,

Ranney³

1981

Proc. Natl. Acad. Sci. U.S.A.

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“…The latter effect presumably requires a particular type of interaction. It is noteworthy to mention that other proteins (Kimelberg and Papahadjopoulos, 1971b;Calissano et al, 1972b), including the brain-specific protein 14-3-2 (Calissano and Bangham, 1971), affect liposome permeability. The link between Ca2+, S-100 and a lipid membrane described in this study, however, appears to be specific and quite unique for the effects observed (leak experiments) and the mechanism possibly underlying such effects (binding experiments).…”

Section: Discussionmentioning

confidence: 99%

Interaction of S-100 protein with cations and liposomes

Calissano¹,

Alemà²,

Fasella³

1974

Biochemistry

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The interaction of the brain-specific protein S-100 with Ca2+, K+, and artificial lipid membranes (liposomes) was studied. The protein S-100 has two sets of Ca2+ binding sites with dissociation constants which, in 60 mM Tris-HCl buffer (pH 7.6 and 22°), are, respectively, =¡5 X 10-5 and 1 X 10~3 M. In the presence of K+ the binding of Ca2+ to the high affinity sites induces a conformational change which causes an increase of the protein intrinsic fluorescence and makes the protein capable of interacting with

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“…lIb 177 loss from about 30 to about 40% per hour, but there is no detectable effect on the 60% per hour loss of glucose (Calissano, Alema and Rusca, 1972) .…”

Section: Hb-lipid Interactions -Comparison To Rbc'smentioning

confidence: 88%

“…Kjmelberg and Papahadjopoulos (1971a) showed that proteins that could penetrate phosphat idyl serine mono layers (Kimelberg and Papahadjopoulos, 1971b;Papahadjopoulos, Cowden and Kimelberg, 1973) but do not increase the glucose permeability (Gould and London, 1972;Calissano, Alema and Rusca, 1972), whereas unfolded bovine serum albumin (pH < 5.5) (Sweet and Zull, 1969), some RBC membrane proteins (Sweet and Zull, 1970;Lidgard and Jones, 1975) and the central nervous system basic Al protein (Gould and London, 1972) do increase glucose permeability.…”

Section: Protein-liposome Interactions Permeabilitymentioning

confidence: 99%

Molecular sieving action of the cell membrane during gradual osmotic hemolysis

MacGregor¹

1977

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Effect of haemoglobin on liposome permeability to Rb+ and other solutes

Cited by 26 publications

References 6 publications

Interaction of sickle cell hemoglobin with erythrocyte membranes.

Interaction of sickle cell hemoglobin with erythrocyte membranes.

Interaction of S-100 protein with cations and liposomes

Molecular sieving action of the cell membrane during gradual osmotic hemolysis

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