Affinity of hemoglobin for the cytoplasmic fragment of human erythrocyte membrane band 3

Chétrite, G.; Cassoly, Robert

doi:10.1016/0022-2836(85)90076-2

Cited by 92 publications

(39 citation statements)

References 23 publications

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“…1 and Table 1). In fact, this observation was in agreement with a competition of the phosphate ion for the same deoxy-Hb site responsible for the interaction with CDB3 [4,5]. This competition should decrease at acidic pH values, due to the phosphate protonation.…”

Section: Resultssupporting

confidence: 79%

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Human erythrocyte metabolism is modulated by the O₂‐linked transition of hemoglobin

et al. 1996

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The metabolic behaviour of human erythrocytes has been investigated with particular regard to the effect of their oxygenation state. Experiments performed at high phosphate concentration (80 mM) within the pH range 7.0-7.8 on erythrocytes at high (HOS) and low (LOS) oxygen saturation showed that at any pH value: (1) glucose consumption was independent of the oxygenation state; (2) pentose phosphate pathway (PPP) flux was about 2 times higher in the HOS than in the LOS state. At low phosphate concentration (1.0 mM) the PPP flux doubled in HOS as well as in LOS erythrocytes, whereas the decrease in glucose consumption was more marked in the HOS state. Metabolism of LOS erythrocytes approached that of HOS erythrocytes under the following conditions: (1) erythrocytes having band 3 modified by 4,4'-diisothiocyanatostilbene-2,2'-disulphonic acid; (2) CO-saturated erythrocytes. These data support the hypothesis of a modulation of the relative rates of PPP and glycolysis achieved through competition between deoxy-hemoglobin (deoxy-Hb) and glycolytic enzymes for the cytoplasmic domain of band 3.

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Section: Resultssupporting

confidence: 79%

“…Subsequently, Walder et al [4] and Chttrite and Cassoly [5] clearly demonstrated that deoxy-Hb displays a higher affinity for the cytoplasmic domain of band 3 (CDB3) than does oxy-*Corresponding author. Istituto di Chimica e Chimica Clinica, Facolt/t di Medicina e Chirurgia, Universitfi Cattolica, Largo F. Vito 1, 00168 Roma, Italy.…”

Section: Introductionmentioning

confidence: 99%

Human erythrocyte metabolism is modulated by the O₂‐linked transition of hemoglobin

et al. 1996

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“…Moreover, it is well known that AE1 is able to interact with hemoglobin by means of its binding to erythrocyte cytoskeleton. This binding is sensitive to hemoglobin oxygenation (33). The data associated with our results, which suggest a role of tAE1 in regulating other transport functioning, might provide an explanation of oxygen control of the KCl cotransporter as well as the Na ϩ /H ϩ exchanger in trout erythrocyte (34,35).…”

Section: Discussionsupporting

confidence: 65%

Evidence for Up-regulation of the Endogenous Na-K-2Cl Co-transporter by Molecular Interactions with the Anion Exchanger tAE1 Expressed in Xenopus Oocyte

Guizouarn

Gabillat

Borgèse

2004

Journal of Biological Chemistry

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Expression of trout anion exchanger 1 (tAE1) in Xenopus oocyte led to the stimulation of a Na ؉ -and Cl ؊ -dependent Rb influx. Functional features and pharmacological data strongly suggest that this Rb influx is mediated by the endogenous Na-K-2Cl (NKCC) co-transporter. The functional relationship between expression of tAE1 and activation of the NKCC co-transporter was investigated. Indeed, it was shown previously that tAE1 expressed in Xenopus oocyte induces a strong anion conductance which is correlated with an increased taurine permeability. Measurements of intracellular ion contents ruled out the involvement of any modification of known electrochemical parameters in NKCC co-transporter activation by tAE1. Furthermore, using chimera of tAE1 made with AE1 from other species unable to exhibit anion conductance led to the conclusion that there was no correlation between tAE1 anion conductance and NKCC co-transporter stimulation. Therefore, a possible molecular interaction between tAE1 and the NKCC co-transporter was investigated. Our results clearly show that NKCC activation is dependent upon the C-terminal part of tAE1. Chimeric constructions where tAE1 C-terminal part was substituted by the corresponding part of mouse AE1 abolished co-transporter activation. Moreover, steric encumbrance on the C-terminal end of tAE1 with a specific antibody or with a protein fusion also prevented the co-transporter activation. These data suggest a new role for some anion exchangers in controlling other transporter activity by molecular interactions.

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“…The fact that ionic strength profoundly influences the strength of the Hbactin and Hb-tubulin interaction does not necessarily rule out their existence in vivo. Millimolar concentrations of Hb, which prevail inside the cell, must contribute to the stability of a low-affinity complex as has been shown to be the case for Hb interacting with the negatively charged N-terminal end of band 3 [8,35]. The presence ofmassive amounts of competitive glycerate-2,3-P2 and ATP in the cytoplasm should certainly exclude a significant binding of Hb in the normal mature red blood cell.…”

Section: Discussionmentioning

confidence: 99%

“…Linkage of tubulin on activated Sepharose 4B (Pharmacia) was performed as described in [8] with the cytoplasmic fragment of the erythrocyte band 3 protein. Binding assays with Hb were carried out in the absence of oxygen as in [S] in 50 mM Mes (pH 6.4) buffer.…”

Section: Tubulinmentioning

confidence: 99%

Interactions of actin and tubulin with human deoxyhemoglobin

Lebbar

Stetzkowski‐Marden

Mauffret

et al. 1987

European Journal of Biochemistry

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Short actin filaments are an essential component of the red-cell membrane skeleton, and microtubules are also present in nucleated erythrocytes as a marginal band. Actin and tubulin share the property of possessing a very anionic terminal peptide. Since deoxyhemoglobin (Hb) is known to be a strong polyanion-binding protein, we have considered how it may interact with actin and tubulin within the intact cell. Here we demonstrate that actin and tubulin form in vitro a high-affinity complex with Hb. This is shown by measuring, by stopped-flow experiments, the decrease of the binding rate constant of CO to Hb in the presence of increasing amounts of actin and tubulin. One tetramer of Hb is bound by an actin monomer, and about two tetramers by an a$-tubulin heterodimer. Binding assays in batch experiments with immobilized tubulin give the same stoichiometry. Formation of the complexes involves the 2,3-bisphosphoglycerate-binding site of Hb and a negatively charged domain, most likely the highly acidic N and C-terminal peptides of actin and tubulin. In addition to providing new opportunities to study the structural and functional properties of actin and tubulin, these results support the idea that in the case of partial metabolic depletion of bisphosphoglycerate and ATP in erythrocytes, Hb may interact with oligomeric actin and tubulin present in the cytoskeleton.Human deoxyhemoglobin (Hb) is certainly one of the bestcharacterized polyanion-binding proteins [l, 21, considering the role of 2,3-bisphosphoglycerate (glycerate-2,3-P2) as the natural effector of its oxygen affinity [3]. X-ray analyses have given explicit details on the interaction between glycerate-2,3-P2 and the cationic amino acid residues involved in the /? chain of the Hb tetramer [2]. In the red cells of the venous blood massive amounts of fully or partially deoxygenated hemoglobin are engaged, in competition with other cationic molecules, in multiple equilibria with several anions, in addition to the millimolar amounts of glycerate-2,3-P2 [4, 51. Some of these polyanions may be localized in the vicinity of the plasmic membrane as suggested by recent evidence indicating that Hb binds within erythrocytes with the highly acidic N-terminus Met-Glu-Glu-Leu-Gln-Asp-Asp-Tyr-GluAsp-Asp-of the cytoplasmic domain of band 3, the aniontransport protein of the erythrocyte membrane [6 -81 (for review see [9]). The red cell membrane skeleton contains short actin filaments (protofilaments) interconnected with spectrin tetramers to constitute a flexible meshwork of proteins underlying the plasmic membrane [lo]. This structure is further reinforced in the nucleated erytrocyte with the presence of a marginal band constituted of a bundle of microtubules [l 11. Actin and tubulin are known to possess, as band 3, a very acidic N and C-terminal peptide invariably represented by a combination of aspartic and glutamic residues. This sequence for muscle actin is Asp-Glu-Asp-Glu-and it is -Glu-Glu-GluGly-Glu-Glu-(Tyr) and -Glu-Glu-Glu-Gly-Glu-Glu-Asp-Glu- In erythrocytes they c...

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Affinity of hemoglobin for the cytoplasmic fragment of human erythrocyte membrane band 3

Cited by 92 publications

References 23 publications

Human erythrocyte metabolism is modulated by the O₂‐linked transition of hemoglobin

Human erythrocyte metabolism is modulated by the O₂‐linked transition of hemoglobin

Evidence for Up-regulation of the Endogenous Na-K-2Cl Co-transporter by Molecular Interactions with the Anion Exchanger tAE1 Expressed in Xenopus Oocyte

Interactions of actin and tubulin with human deoxyhemoglobin

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Affinity of hemoglobin for the cytoplasmic fragment of human erythrocyte membrane band 3

Cited by 92 publications

References 23 publications

Human erythrocyte metabolism is modulated by the O2‐linked transition of hemoglobin

Human erythrocyte metabolism is modulated by the O2‐linked transition of hemoglobin

Evidence for Up-regulation of the Endogenous Na-K-2Cl Co-transporter by Molecular Interactions with the Anion Exchanger tAE1 Expressed in Xenopus Oocyte

Interactions of actin and tubulin with human deoxyhemoglobin

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Human erythrocyte metabolism is modulated by the O₂‐linked transition of hemoglobin

Human erythrocyte metabolism is modulated by the O₂‐linked transition of hemoglobin