Quantitative analysis of the association of human hemoglobin with the cytoplasmic fragment of band 3 protein.

Cassoly, Robert

doi:10.1016/s0021-9258(18)32746-7

Cited by 48 publications

(24 citation statements)

References 18 publications

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“…1985 American Chemical Society hemoglobin (Cassoly, 1983). Recently, the electron density map of a cocrystal of deoxyhemoglobin and an acidic N-terminal fragment of the cytoplasmic domain of band 3 has been obtained, and the derived three-dimensional structure demonstrates that the band 3 peptide inserts into the 2,3-diphosphoglycerate binding cavity of Hb (Walder et al, 1984).…”

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confidence: 99%

Hemichrome binding to band 3: nucleation of Heinz bodies on the erythrocyte membrane

Waugh¹

1985

Biochemistry

180

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Hemichromes, the precursors of red cell Heinz bodies, were prepared by treatment of native hemoglobin with phenylhydrazine, and their interaction with the cytoplasmic surface of the human erythrocyte membrane was studied. Binding of hemichromes to leaky red cell ghosts was found to be biphasic, exhibiting both high-affinity and low-affinity sites. The high-affinity sites were shown to be located on the cytoplasmic domain of band 3, since (i) glyceraldehyde-3-phosphate dehydrogenase, a known ligand of band 3, competes with the hemichromes for their binding sites, (ii) removal of the cytoplasmic domain of band 3 by proteolytic cleavage causes loss of the high-affinity sites, and (iii) the isolated cytoplasmic domain of band 3 interacts tightly with hemichromes, rapidly forming a pH-dependent, water-insoluble copolymer upon mixing in aqueous solution. Since the copolymer of hemichromes with the cytoplasmic domain of band 3 was readily isolatable, a partial characterization of its properties was conducted. The copolymer was shown to be of defined stoichiometry, containing approximately 2.5 hemichrome tetramers (or approximately 5 hemichrome dimers) per band 3 dimer, regardless of the ratio of hemichrome:band 3 in the initial reaction solution. The copolymer was found to be of macroscopic dimensions, generating particles which could be easily visualized without use of a microscope. The coprecipitation was also highly selective for hemichromes, since, in mixed solutions with native hemoglobin, only hemichrome was observed in the isolated pellet. Furthermore, no precipitate was ever observed upon mixing the cytoplasmic domain of band 3 with oxyhemoglobin, deoxyhemoglobin, (carbonmonoxy) hemoglobin, or methemoglobin.(ABSTRACT TRUNCATED AT 250 WORDS)

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confidence: 99%

Hemichrome binding to band 3: nucleation of Heinz bodies on the erythrocyte membrane

Waugh¹

1985

Biochemistry

180

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“…While the present work was in progress, quantitative analysis of the association of hemoglobin with an isolated segment of band 3 protein was reported (Cassoly, 1983); also, Walder et al (1984) reported the interaction of hemoglobin with the synthetic peptide corresponding to the first 11 residues of band 3 and with the entire 43-kilodalton cytoplasmic domain of the protein.…”

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confidence: 77%

“…The present studies differ from this as well as the previous studies (Shaklai et al, 1977;Salhany et al, 1980Salhany et al, , 1981 which have used unsealed ghost preparations in that the band 3 preparation as a whole (as inside-out vesicles, with all the lipids of the erythrocyte membrane intact) has been used. Further, Cassoly's paper (Cassoly, 1983) does not shed light on the interaction with the lipids.…”

Section: Discussionmentioning

confidence: 99%

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Interaction of hemoglobin and its component .alpha. and .beta. chains with band 3 protein

Premachandra¹

1986

Biochemistry

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The equilibrium binding of hemoglobin to isolated band 3 protein exhibited positive cooperativity [Hill coefficient = 1.65 +/- 0.1; total number of binding sites at pH 6.6 in 5 mM sodium phosphate buffer = 32 500 +/- 940 pmol/mg; Ka = (3.0 +/- 0.5) X 10(5) M-1]. The binding was reversible and ionic in nature as the bound hemoglobin was readily displaced by KCl, ATP, and 2,3-diphosphoglycerate, the latter two being more effective than KCl on a molar basis. The ratio of the interaction of hemoglobin to band 3 protein per se was 1:1, whereas the band 3 preparation as a whole (protein + lipids) was 3:1. Saturating levels of glyceraldehyde-3-phosphate dehydrogenase blocked only 33% of the total binding sites which were localized at the cytoplasmic segment; the remaining 67% was localized in lipids by their extraction with acetone. Reconstitution of acetone-extracted band 3 with phospholipid liposomes indicated phosphatidylserine as the binding site. The positive cooperativity in binding to acetone-extracted band 3 was increased (Hill constant = 2.1 +/- 0.1) compared to the band 3 preparation. After separation of the alpha and beta chains of hemoglobin, only the alpha chain binds to band 3 with positive cooperativity to an extent of 45-50% of native hemoglobin with similar affinity. The binding capacity of p-(hydroxymercuri)benzoate (HMB) derivatives of hemoglobin and its alpha chain was less than that of native hemoglobin, whereas HMB-beta chain or beta chain did not bind.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…Third, during RBC deoxygenation, deoxyHb binds band 3, and band 3-ankyrin dissociation starts to occur. The kinetics of deoxyHbband 3 binding is fast [the on-rate k on and binding constant K A are on the order of 10 6 /M s (41) and 10 6 /M (26,42), respectively], whereas the band 3-ankyrin dissociation is very slow [the off-rate k off and dissociation constant K d are on the order of 10 −3 /s (43) and 10 −8 M (44,45), respectively]. Thus, if the observed critical t total represents these three kinetic processes, then band 3-ankyrin dissociation will be the rate-limiting step and likely accounts for the critical t total .…”

Section: Discussionmentioning

confidence: 99%

Oxygen tension–mediated erythrocyte membrane interactions regulate cerebral capillary hyperemia

et al. 2019

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The tight coupling between cerebral blood flow and neural activity is a key feature of normal brain function and forms the basis of functional hyperemia. The mechanisms coupling neural activity to vascular responses, however, remain elusive despite decades of research. Recent studies have shown that cerebral functional hyperemia begins in capillaries, and red blood cells (RBCs) act as autonomous regulators of brain capillary perfusion. RBCs then respond to local changes of oxygen tension (PO2) and regulate their capillary velocity. Using ex vivo microfluidics and in vivo two-photon microscopy, we examined RBC capillary velocity as a function ofPO2and showed that deoxygenated hemoglobin and band 3 interactions on RBC membrane are the molecular switch that responds to localPO2changes and controls RBC capillary velocity. Capillary hyperemia can be controlled by manipulating RBC properties independent of the neurovascular unit, providing an effective strategy to treat or prevent impaired functional hyperemia.

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Quantitative analysis of the association of human hemoglobin with the cytoplasmic fragment of band 3 protein.

Cited by 48 publications

References 18 publications

Hemichrome binding to band 3: nucleation of Heinz bodies on the erythrocyte membrane

Hemichrome binding to band 3: nucleation of Heinz bodies on the erythrocyte membrane

Interaction of hemoglobin and its component .alpha. and .beta. chains with band 3 protein

Oxygen tension–mediated erythrocyte membrane interactions regulate cerebral capillary hyperemia

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