Regulation of linkages between the erythrocyte membrane and its skeleton by 2,3-diphosphoglycerate

Moriyama, Ryuichi; Lombardo, Christian R.; Workman, Ryan F.; Low, Philip S.

doi:10.1016/s0021-9258(18)82083-x

Cited by 45 publications

(5 citation statements)

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“…WGA lectin binding to the sugar moiety did not affect fluorescein motion in the intramembrane domain of band 3, consistent with the observation that endoglycosidase digestion of the sugar on band 3 did not affect band 3 function (Casey et al, 1992). Similarly, changes in the conformation of cdb3 induced by increasing pH in the range 8-10 (Low et al, 1988) and 2,3-DPG binding (Moriyama et al, 1993) had little effect on the fluorescence anisotropy decay. These results are consistent with the finding that cleavage of cdb3 does not affect band 3-mediated anion transport (Lepke et al, 1992), and support the functional independence of the intramembrane domain of band 3.…”

Section: Discussionsupporting

confidence: 73%

Anisotropy Decay Measurement of Segmental Dynamics of the Anion Binding Domain in Erythrocyte Band 3

Bicknese

Rossi²,

Thevenin³

et al. 1995

Biochemistry

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Time-resolved anisotropy was utilized to detect nanosecond segmental motions of the band 3 intramembrane domain. Band 3 at lysine 430 was fluorescently labeled in ghost membranes by fluorescein or eosin maleimide treatment of intact human erythrocytes followed by hypotonic lysis. Single lifetimes for fluorescein (3.8-4.1 ns) and eosin (3.2-3.4 ns) were observed. Phase-modulation measurement of anisotropy decay indicated a segmental motion model, r(t) = exp(-t/tau 1c)[r infinity + (ro-r infinity) exp(-t/tau 2c)], defined by rotational correlation times corresponding to band 3 segmental motion (tau 1c, 30-70 ns) and rapid fluorescein motion in its binding pocket (tau 2c, 200-400 ps), and a residual anisotropy (r infinity, 0.23-0.28) describing hindered fluorescein motion. In PBS at pH 7.4, tau 1c, tau 2c, and r infinity were 44 ns, 307 ps, and 0.24, respectively, predicting a steady-state anisotropy of 0.24, in agreement with the measured value of 0.23. Factors that might influence band 3 structure/dynamics were examined. Whereas pH (range 5-10) had little effect on r(t), [NaCl] addition (0-150 mM) remarkably decreased tau 1c from 68 to 44 ns. The decrease in tau 1c correlated with solution ionic strength, and did not depend on osmolality (studied by mannitol addition), or specific anion interactions (comparing Cl, Br, F, SO4, citrate). The ionic strength effect was not observed in fluorescein-labeled carbonic anhydrase and trypsin-cleaved band 3, suggesting a specific effect on intact band 3. Anisotropy decay was relatively insensitive to external lectin or internal 2,3-DPG binding, but was sensitive to temperature, membrane fluidity, urea denaturation, fluid-phase viscosity, and aldehyde fixation.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionsupporting

confidence: 73%

Anisotropy Decay Measurement of Segmental Dynamics of the Anion Binding Domain in Erythrocyte Band 3

Bicknese

Rossi²,

Thevenin³

et al. 1995

Biochemistry

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“…EleVation of Intracellular 2,3-Diphosphoglycerate LeVels. Linkages between the erythrocyte membrane and its skeleton are affected by intracellular DPG (Moriyama et al, 1993). At higher than normal levels, DPG increases the lateral diffusion of integral membrane proteins, dissociates spectrin-actin-band 4.1 complexes, and decreases the number of attachments between the skeleton and the membrane (Schindler et al, 1980;Sheetz & Casaly, 1980).…”

Section: Resultsmentioning

confidence: 99%

Physical Determinants of Intermembrane Protein Transfer

Waters¹,

Sen²,

Brunauer³

et al. 1996

Biochemistry

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Intermembrane protein transfer between erythrocytes and phospholipid vesicles was examined under a variety of conditions to investigate physical factors governing this process. Human erythrocytes were incubated with sonicated dimyristoylphosphatidylcholine vesicles containing trace [14C]dipalmitoylphosphatidylcholine. Protein-vesicle complexes were separated from cells and from membrane fragments by density gradient centrifugation. The yield of isolated protein vesicles was determined from the 14C-vesicle marker; protein compositions were analyzed by SDS-polyacrylamide gel electrophoresis. Enzymatic removal of portions of the cytoplasmic or exoplasmic domains of cell membrane proteins had little effect on the extent of protein transfer. Membrane additives such as cholate produced a 2-fold increase in protein-vesicle yield. The selectivity of protein transfer from erythrocytes was influenced by the lipid composition of recipient vesicles: inclusion of cholesterol increased band 3 content while the presence of anionic phospholipids reduced transfer. Proteins transferred from 32P-labeled cells differed in specific radioactivity from bulk cell proteins: glycophorin, highly phosphorylated in the cell membrane, showed no detectable labeling in the corresponding protein-vesicle band. These observations suggest that cell-to-vesicle protein transfer is insensitive to bulk steric and electrostatic properties of cell membranes, but enhanced by membrane defects. Recipient membrane composition influences the selectivity of transferred proteins and may reveal subtle differences in the membrane association of protein subpopulations.

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“…These dimers have renal toxicity. Furthermore, in the intact cell, the effect of 2,3-BPG on O 2 delivery seems to be related to its modulation of the mechanical properties of the erythrocyte membrane, besides its well known impact on hemoglobin-O 2 affinity [20]. Even with the required cofactor (2,3-BPG), human hemoglobin, cannot readily release oxygen as required when outside red blood cells.…”

Section: Discussionmentioning

confidence: 99%

Preservation of myocardial energy status by bovine hemoglobin solutions during ischemia

Carlucci

Miraldi

Barretta

et al. 2002

Biomedicine & Pharmacotherapy

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Regulation of linkages between the erythrocyte membrane and its skeleton by 2,3-diphosphoglycerate

Cited by 45 publications

References 0 publications

Anisotropy Decay Measurement of Segmental Dynamics of the Anion Binding Domain in Erythrocyte Band 3

Anisotropy Decay Measurement of Segmental Dynamics of the Anion Binding Domain in Erythrocyte Band 3

Physical Determinants of Intermembrane Protein Transfer

Preservation of myocardial energy status by bovine hemoglobin solutions during ischemia

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