Regulation of glycolysis via reversible enzyme binding to the membrane protein, band 3

Low, Philip S.; Rathinavelu, Prema; Harrison, Marietta L.

doi:10.1016/s0021-9258(18)82379-1

Cited by 153 publications

(39 citation statements)

References 29 publications

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“…Further disruption of the cdB3 metabolon and EMP/HMP fluxes could be explained by the progressive oxidation of cdB3 interacting partners at functional residues, such as C152 and 156 (and H179) in the active site of GAPDH 33 and C93 of the hemoglobin beta chain. 60 All of these events are known to impact cdB3 conformation/clustering and impair normal protein complex assembly at Band3, 48,84,85 which would be expected to reduce both the baseline and dynamic range in HMP flux and consequently, depower NADPH and GSH recycling during oxidant loading (as we observed).…”

Section: Discussionmentioning

confidence: 57%

“…Such loss would be consistent with disruption of the cdB3-based O 2 dependent glycolytic metabolon assembly we observed by imaging of the intracellular location of the key EMP enzyme GAPDH (enzyme at the EMP/HMP confluence, Figure 1) in healthy control and stored RBCs. O 2 dependent GAPDH shuttling between the RBC membrane and cytoplasm, normally observed in uninjured RBCs, 3,44,48 was lost in stored RBCs (Figure 6(C)). Specifically, stored RBCs demonstrated failure of GAPDH membrane sequestration in oxygenated RBCs, which is associated with constraint in HMP dynamic range (Figure 1).…”

Section: Analysis Of Band 3 (Cdb3) and Gapdh Bindingmentioning

confidence: 86%

“…Specifically, stored RBCs demonstrated failure of GAPDH membrane sequestration in oxygenated RBCs, which is associated with constraint in HMP dynamic range (Figure 1). 3,44,48 3.8 | GAPDH binding GAPDH binding capacity was determined for membrane isolated at each storage week. Since membrane density (wt/vol) varies as a function of storage duration, we normalized membrane surface area across storage weeks by utilizing a membrane on bead model and standardizing bead # (6 × 10 8 ) between experiments.…”

Section: Analysis Of Band 3 (Cdb3) and Gapdh Bindingmentioning

confidence: 99%

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Quantifying dynamic range in red blood cell energetics: Evidence of progressive energy failure during storage

Rogers

Brummet

et al. 2021

Transfusion

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Background During storage, red blood cells (RBCs) undergo significant biochemical and morphologic changes, referred to collectively as the “storage lesion”. It was hypothesized that these defects may arise from disrupted oxygen‐based regulation of RBC energy metabolism, with resultant depowering of intrinsic antioxidant systems. Study Design and Methods As a function of storage duration, the dynamic range in RBC metabolic response to three models of biochemical oxidant stress (methylene blue, hypoxanthine/xanthine oxidase, and diamide) was assessed, comparing glycolytic flux by NMR and UHPLC–MS methodologies. Blood was processed/stored under standard conditions (AS‐1 additive solution) with leukoreduction. Over a 6‐week period, RBC metabolic and antioxidant status were assessed at baseline and following exposure to the three biochemical oxidant models. Comparison was made of glycolytic flux (1H‐NMR tracking of [2‐13C]‐glucose and metabolomic phenotyping with [1,2,3‐13C3] glucose), reducing equivalent (NADPH/NADP+) recycling, and thiol‐based (GSH/GSSG) antioxidant status. Results As a function of storage duration, we observed the following: (1) a reduction in baseline hexose monophosphate pathway (HMP) flux, the sole pathway responsible for the regeneration of the essential reducing equivalent NADPH; with (2) diminished stress‐based dynamic range in both overall glycolytic as well as proportional HMP flux. In addition, progressive with storage duration, RBCs showed (3) constraint in reducing equivalent (NADPH) recycling capacity, (4) loss of thiol based (GSH) recycling capacity, and (5) dysregulation of metabolon assembly at the cytoplasmic domain of Band 3 membrane protein (cdB3). Conclusion Blood storage disturbs normal RBC metabolic control, depowering antioxidant capacity and enhancing vulnerability to oxidative injury.

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Section: Discussionmentioning

confidence: 57%

Section: Analysis Of Band 3 (Cdb3) and Gapdh Bindingmentioning

confidence: 86%

Section: Analysis Of Band 3 (Cdb3) and Gapdh Bindingmentioning

confidence: 99%

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Quantifying dynamic range in red blood cell energetics: Evidence of progressive energy failure during storage

Rogers

Brummet

et al. 2021

Transfusion

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“…The prolonged existence of this superoxide radical increases the probability of forming hydroxyl radicals via the Fenton reaction [67]. Hydroxyl radicals generate a cascade of radical species that target and damage membrane phospholipids and associated cell proteins that maintain cell functionality and structure [68][69][70][71]. RBCs begin the removal of the damaged membrane via vesiculation, shipping toxic byproducts out of the cell and into the supernatant in microvesicles [72][73][74][75].…”

Section: Rbc Storage Lesion: Definitionmentioning

confidence: 99%

Application of image flow cytometry and photoacoustics for the characterization of red blood cell storage lesions

Pinto¹

2021

Preprint

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Significant functional/structural changes of red blood cells (RBCs) have been documented during its in vitro storage. Collectively termed as RBC storage lesions, changes include an increase in RBC oxygen saturation (SO2) and an increase in irreversibly damaged RBCs (spheroechinocytes). In this work, novel optical techniques are presented for determining the spheroechinocyte population as a function of storage time via automated image flow cytometry (IFC) morphology characterization, and the acquisition of RBC SO2 via an in situ photoacoustic (PA) method. Blood gas analysis (BGA) was used as the gold standard SO2 measure. Over the lifespan of seven blood bags, the IFC spheroechinocyte population – PA SO2 correlation was found to be strong (0.600.95) shows high potential for in situ monitoring of RBC storage lesions.

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“…The N-terminus of Band3 allows RBCs to modify their metabolism and function in response to the oxygen saturation of hemoglobin. [39][40][41] We acquired three strains of previously reported mice in which the Nterminus of the endogenous murine Band3 was replaced with either the canonical or mutated N-terminus of human Band3. All mice were reported as having been backcrossed to a B6 background.…”

Section: Introductionmentioning

confidence: 99%

Mouse background genetics in biomedical research: The devil's in the details

et al. 2021

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Background: Genetically modified mice are used widely to explore mechanisms in most biomedical fields-including transfusion. Concluding that a gene modification is responsible for a phenotypic change assumes no other differences between the gene-modified and wild-type mice besides the targetted gene. Study Design and Methods:To test the hypothesis that the N-terminus of Band3, which regulates metabolism, affects RBC storage biology, RBCs from mice with a modified N-terminus of Band3 were stored under simulated blood bank conditions. All strains of mice were generated with the same initial embryonic stem cells from 129 mice and each strain was backcrossed with C57BL/6 (B6) mice. Both 24-h recoveries post-transfusion and metabolomics were determined for stored RBCs. Genetic profiles of mice were assessed by a high-resolution SNP array.Results: RBCs from mice with a mutated Band3 N-terminus had increased lipid oxidation and worse 24-h recoveries, "demonstrating" that Band3 regu-

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Regulation of glycolysis via reversible enzyme binding to the membrane protein, band 3

Cited by 153 publications

References 29 publications

Quantifying dynamic range in red blood cell energetics: Evidence of progressive energy failure during storage

Quantifying dynamic range in red blood cell energetics: Evidence of progressive energy failure during storage

Application of image flow cytometry and photoacoustics for the characterization of red blood cell storage lesions

Mouse background genetics in biomedical research: The devil's in the details

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