Response of the glycolysis of human erythrocytes to the transition from the oxygenated to the deoxygenated state at constant intracellular pH

Rapoport, Iris; Berger, H.; Rapoport, S.; Elsner, R; Gerber, Gerhard

doi:10.1016/0304-4165(76)90120-3

Cited by 27 publications

(18 citation statements)

References 19 publications

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“…Moreover, Hamasaki et al [2] showed that lactate production and the Embden-Meyerhof pathway (EMP) increased upon erythrocyte deoxygenation. These observations were subsequently confirmed under strict pH control by Rapoport et al [3]. This unexpected Pasteur effect of human erythrocytes, which are cells without a nucleus and mitochondria, was attributed to complex changes in the activity of various ions, metabolites and cofactors, originating from the higher affinity of deoxy-hemoglobin (deoxy-Hb), as compared to oxy-Hb, for heterotropic effectors, i.e.…”

Section: Introductionmentioning

confidence: 69%

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: Introductionmentioning

confidence: 69%

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

et al. 1996

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“…Taking into account these features, researchers have hypothesized that RBCs have appropriate mechanisms for responding quickly to hypoxia to upregulate de novo ATP synthesis and glycolytic flux, leading to the increase in 2,3-BPG. Historically, the hypoxic acceleration of glycolysis in RBCs was thought to be induced by alterations in pH or the metabolic compensation of ATP [47, 48]. However, recent evidence from studies with intact RBCs has shown that T-state hemoglobin triggers an increase in the activities of glycolytic enzymes that interact with band 3 and plays a central role in acceleration of glucose consumption to increase the synthesis of ATP and 2,3-BPG [49].…”

Section: Metabolic Model Of Human Rbcs Using the E-cell Systemmentioning

confidence: 99%

A Metabolic Model of Human Erythrocytes: Practical Application of the E-Cell Simulation Environment

Yachie‐Kinoshita

Nishino

Shimo

et al. 2010

Journal of Biomedicine and Biotechnology

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The human red blood cell (RBC) has long been used for modeling of complex biological networks, for elucidation of a wide variety of dynamic phenomena, and for understanding the fundamental topology of metabolic pathways. Here, we introduce our recent work on an RBC metabolic model using the E-Cell Simulation Environment. The model is sufficiently detailed to predict the temporal hypoxic response of each metabolite and, at the same time, successfully integrates modulation of metabolism and of the oxygen transporting capacity of hemoglobin. The model includes the mechanisms of RBC maintenance as a single cell system and the functioning of RBCs as components of a higher order system. Modeling of RBC metabolism is now approaching a fully mature stage of realistic predictions at the molecular level and will be useful for predicting conditions in biotechnological applications such as long-term cold storage of RBCs.

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“…1). Thus, upon Hb deoxygenation, glycolysis accelerates [37][38][39][40]. Indeed, hypoxia induces release of ATP from RBCs due to the activation of glycolysis following deoxyHb binding to cdB3 [41].…”

Section: +mentioning

confidence: 99%

Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

Barvitenko

Adragna

Weber³

2005

Cell Physiol Biochem

135

104

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Erythrocytes play a key role in human and vertebrate metabolism. Tissue O₂ supply is regulated by both hemoglobin (Hb)-O₂ affinity and erythrocyte rheology, a key determinant of tissue perfusion. Oxygenation-deoxygenation transitions of Hb may lead to re-organization of the cytoskeleton and signalling pathways activation/deactivation in an O₂-dependent manner. Deoxygenated Hb binds to the cytoplasmic domain of the anion exchanger band 3, which is anchored to the cytoskeleton, and is considered a major mechanism underlying the oxygenation-dependence of several erythrocyte functions. This work discusses the multiple modes of Hb-cytoskeleton interactions. In addition, it reviews the effects of Mg²⁺, 2,3-diphosphoglycerate, NO, shear stress and Ca²⁺, all factors accompanying the oxygenation-deoxygenation cycle in circulating red cells. Due to the extensive literature on the subject, the data discussed here, pertain mainly to human erythrocytes whose O₂ affinity is modulated by 2,3-diphosphoglycerate, ectothermic vertebrate erythrocytes that use ATP, and to bird erythrocytes that use inositol pentaphosphate.

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Response of the glycolysis of human erythrocytes to the transition from the oxygenated to the deoxygenated state at constant intracellular pH

Cited by 27 publications

References 19 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

A Metabolic Model of Human Erythrocytes: Practical Application of the E-Cell Simulation Environment

Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

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Response of the glycolysis of human erythrocytes to the transition from the oxygenated to the deoxygenated state at constant intracellular pH

Cited by 27 publications

References 19 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

A Metabolic Model of Human Erythrocytes: Practical Application of the E-Cell Simulation Environment

Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

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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