Erythrocyte Metabolism. V. Levels of Glycolytic Enzymes and Regulation of Glycolysis*

Chapman, Robert; Hennessey, M. A.; Waltersdorph, A M; Huennekens, F.M.; Gabrio, Beverly Wescott

doi:10.1172/jci104587

Cited by 136 publications

(48 citation statements)

References 25 publications

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“…The reaction catalysed by hexokinase is one of the rate-limiting steps in glucose metabolism, and the control is exerted through activation (Pi) or inhibition (glucose-6-phosphate) of the reaction (Rose & O'Connell, 1964). The glucose consumption of fresh cells is raised by Pi as is the consumption of nucleosides (Chapman, Hennessey, Waltersdorph, Huennekens & Gabrio, 1962;Tsuboi & Fukunaga, 1965; Minakami, Kakinuma & Yoshikawa, 1964;Rizzo & Eckel, 1966). Intracellular Pi acts by relieving the inhibition of the hexokinase reaction by glucose-6-phosphate (Rose, Warms & O'Connell, 1964), and also causes a fall in the concentration of glucose-6-phosphate (Rizzo & Eckel, 1966).…”

Section: Metabolism Of Nucleosides and Glucosementioning

confidence: 99%

Potassium transport and nucleoside metabolism in human red cells

Whittam¹,

Wiley²

1967

The Journal of Physiology

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SUMMARY1. A study has been made of active cation transport in relation to the metabolism of nucleosides and deoxynucleosides in human red blood cells.2. Lactate production from inosine depended on the cellular inorganic phosphate available for phosphorolysis and was raised to some 4 times the normal rate from glucose. Inosine inhibited glucose metabolism according to the amount of glucose-6-phosphate produced. Guanosine behaved similarly, but glucose-6-phosphate was not formed from adenosine, deoxyinosine and deoxyguanosine.3. Glucose metabolism was related to the ATP content of the cells, which was raised by incubation with adenosine, or with inosine plus adenine.4. Adenosine and deoxyadenosine raised the potassium influx above the values found with inosine and deoxyinosine under conditions when the lactate production was constant. Active potassium influx was correlated with the ATP concentration in the cells, but independent of the lactate produ ction when the latter was raised above normal.

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Section: Metabolism Of Nucleosides and Glucosementioning

confidence: 99%

Potassium transport and nucleoside metabolism in human red cells

Whittam¹,

Wiley²

1967

The Journal of Physiology

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“…In recent years investigations of erythrocyte metabolism have been concerned with the interrelationships of enzymes, coenzymes, substrates, cofactors, and pH, inter alia (1)(2)(3)(4)(5)(6)(7)(8). Although data have accumulated on these various aspects of the metabolism of normal and pathological erythrocytes, little direct information has been available heretofore on pyridine nucleotide coenzymes, despite their importance in both the glycolytic and the hexose monophosphate shunt pathways.…”

mentioning

confidence: 99%

Pyridine nucleotides in erythrocyte metabolism.

Gross¹,

Schroeder²,

Gabrio³

1966

J. Clin. Invest.

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In recent years investigations of erythrocyte metabolism have been concerned with the interrelationships of enzymes, coenzymes, substrates, cofactors, and pH, inter alia (1-8). Although data have accumulated on these various aspects of the metabolism of normal and pathological erythrocytes, little direct information has been available heretofore on pyridine nucleotide coenzymes, despite their importance in both the glycolytic and the hexose monophosphate shunt pathways. The availability of these compounds in the blood of immature subjects is of particular interest because of certain abnormalities in the erythrocytes of fullterm newborn and prematurely born infants. These abnormalities, which include decreased survival of 51Cr-labeled erythrocytes in premature infants (9, 10) and increased susceptibility to Heinz body formation (11) and to methemoglobinemia (12-15) in both full-term and premature infants, as well as the occurrence of unexplained hemolytic anemias, suggest the possibility of transient biochemical defects in the erythrocytes of these young subjects. Although the activities of the pyridine nucleotide-dependent enzymes in both the glycolytic and shunt pathways are increased in the erythrocytes of young infants (16,17), the levels of the oxidized and reduced coenzymes themselves have not been reported.In the present study the concentrations of DPN,l

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“…Levels of glucose-6-phosphate dehydrogenase (G-6-PD) and 6-phosphogluconic acid dehydrogenase (6-PGD) were assayed by a modification of the method of Glock and McLean as modified by Zinkham and Lenhard (33). Hexokinase activity was determined according to the method of Chapman et al (6). Pyruvate kinase was assayed by the technique of Tanaka et al (27).…”

Section: Methodsmentioning

confidence: 99%

Hemoglobin Cheverly: an Unstable Hemoglobin Associated with Chronic Mild Anemia

et al. 1983

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SummaryThe evaluation of a family with chronic mild anemia led to the identification of a new unstable hemoglobin (Hemoglobin Cheverly). Modest anemia and reticulocytosis, normal to slightly increased mean corpuscular volume (MCV), and normal mean corpuscular hemoglobin concentration (MCHC) were present in the affected family members. Electrophoresis of blood samples on cellulose acetate and on citrate agar revealed normal patterns. Globin chain analysis and isoelectric focusing data were also normal. After incubation for 3 h at 41°C, Heinz bodies were detected in 95-100% of erythrocytes from affected individuals. Positive heat and isopropanol tests confirmed the initial observation of the Heinz body preparation and indicated that an unstable hemoglobin was present. Structural analysis showed an amino acid substitution of Phe-Ser at position 45 (CD4) in the P chain.

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Erythrocyte Metabolism. V. Levels of Glycolytic Enzymes and Regulation of Glycolysis*

Cited by 136 publications

References 25 publications

Potassium transport and nucleoside metabolism in human red cells

Potassium transport and nucleoside metabolism in human red cells

Pyridine nucleotides in erythrocyte metabolism.

Hemoglobin Cheverly: an Unstable Hemoglobin Associated with Chronic Mild Anemia

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