Relationship of solute permeability to erythrocyte glycolysis

doi:10.1016/0005-2736(70)90009-X

Biochimica et Biophysica Acta (BBA) - Biomembranes

Volume 196, Issue 2, 3 February 1970, Pages 215-220

https://doi.org/10.1016/0005-2736(70)90009-X Get rights and content

Abstract

Erythrocyte suspensions demonstrate remarkable changes in glycolytic rate in response to the permeability characteristics of the solutes present. Erythrocytes when placed in electrolyte or nonelectrolyte media of limited permeability produce lactate at accelerated rates, attributable to a stimulation of ATP degradation. The mechanism(s) of increased turnover of ATP and the purpose to which the excess energy is directed remain to be clarified.

References (22)

O.H. Lowry et al.
J. Biol. Chem.
(1964)
K.K. Tsuboi
Biochim. Biophys. Acta
(1963)
T. Kuzuya et al.
J. Biol. Chem.
(1965)
S. Minakami et al.
Biochem. Biophys. Res. Commun.
(1964)
S. Minakami et al.
Biochim. Biophys. Acta
(1965)
K.K. Tsuboi et al.
J. Biol. Chem.
(1965)
I.A. Rose et al.
Biochem. Biophys. Res. Commun.
(1964)
P.L. Mollison et al.
Lancet
(1958)
J.M. Murphy
J. Lab. Med.
(1963)
R. Whittam et al.
Biochem. J.
(1965)

G.E. Cartwright

Diagnostic Laboratory Hematology

Cited by (13)

Effect of membrane potential and internal pH on active sodium-potassium transport and on ATP content in high-potassium sheep erythrocytes
1979, BBA - Biomembranes
Ouabain-sensitive Na⁺ and K⁺ fluxes and ATP content were determined in high potassium sheep erythrocytes at different values of membrane potential and internal pH. Membrane potential was adjusted by suspending erythrocytes in media containing different concentrations of MgCl₂ and sucrose. Concomitantly either the external pH was changed sufficiently to maintain a constant internal pH or the external pH was kept constant with a resultant change of internal pH. The erythrocytes were preincubated before the flux experiment started in a medium which produced increased ATP content in order to avoid substrate limitation of the pump. p] It was found that an increased cellular pH reduced the rates of active transport of Na⁺ and K⁺ without significantly altering the ratio of pumped $Na^{+} K^{+}$ . This reduction was not due to limitation in the supply of ATP although ATP content decreased when internal pH increased. Changes of membrane potential in the range between −10 and +60 mV at constant internal pH did not affect the rates of active transport of Na⁺ or K⁺.
Regulation of erythrocyte glycolysis. Membrane-mediated activation induced in low-electrolyte medium
1974, BBA - Biomembranes
Human erythrocyte suspensions prepared in low-electrolyte medium maintain a high rate of glycolytic flow, which may exceed by 3-fold the normal rate of glucose utilization by these cells. Rapid redistribution of permeable cation and anion occurs in low-electrolyte media to new Donnan equilibria with changes in both intramembrane and intracellular ionic environment indicated. A primary consequence of the ionic redistribution involves proton loss with intracellular alkalinization accounting for a part, but not all, of the resultant glycolytic stimulation. Stimulation of glycolytic rate in response to pH includes an apparent highly coordinated dual mechanism involving both pH-induced acceleration of ATP degradation and pH activation of the regulatory enzyme phosphofructokinase. A second pH-independent, membrane-mediated, stimulation of glycolytic rate is also indicated in low-electrolyte media. The basis of this additional stimulation involves again an induced acceleration of ATP-degradation rate, with changes in intramembrane ionic environment and resultant effects on the associated ATPase of apparent contributing significance.
Regulation of mammalian hexokinase: Regulatory differences between isoenzyme I and II
1973, Archives of Biochemistry and Biophysics
Mammalian hexokinase isoenzymes I and II have been shown to differ qualitatively in response to various modifiers. Although both enzymes are inhibited by glucose 6-phosphate, only isoenzyme II exhibits a slow response to the presence of this inhibitor. P_i decreases the affinity of glucose 6-phosphate for Sarcoma 37 hexokinase I, but has no effect on hexokinase II from the same cell. P_i overcomes all of the inhibition of red cell hexokinase by glucose-6-P and hence the two effectors act competitively. At pH 6.5, catecholamines increase the V of isoenzyme I of Sarcoma 37 and brain in the soluble and mitochondrial forms but do not activate these forms of tumor isoenzyme II. Citrate activates brain and tumor isoenzyme I when they are inhibited by tris(hydroxy-methyl)aminomethylethane sulfonate (TES) and ADP; however, tumor isoenzyme II is not activated.
Regulation of human red cell glycolysis: A review
1971, Experimental Eye Research
Studies in Red Blood Cell Preservation: 7. In vivo and in vitro Studies with a Modified Phosphate‐Ammonium Additive Solution
1993, Vox Sanguinis
Manipulating Red Cell Intra‐ and Extracellular pH by Washing
1991, Vox Sanguinis

View all citing articles on Scopus

View full text

Relationship of solute permeability to erythrocyte glycolysis

Abstract

J. Biol. Chem.

Biochim. Biophys. Acta

J. Biol. Chem.

Biochem. Biophys. Res. Commun.

Biochim. Biophys. Acta

J. Biol. Chem.

Biochem. Biophys. Res. Commun.

Lancet

J. Lab. Med.

Biochem. J.

Diagnostic Laboratory Hematology