Interaction of a rat kidney endoplasmic reticulum fraction with glycolytic enzymes

Jones, Vernon D.; Norris, John L.; Landon, Erwin J.

doi:10.1016/0006-3002(63)91082-5

Cited by 17 publications

(10 citation statements)

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“…The nuclear fraction possesses adenosine-triphosphatase activity, and the addition of pyruvate lowered the stimulating effect of this fraction, as it did that of the other ADP-forming systems. These results are in many ways similar to those observed by Jones et al (1963) for the effect of the endoplasmic reticulum of kidney tissue on glycolysis by kidney supernatant preparations. Jones et al (1963) demonstrated a direct action of adenosine triphosphatase on the reaction catalysed by a purified preparation of 3-phosphoglycerate kinase.…”

Section: Discussion T8 ;6supporting

confidence: 88%

“…2 of Table 8). Jones, Norris & Landon (1963), using rat-kidney preparations, and Wenner & Cereijo-Santalo (1963), using mouse liver, showed that the formation of glycolytic end products was affected markedly by ADP or ADP-generating systems acting at the 3-phosphoglycerate-kinase (EC 2.7.2.3) stage. Thus they demonstrated that the addition of such factors as arsenate, adenosine-triphosphatase activity or an ADP-generating system (consisting of ATP, 2deoxyglucose and hexokinase) accelerated lactate formation by supernatant preparations, especially with fructose 1,6-diphosphate as substrate, and that such stimulation occurred even in the presence of an optimum concentration of ADP.…”

Section: Wholementioning

confidence: 99%

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Factors Affecting Hepatic Glycolysis and Some Changes That Occur During Development

Lea¹,

Walker²

1965

Biochemical Journal

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1. Glycolysis by the supernatant fraction of homogenates of liver from guinea pigs and rats at various stages of development (foetal, newborn and adult) has been examined in a suitably fortified medium by measurement of inorganic phosphate uptake and production of lactate and glycerol 1-phosphate. 2. Starting with glucose as substrate, two rate-determining steps in glycolysis occur at the stages of glucose phosphorylation and the phosphofructokinase reaction in liver tissue from animals of all ages. Effects of the post-natal development of glucokinase are recorded. 3. The appearance of microsomal glucose 6-phosphatase activity around birth has an effect on glycolysis owing to competition for glucose 6-phosphate. 4. A stimulating effect of the nuclear fraction, especially from foetal liver, on glycolysis by the supernatant fraction is interpreted as being due to stimulation by adenosine-triphosphatase activity at the 3-phosphoglycerate-kinase stage.

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Section: Discussion T8 ;6supporting

confidence: 88%

Section: Wholementioning

confidence: 99%

Factors Affecting Hepatic Glycolysis and Some Changes That Occur During Development

Lea¹,

Walker²

1965

Biochemical Journal

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“…At high ATP, no effect of ouabain on the reverse reaction of ghost PGK was demonstrable. Jones et al (1963) have demonstrated the presence of both PGK and Na, K-ATPase activity in a preparation of rat kidney microsomes which possesses the ability to stimulate glycolysis in a soluble fraction of the kidney homogenate. Although these authors do not report studies of the metabolic effects of ouabain or variations in cation content, it is likely that their system bears many resemblances to the one presented here.…”

Section: Discussionmentioning

confidence: 99%

The Role of Membrane Phosphoglycerate Kinase in the Control of Glycolytic Rate by Active Cation Transport in Human Red Blood Cells

Parker

Hoffman

1967

The Journal of General Physiology

179

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When the internal Na of human red cells is raised, both K influx and lactate production increase and become more sensitive to the inhibitory action of ouabain. This occurs with either glucose or purine nucleoside as substrate. Fresh whole hemolysates enriched with Na and Mg will convert intermediates above the triose phosphate dehydrogenase step to lactate at a rate which is slowed by ouabain. Intermediates beyond the phosphoglycerate kinase step (PGK) are metabolized at a very rapid rate which is not affected by ouabain. No metabolic effects of ouabain were found in ghost-free hemolysates. Hemoglobin-free ghosts were shown to have both triose phosphate dehydrogenase and PGK activity. The rate of this two-enzyme sequence was found to be a function of the ADP concentration, being maximal when ADP > 0.35 mnm. Initial addition of ATP to the ghost system rendered the forward rate of the sequence sensitive to the inhibitory action of ouabain. When the sequence was run in reverse, no inhibitory effect of ouabain could be demonstrated. It is concluded that membrane PGK is a point at which the Na-K transport system can influence the metabolic rate and that this action is possibly exerted via a compartmentalized form of ADP which is an immediate substrate for the ghost PGK.

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“…Schrier (43) and Parker and Hoffman (44) proposed that phosphoglycerate kinase could generate ATP adjacent to Na+-K+-ATPase within the microenvironment of the membrane. Jones et al (45) demonstrated a similar relationship in kidney microsomes suggesting that whole cell concentrations of ATP may not necessarily correlate with transport; rather the activity of ATP producing reactions (glycolysis or oxidative phosphorylation) may more closely approximate Na+-K+-ATPase activity. Thus, it is possible that the turnover of ATP (ATP synthesis and hydrolysis) is a more important determinant of renal transport than absolute ATP levels.…”

Section: Discussionmentioning

confidence: 75%

³¹P NMR studies of ATP concentrations and P_i–ATP exchange in the rat kidney in Vivo: Effects of inhibiting and stimulating renal metabolism

Shine

Xuan

Weiner

1990

Magnetic Resonance in Med

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Previous investigators found that cyanide (CN-) is a potent inhibitor of renal Na+ transport, while the uncoupling agent 2,4-dinitrophenol (DNP) and fructose (both which lower ATP levels) are weak transport inhibitors. To examine the disparate effects of these substances measurements of ATP were performed, using 31P NMR, while simultaneously monitoring renal Na+ transport. Infusion of CN-, DNP, and fructose lowered whole kidney ATP levels by about the same extent (30%) while only CN- inhibited Na+ transport. This may be due to the fact that CN- has a potent action on the thick ascending limb of Henle, while fructose and DNP may have a more proximal action. Alternatively, ATP turnover may be a more important determinant of transport than ATP concentrations. Saturation transfer experiments were performed to measure Pi-ATP flux. Unilateral nephrectomy, high protein feeding, and methylprednisolone were used to stimulate metabolism and transport. The rate of Pi-ATP flux was 20.1 mumol/min/g. However, because oxygen consumption was stimulated, the ATP/O ratio was 0.85, considerably less than the theoretical value of 3. Finally, atrial natriuretic factor, which increased Na+ transport, had no effect on Pi-ATP flux. The results raise the possibility that the saturation transfer technique does not detect all Pi-ATP flux, especially when renal metabolism is stimulated.

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Interaction of a rat kidney endoplasmic reticulum fraction with glycolytic enzymes

Cited by 17 publications

References 10 publications

Factors Affecting Hepatic Glycolysis and Some Changes That Occur During Development

Factors Affecting Hepatic Glycolysis and Some Changes That Occur During Development

The Role of Membrane Phosphoglycerate Kinase in the Control of Glycolytic Rate by Active Cation Transport in Human Red Blood Cells

³¹P NMR studies of ATP concentrations and P_i–ATP exchange in the rat kidney in Vivo: Effects of inhibiting and stimulating renal metabolism

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Interaction of a rat kidney endoplasmic reticulum fraction with glycolytic enzymes

Cited by 17 publications

References 10 publications

Factors Affecting Hepatic Glycolysis and Some Changes That Occur During Development

Factors Affecting Hepatic Glycolysis and Some Changes That Occur During Development

The Role of Membrane Phosphoglycerate Kinase in the Control of Glycolytic Rate by Active Cation Transport in Human Red Blood Cells

31P NMR studies of ATP concentrations and Pi–ATP exchange in the rat kidney in Vivo: Effects of inhibiting and stimulating renal metabolism

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³¹P NMR studies of ATP concentrations and P_i–ATP exchange in the rat kidney in Vivo: Effects of inhibiting and stimulating renal metabolism