The hydrogen ion concentrations and erythrocyte glycolysis

Minakami, Shigeki; Saito, Toshihito; Suzuki, Chiyo; Yoshikawa, Hideki

doi:10.1016/0006-291x(64)90425-5

Cited by 40 publications

(6 citation statements)

References 10 publications

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“…(G. Hubscher, unpublished work), whereas homogenates of rat liver have specific activities of 4-5 (Sedgwick, 1965). The finding that hexokinase and phosphofructokinase are the rate-limiting steps of glycolysis in cat small-intestinal mucosa may be compared with similar observations reported for erythrocytes (Minakami, Saito, Suzuki & Yoshikawa, 1964), kidney slices (Wu, 1965) and rat and guinea-pig liver homogenates (Lea & Walker, 1965).…”

Section: Additionsupporting

confidence: 58%

Glucose metabolism in the mucosa of the small intestine. Glycolysis in subcellular preparations from the cat and rat

Lm¹,

Hübscher²

1966

Biochemical Journal

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1. Lactic acid formation in supernatant fractions of homogenates of cat or rat small-intestinal mucosa was measured under optimum conditions with glucose, fructose, glucose 6-phosphate, fructose 1,6-diphosphate or 3-phosphoglycerate as substrate. 2. Between 80 and 107% of the glycolytic activity of the homogenate was recovered in these particle-free preparations when glucose, fructose, glucose 6-phosphate or fructose 1,6-diphosphate was used as substrate. 3. Evidence was obtained that hexokinase and phosphofructokinase were the rate-limiting enzymes in the initial sequence of glycolytic reactions. The limitation of rate by hexokinase was much more pronounced in preparations from the cat than in those from the rat. 4. With subcellular preparations from cat or rat small intestine lactic acid was also formed from ribose 5-phosphate and at rates similar to those observed with glucose. 5. A higher rate of glycolysis was observed with glucose 6-phosphate as substrate with preparations from the proximal half of the small intestine of the rat as compared with the distal half. 6. Mucosal preparations from rats starved for 24-48hr. exhibited only about one-quarter of the glycolytic activity of those of fed control groups. The decreased rate of formation of lactic acid from either glucose or fructose was mainly due to a decrease in the activity of hexokinase(s). The activities of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase and a number of other enzymes were not significantly decreased by starvation. 7. The results are discussed in relation to metabolic control of glycolysis in other mammalian tissues.

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Section: Additionsupporting

confidence: 58%

Glucose metabolism in the mucosa of the small intestine. Glycolysis in subcellular preparations from the cat and rat

Lm¹,

Hübscher²

1966

Biochemical Journal

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“…We have confirmed these findings, and Table 1 shows 2 , 0 that at pH 6.9 the concentration of Gri-2,3-P2 fell dramatically, whereas at pH 7.4 or 8.2 it remained relatively stable. In agreement with previous data [14,15] 4 h incubation at pH 6.9, but not at pH 7.4 or 8.…”

Section: \ 10 Osupporting

confidence: 93%

Fructose 2,6-bisphosphate in rat erythrocytes. Inhibition of fructose 2,6-bisphosphate synthesis and measurement by glycerate 2,3-bisphosphate

Sobrino

Rider

Gualberto

et al. 1987

Biochemical Journal

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The concentration of fructose 2,6-bisphosphate found in freshly isolated erythrocytes was below the limit of detection (20 pmol/ml of packed cells). However, it increased to about 250 pmol/ml of cells when erythrocytes were incubated with glucose at pH 6.9, but not at pH 7.4 or 8.2. This could be explained by variations in the content of glycerate 2,3-bisphosphate, which was found to inhibit 6-phosphofructo-2-kinase, the enzyme responsible for fructose 2,6-bisphosphate synthesis. Glycerate 2,3-bisphosphate was also found to inhibit the potato enzyme (pyrophosphate:fructose-6-phosphate 1-phosphotransferase) used for the measurement of fructose 2,6-bisphosphate.

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“…We performed in vitro 6PGD and G6PD assays in the presence of increasing concentrations of 3-PG. Physiological concentrations of 3-PG in human cells are reported to be approximately 50–80μM (Feig et al, 1971; Minakami et al, 1964; Mulquiney and Kuchel, 1999). As shown in Table S3, we determined that, in H1299, MDA-MB231 and Molm14 cells, the 3-PG levels are approximately 60–80μM in control vector cells and 200–300μM in PGAM1 knockdown cells, while the 3-PG concentrations are approximately 160μM and 310μM in 212LN control and PGAM1 knockdown cells, respectively.…”

Section: Resultsmentioning

confidence: 99%

Phosphoglycerate Mutase 1 Coordinates Glycolysis and Biosynthesis to Promote Tumor Growth

et al. 2012

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SUMMARY It remains unclear how cancer cells coordinate glycolysis and biosynthesis to support rapidly growing tumors. We found that glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), commonly upregulated in human cancers due to loss of TP53, contributes to biosynthesis regulation in part by controlling intracellular levels of its substrate 3-phosphoglycerate (3-PG) and product 2-phosphoglycerate (2-PG). 3-PG binds to and inhibits 6-phosphogluconate dehydrogenase in the oxidative pentose phosphate pathway (PPP), while 2-PG activates 3-phosphoglycerate dehydrogenase to provide feedback control of 3-PG levels. Inhibition of PGAM1 by shRNA or a small molecule inhibitor PGMI-004A results in increased 3-PG and decreased 2-PG levels in cancer cells, leading to significantly decreased glycolysis, PPP flux and biosynthesis, as well as attenuated cell proliferation and tumor growth.

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The hydrogen ion concentrations and erythrocyte glycolysis

Cited by 40 publications

References 10 publications

Glucose metabolism in the mucosa of the small intestine. Glycolysis in subcellular preparations from the cat and rat

Glucose metabolism in the mucosa of the small intestine. Glycolysis in subcellular preparations from the cat and rat

Fructose 2,6-bisphosphate in rat erythrocytes. Inhibition of fructose 2,6-bisphosphate synthesis and measurement by glycerate 2,3-bisphosphate

Phosphoglycerate Mutase 1 Coordinates Glycolysis and Biosynthesis to Promote Tumor Growth

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