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Results for “pentose phosphate pathway”

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At least 19 recordsLinked to original sources

PubMed1977

The effect of 6-aminonicotinamide blockade of the pentose phosphate pathway on catecholamines in the rat adrenal medulla, superior cervical ganglion, hypothalamus and synaptosome fractions.

The effect on tissue catecholamines of blockade of the pentose phosphate pathway with 6-aminonicotinamide (6-AN) was studied in the rat. 6-AN at 35-50 mg kg-1 persistently lowered the adrenaline content in the adrenal gland to less than 10% of control values and caused a 50% loss of noradrenaline, which recovered. When the amine turnover rate was increased by a preceding period of drum stress, 6-AN also consistently depressed noradrenaline in the gland. 6-AN was without significant effect on the noradrenaline concentration in heart tissue, hypothalamus and superior cervical ganglion and did not affect the uptake or release of catecholamines in vitro. The possibility is discussed that 6-AN interferes with the biosynthesis of catecholamines, when it blocks the pentose phosphate pathway, by decreasing the supply of reducing equivalents in the form of NADPH which are necessary for the tetrahydropteridine cofactors of tyrosine hydroxylase.

6-Aminonicotinamide↗

PubMed1979

NADPH production in the oxidative pentose phosphate pathway as source of reducing equivalents in glycolysis of human red cells in vitro.

Studies have been carried out on human erythrocytes in vitro to clarify the deficit of pyruvate formation under conditions when 2,3 DPG is degraded. The results lead to the conclusion that there exist a cross connection between the glycolytic and the oxidative pentose phosphate pathway which is mediated by the NADP/NADPH couple. NADPH serves as additional reducing equivalent in the reaction of the LDH. In the absence of glucose the pool of the metabolites of the pentose phosphate pathway is able to supply glucose-6-phosphate for the production of NADPH by recombination. The reaction of NADPH at the LDH is probably of significance under in vivo conditions.

Diphosphoglyceric Acids↗

PubMed1976

[Soluble, nuclear and mitochondrial forms of dehydrogenases, pentose-phosphate pathway transferases and nucleases in chicken liver].

The sub-cellular topography of oxidative and non-oxidative enzymes of the pentose phosphate pathway of carbohydrates metabolism and enzymes of the nucleic exchange (acid and alkaline deoxyribonucleases and ribonucleases) in chicken liver is studied. Nuclear and mitochondrial forms of the enzymes are discovered. The activity of the enzymes studied of carbohydrates metabolism is shown to correlate with that of the enzymes of nucleic metabolism in cytosol, nucleic and mitochondrial liver fractions.

Animals↗

PubMed1975

The effect of o-salicylate upon pentose phosphate pathway activity in normal and G6PD-deficient red cells.

The effect of the major metabolite of aspirin, namely salicylic acid, upon the pentose phosphate pathway (PPP) of normal and G6PD-deficient red cells has been studied. Salicylic acid was shown to inhibit this pathway in proportion to the amount present. At any concentration of this substance there was greater inhibition of the PPP in G6PD-deficient than in normal red cells.

Blood Glucose↗

PubMed2026

Metabolic atlas of early human cortex reveals glycolytic remodeling and pentose phosphate pathway control of cell fate transitions.

Cortical development involves rapid progenitor expansion and cell diversification supported by tightly regulated metabolic programs, yet these programs remain largely uncharacterized in human development. Here, we generated a metabolic atlas of the early human cortex using primary tissue and stem cell-derived cortical organoids. We observed dynamic changes in core metabolic functions, including an unexpected increase in glycolysis and pentose phosphate pathway (PPP) activity during late neurogenesis. Manipulation of glucose availability in cortical organoids altered cell-type composition, increasing outer radial glia (oRG) and inhibitory neuron populations. Pharmacological and genetic inhibition of PPP enzymes recapitulated these cell fate changes. Ribose was sufficient to rescue radial glia (RG) gene expression changes, revert organoid cell-type composition, and restore levels of ATP and hypotaurine. These data identify a critical role for the PPP in modulating RG cell fate specification and generate a resource for future exploration of additional metabolic pathways in human cortical development.

cell fate↗

PubMed2024

The NRF2-CARM1 axis links glucose sensing to transcriptional and epigenetic regulation of the pentose phosphate pathway in gastric cancer.

Cancer cells autonomously alter metabolic pathways in response to dynamic nutrient conditions in the microenvironment to maintain cell survival and proliferation. A better understanding of these adaptive alterations may reveal the vulnerabilities of cancer cells. Here, we demonstrate that coactivator-associated arginine methyltransferase 1 (CARM1) is frequently overexpressed in gastric cancer and predicts poor prognosis of patients with this cancer. Gastric cancer cells sense a reduced extracellular glucose content, leading to activation of nuclear factor erythroid 2-related factor 2 (NRF2). Subsequently, NRF2 mediates the classic antioxidant pathway to eliminate the accumulation of reactive oxygen species induced by low glucose. We found that NRF2 binds to the CARM1 promoter, upregulating its expression and triggering CARM1-mediated hypermethylation of histone H3 methylated at R arginine 17 (H3R17me2) in the glucose-6-phosphate dehydrogenase gene body. The upregulation of this dehydrogenase, driven by the H3R17me2 modification, redirects glucose carbon flux toward the pentose phosphate pathway. This redirection contributes to nucleotide synthesis (yielding nucleotide precursors, such as ribose-5-phosphate) and redox homeostasis and ultimately facilitates cancer cell survival and growth. NRF2 or CARM1 knockdown results in decreased H3R17me2a accompanied by the reduction of glucose-6-phosphate dehydrogenase under low glucose conditions. Collectively, this study reveals a significant role of CARM1 in regulating the tumor metabolic switch and identifies CARM1 as a potential therapeutic target for gastric cancer treatment.

Stomach Neoplasms↗

PubMed1975

[Pentose phosphate pathway and nucleic acid synthesis in human funicular tissue. In vitro studies].

Umbilical cord slices were incubated with either 1- or 6-14C-glucose, the radioactivities of which were measured in CO2 evolved. The ratio, 1 CO2/6 CO2 was low, being comprised between 1 and 2. Furthermore, this incubation of cord slices with tritiated uridine or thymidine resulted in very low incorporations, especially for the latter. Therefore, both the pentose phosphate pathway and the synthesis of nucleic acid have a low activity in the cord tissue: these might be signs of senescence in this otherwise fetal organ.

Carbon Dioxide↗

PubMed1979

[Activities of dehydrogenases of the pentose phosphate pathway and transketolase in transplanted mouse hepatomas with different growth rates and in organs of tumor carriers].

The activities of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and transketolase were studied in the cytoplasmic fractions of transplanted mouse hepatomas differing in their growth rates, and in the liver, spleen and cortical layer of kidneys of tumour carriers and normal mice. It was shown that transplantation of hepatomas changes the activity of the pentose phosphate pathway enzymes in tumour carrier tissues unaffected by neoplasm. Deviations from normalcy were mainly similar to those observed in the hepatomas. The changes in the enzymatic activities were especially well-pronounced in the mice having rapidly growing hepatomas. This may be due to a generalized effect of the tumour on the organism, which is concurrent with malignancy.

Animals↗

PubMed1979