Purification and biochemical characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase from rat lung and inhibition effects of some antibiotics

Adem, Şevki; Çiftçi, Mehmet

doi:10.3109/14756366.2015.1132711

Cited by 18 publications

(10 citation statements)

References 59 publications

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“…The results indicated that the G6PD, 6PGD, and GR enzymes are homodimers. Similar results have been observed for rat kidney, rat lung, rat heart, trout liver, human erythrocytes, and calf liver …”

Section: Discussionsupporting

confidence: 88%

In vitro and in vivo effects of iron on the expression and activity of glucose 6‐phosphate dehydrogenase, 6‐phosphogluconate dehydrogenase, and glutathione reductase in rat spleen

Baltaci

Guler

Ceylan

et al. 2018

J Biochem & Molecular Tox

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Iron is an indispensable element for vital activities in almost all living organisms. It is also a cofactor for many proteins, enzymes, and other essential complex biochemical processes. Therefore, iron trafficking is firmly regulated by Hepcidin (Hamp), which is regarded as the marker for iron accumulation. The disruption of iron homeostasis leads to oxidative stress that causes various human diseases, but this mechanism is still unclear. The aim of this study is to provide a better in vivo and in vitro understanding of how long‐term iron overload affects the gene expression and activities of some antioxidant enzymes, such as glucose 6‐phosphate dehydrogenase (G6PD), 6‐phosphogluconate dehydrogenase (6PGD), and glutathione reductase (GR) in the spleen. The findings of this study show that iron overload reduces the gene expression of G6pd, 6pgd, and Gr, but its actual effect was on the protein level.

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Section: Discussionsupporting

confidence: 88%

In vitro and in vivo effects of iron on the expression and activity of glucose 6‐phosphate dehydrogenase, 6‐phosphogluconate dehydrogenase, and glutathione reductase in rat spleen

Baltaci

Guler

Ceylan

et al. 2018

J Biochem & Molecular Tox

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“…Similarly inhibitory effects of some antibiotics on purified rat lung G6PD, 6PGD, and GR enzymes were investigated. Levofloxacin, furosemide, ceftazidime, cefuroxime, and gentamicin were found to exert inhibition on enzyme activity . In another study, inhibitory effects of some metals on GR enzyme purified from human erythrocytes .…”

Section: Discussionmentioning

confidence: 91%

“…Similarly 6‐phosphogluconate dehydrogenase, catalyzes third reaction in the same pathway and converts 6‐phosphogluconate into d ‐ribulose 5‐phosphate in the presence of NADP + . GR enzyme, which is a member of oxidoreductase enzyme family, converts oxidized glutathione into reduced glutathione . TrxR belongs to pyridine nucleotide disulfate oxidoreductase flavonoid family.…”

Section: Discussionmentioning

confidence: 99%

The effect of astaxanthin and cadmium on rat erythrocyte G6PD, 6PGD, GR, and TrxR enzymes activities in vivo and on rat erythrocyte 6PGD enzyme activity in vitro

Akkoyun

Bengü²,

Temel

et al. 2018

J Biochem & Molecular Tox

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In this study, the effects of astaxanthin (AST) that belongs to carotenoid family and cadmium (Cd), which is an important heavy metal, on rat erythrocyte G6PD, 6PGD, GR, and TrxR enzyme activities in vivo and on rat erythrocyte 6PGD enzyme activity in vitro were studied. In in vitro studies, 6PGD enzyme was purified from rat erythrocytes with 2',5'-ADP Sepharose4B affinity chromatography. Results showed inhibition of enzyme by Cd at IC ; 346.5 μM value and increase of 6PGD enzyme activity by AST. In vivo studies showed an increase in G6PD, 6PGD, and GR enzyme activities (P ˃ 0.05) and no chance in TrxR enzyme activity by AST. Cd ion inhibited G6PD, 6PGD, and GR enzyme activities (P ˂ 0.05) and also decreased TrxR enzyme activity (P ˃ 0.05). AST + Cd group G6PD enzyme activity was statistically low compared with control group (P ˂ 0.05). 6PGD and TrxR enzyme activities decreased without statistical significance (P ˃ 0.05); however, GR enzyme activity increased statistically significantly (P ˂ 0.05).

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“…NADPH inhibits 6PGD, so it has a negative mechanism. Again, the optimum pHi for this enzyme is alkaline [ 43 , 44 ].…”

Section: Oxidative Phasementioning

confidence: 99%

The Pentose Phosphate Pathway Dynamics in Cancer and Its Dependency on Intracellular pH

et al. 2020

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The Pentose Phosphate Pathway (PPP) is one of the key metabolic pathways occurring in living cells to produce energy and maintain cellular homeostasis. Cancer cells have higher cytoplasmic utilization of glucose (glycolysis), even in the presence of oxygen; this is known as the “Warburg Effect”. However, cytoplasmic glucose utilization can also occur in cancer through the PPP. This pathway contributes to cancer cells by operating in many different ways: (i) as a defense mechanism via the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) to prevent apoptosis, (ii) as a provision for the maintenance of energy by intermediate glycolysis, (iii) by increasing genomic material to the cellular pool of nucleic acid bases, (iv) by promoting survival through increasing glycolysis, and so increasing acid production, and (v) by inducing cellular proliferation by the synthesis of nucleic acid, fatty acid, and amino acid. Each step of the PPP can be upregulated in some types of cancer but not in others. An interesting aspect of this metabolic pathway is the shared regulation of the glycolytic and PPP pathways by intracellular pH (pHi). Indeed, as with glycolysis, the optimum activity of the enzymes driving the PPP occurs at an alkaline pHi, which is compatible with the cytoplasmic pH of cancer cells. Here, we outline each step of the PPP and discuss its possible correlation with cancer.

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Purification and biochemical characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase from rat lung and inhibition effects of some antibiotics

Cited by 18 publications

References 59 publications

In vitro and in vivo effects of iron on the expression and activity of glucose 6‐phosphate dehydrogenase, 6‐phosphogluconate dehydrogenase, and glutathione reductase in rat spleen

In vitro and in vivo effects of iron on the expression and activity of glucose 6‐phosphate dehydrogenase, 6‐phosphogluconate dehydrogenase, and glutathione reductase in rat spleen

The effect of astaxanthin and cadmium on rat erythrocyte G6PD, 6PGD, GR, and TrxR enzymes activities in vivo and on rat erythrocyte 6PGD enzyme activity in vitro

The Pentose Phosphate Pathway Dynamics in Cancer and Its Dependency on Intracellular pH

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