scholarly journals NHERF1 Loss Upregulates Enzymes of the Pentose Phosphate Pathway in Kidney Cortex

Antioxidants ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 862
Author(s):  
Adrienne Bushau-Sprinkle ◽  
Michelle T. Barati ◽  
Kenneth B. Gagnon ◽  
Syed Jalal Khundmiri ◽  
Kathleen Kitterman ◽  
...  
Keyword(s):  
Pentose Phosphate Pathway ◽  
Mitochondrial Protein ◽  
Pentose Phosphate ◽  
Metabolic Enzyme ◽  
Kidney Cortex ◽  
Mitochondrial Morphology ◽  
Proximal Tubule Cells ◽  
Cisplatin Nephrotoxicity ◽  
Increased Sensitivity ◽  
Glucose 6 Phosphate Dehydrogenase

(1) Background: We previously showed Na/H exchange regulatory factor 1 (NHERF1) loss resulted in increased susceptibility to cisplatin nephrotoxicity. NHERF1-deficient cultured proximal tubule cells and proximal tubules from NHERF1 knockout (KO) mice exhibit altered mitochondrial protein expression and poor survival. We hypothesized that NHERF1 loss results in changes in metabolic pathways and/or mitochondrial dysfunction, leading to increased sensitivity to cisplatin nephrotoxicity. (2) Methods: Two to 4-month-old male wildtype (WT) and KO mice were treated with vehicle or cisplatin (20 mg/kg dose IP). After 72 h, kidney cortex homogenates were utilized for metabolic enzyme activities. Non-treated kidneys were used to isolate mitochondria for mitochondrial respiration via the Seahorse XF24 analyzer. Non-treated kidneys were also used for LC-MS analysis to evaluate kidney ATP abundance, and electron microscopy (EM) was utilized to evaluate mitochondrial morphology and number. (3) Results: KO mouse kidneys exhibit significant increases in malic enzyme and glucose-6 phosphate dehydrogenase activity under baseline conditions but in no other gluconeogenic or glycolytic enzymes. NHERF1 loss does not decrease kidney ATP content. Mitochondrial morphology, number, and area appeared normal. Isolated mitochondria function was similar between WT and KO. Conclusions: KO kidneys experience a shift in metabolism to the pentose phosphate pathway, which may sensitize them to the oxidative stress imposed by cisplatin.

The influence of lipogenic and lipolytic conditions on the pentose phosphate pathway dehydrogenases in rat-kidney-cortex

1990 ◽  
Vol 98 (2) ◽  
pp. 283-289 ◽  
Author(s):  
J. Peragon ◽  
F. Aranda ◽  
L. Garcia-salguero ◽  
J. B. Barroso ◽  
M. V. Amores ◽  
...  
Keyword(s):  
Pentose Phosphate Pathway ◽  
Rat Kidney ◽  
Pentose Phosphate ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

Respiratory enzyme activities during germination inBrassicaseed lots of differing vigour

1996 ◽  
Vol 6 (4) ◽  
pp. 165-174 ◽  
Author(s):  
Mary Bettey ◽  
W.E. Finch-Savage
Keyword(s):  
Oxygen Consumption ◽  
Pentose Phosphate Pathway ◽  
Sharp Increase ◽  
Artificial Aging ◽  
Pentose Phosphate ◽  
Untreated Seed ◽  
Seed Vigour ◽  
Regulatory Enzymes ◽  
Rate Of Oxygen Consumption ◽  
Glucose 6 Phosphate Dehydrogenase

AbstractThe rate of oxygen consumption by cabbage seeds increased on imbibition and there was a further sharp increase on germination. This was delayed in artificially aged seeds of low vigour. The increases in oxygen consumption reflect the increased oxidation of carbohydrates via respiratory pathways. The activities of key regulatory enzymes of glycolysis and the oxidative pentose phosphate pathway were measured in aged and unaged seed lots of cabbage. Differences in the activities of glucose 6-phosphate dehydrogenase and pyrophosphate:fructose 6-phosphate 1-phosphotransferase were correlated with the rate of germination (T50) in seed lots with large differences in seed vigour induced experimentally by artificial aging. However, the activities of these enzymes could not be used to distinguish between untreated seed lots which had smaller vigour differences apparent only under stress. The enzymes are presumably not controlling and determining seed vigour, but merely reflecting actual seed performance under the current conditions.

scholarly journals Deletion of the Glucose-6-Phosphate Dehydrogenase Gene KlZWF1 Affects both Fermentative and Respiratory Metabolism in Kluyveromyces lactis

2006 ◽  
Vol 6 (1) ◽  
pp. 19-27 ◽  
Author(s):  
Michele Saliola ◽  
Gina Scappucci ◽  
Ilaria De Maria ◽  
Tiziana Lodi ◽  
Patrizia Mancini ◽  
...  
Keyword(s):  
Biomass Yield ◽  
Kluyveromyces Lactis ◽  
Carbon Sources ◽  
Pentose Phosphate ◽  
Respiratory Metabolism ◽  
Wild Type ◽  
Dehydrogenase Gene ◽  
Increased Sensitivity ◽  
Dimeric Form ◽  
Glucose 6 Phosphate Dehydrogenase

ABSTRACT In Kluyveromyces lactis, the pentose phosphate pathway is an alternative route for the dissimilation of glucose. The first enzyme of the pathway is the glucose-6-phosphate dehydrogenase (G6PDH), encoded by KlZWF1. We isolated this gene and examined its role. Like ZWF1 of Saccharomyces cerevisiae, KlZWF1 was constitutively expressed, and its deletion led to increased sensitivity to hydrogen peroxide on glucose, but unlike the case for S. cerevisiae, the Klzwf1Δ strain had a reduced biomass yield on fermentative carbon sources as well as on lactate and glycerol. In addition, the reduced yield on glucose was associated with low ethanol production and decreased oxygen consumption, indicating that this gene is required for both fermentation and respiration. On ethanol, however, the mutant showed an increased biomass yield. Moreover, on this substrate, wild-type cells showed an additional band of activity that might correspond to a dimeric form of G6PDH. The partial dimerization of the G6PDH tetramer on ethanol suggested the production of an NADPH excess that was negative for biomass yield.

scholarly journals Regulation of the pentose phosphate cycle Cofactor that controls the inhibition of glucose-6-phosphate dehydrogenase by NADPH in rat liver

1986 ◽  
Vol 239 (3) ◽  
pp. 553-558 ◽  
Author(s):  
M Nogueira ◽  
G Garcia ◽  
C Mejuto ◽  
M Freire
Keyword(s):  
Ion Exchange ◽  
Rat Liver ◽  
Pentose Phosphate Pathway ◽  
Reductase Activity ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Pentose Phosphate ◽  
Glutathione Reductase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

A cofactor of Mr 10(4), characterized as a polypeptide, was found to co-operate with GSSG to prevent the inhibition of glucose-6-phosphate dehydrogenase by NADPH, in order to ensure the operation of the oxidative phase of the pentose phosphate pathway, in rat liver [Eggleston & Krebs (1974) Biochem. J. 138, 425-435; Rodriguez-Segade, Carrion & Freire (1979) Biochem. Biophys. Res. Commun. 89, 148-154]. This cofactor has now been partially purified by ion-exchange chromatography and molecular gel filtration, and characterized as a protein of Mr 10(5). The lighter cofactor reported previously was apparently the result of proteolytic activity generated during the tissue homogenization. The heavier cofactor was unstable, and its amount increased in livers of rats fed on carbohydrate-rich diet. Since the purified cofactor contained no glutathione reductase activity, the involvement of this enzyme in the deinhibitory mechanism of glucose-6-phosphate dehydrogenase by NADPH should be ruled out.

Hexose-6-phosphate dehydrogenase in the endoplasmic reticulum

2010 ◽  
Vol 391 (1) ◽  
Author(s):  
Silvia Senesi ◽  
Miklos Csala ◽  
Paola Marcolongo ◽  
Rosella Fulceri ◽  
Jozsef Mandl ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Metabolic Syndrome ◽  
Endoplasmic Reticulum ◽  
Pentose Phosphate Pathway ◽  
Hydroxysteroid Dehydrogenase ◽  
Pyridine Nucleotide ◽  
Pentose Phosphate ◽  
The Metabolic Syndrome ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract Hexose-6-phosphate dehydrogenase (H6PD) is a luminal enzyme of the endoplasmic reticulum that is distinguished from cytosolic glucose-6-phosphate dehydrogenase by several features. H6PD converts glucose-6-phosphate and NADP+ to 6-phosphogluconate and NADPH, thereby catalyzing the first two reactions of the pentose-phosphate pathway. Because the endoplasmic reticulum has a separate pyridine nucleotide pool, H6PD provides NADPH for luminal reductases. One of these enzymes, 11β-hydroxysteroid dehydrogenase type 1 responsible for prereceptorial activation of glucocorticoids, has been the focus of much attention as a probable factor in the pathomechanism of several human diseases including insulin resistance and the metabolic syndrome. This review summarizes recent advances related to the functions of H6PD.

scholarly journals Activity of key enzymes involved in glucose and triglyceride catabolism during bovine oocyte maturation in vitro

Reproduction ◽  
2002 ◽  
pp. 675-681 ◽  
Author(s):  
P Cetica ◽  
L Pintos ◽  
G Dalvit ◽  
M Beconi
Keyword(s):  
Enzymatic Activity ◽  
Pentose Phosphate Pathway ◽  
In Vitro Maturation ◽  
Specific Activity ◽  
Lipolytic Activity ◽  
Cumulus Cells ◽  
Pentose Phosphate ◽  
Key Enzymes ◽  
Glucose 6 Phosphate Dehydrogenase

Little is known about the metabolic profile of cumulus-oocyte complexes (COCs) during maturation. The aim of this study was to determine the differential participation of enzymatic activity in cumulus cells and the oocyte during in vitro maturation of bovine oocytes, by measuring the activity of key enzymes involved in the regulation of glycolysis (phosphofructokinase), the pentose phosphate pathway (glucose-6-phosphate dehydrogenase) and lipolysis (lipase). COCs were matured in medium 199 plus 10% (v/v) steer serum for 22-24 h at 39 degrees C in 5% CO(2):95% humidified air. Phosphofructokinase, glucose-6-phosphate dehydrogenase and lipase activities were measured in immature and in vitro matured COCs, denuded oocytes and cumulus cells, respectively. Phosphofructokinase and glucose-6-phosphate dehydrogenase activities (enzymatic units) remained constant during in vitro maturation of COCs, but there was a significant decrease in lipase activity (units) (P < 0.05), as activity in cumulus cells decreased significantly (P < 0.05). For the three enzymes studied, enzyme activity (units) remained unchanged in the oocyte during in vitro maturation. Specific activity increased in the oocyte (P < 0.05) and decreased in cumulus cells as a result of maturation (P < 0.05). In cumulus cells, phosphofructokinase was the most abundant of the three enzymes followed by glucose-6-phosphate dehydrogenase and then lipase (P < 0.05), whereas in the denuded oocyte this order was reversed (P < 0.05). Thus, the metabolism of cumulus cells is adapted to control the flow of metabolites toward the oocyte, which maintains its enzymatic activity even when dissociated from cumulus cells during maturation. The high activity of phosphofructokinase in cumulus cells indicates that glucose is metabolized mainly via the glycolytic pathway in these cells. The greater relative activity of glucose-6-phosphate dehydrogenase recorded in the oocyte indicates that glucose uptake could be directed mainly toward the pentose phosphate pathway. The marked lipolytic activity concentrated in the oocyte indicates an active participation in lipid catabolism during maturation.

scholarly journals Antioxidant SMe1EC2 modulates pentose phosphate pathway and glutathione-dependent enzyme activities in tissues of aged diabetic rats

2017 ◽  
Vol 10 (4) ◽  
pp. 148-154 ◽  
Author(s):  
Nuray Nuriye Ulusu ◽  
Müslüm Gök ◽  
Arzu Ayşe Sayin Şakul ◽  
Nuray Ari ◽  
Milan Stefek ◽  
...  
Keyword(s):  
Pentose Phosphate Pathway ◽  
Enzyme Activities ◽  
Body Weight Loss ◽  
Diabetic Rats ◽  
Pentose Phosphate ◽  
Aged Rats ◽  
Glutathione S Transferase ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
And Control

Abstract The pentose phosphate pathway and glutathione-associated metabolism are the main antioxidant cellular defense systems. This study investigated the effects of the powerful antioxidant SMe1EC2 (2-ethoxycarbonyl-8-methoxy-2,3,4,4a,5,9b-hexahydro-1H-pyrido[4,3-b] indolinium dichloride) on pentose phosphate pathway (PPP) and glutathione-dependent enzyme activities in aged diabetic and aged matched control rats. Diabetes was induced by streptozotocin injection in rats aged 13-15 months. Diabetic and control rats were divided into two subgroups, one untreated and one treated with SMe1EC2 (10 mg/kg/day, orally) for 4 months. SMe1EC2 ameliorated body weight loss, but not hyperglycemia of aged diabetic rats. Diabetes resulted in decreased glucose-6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD) and glutathione-S-transferase (GST), yet in unchanged glutathione reductase (GR) in the liver of aged diabetic rats. In the liver of the aged control rats, SMe1EC2 did not affect G6PDH, 6PGDH and GR, but it inhibited GST. SMe1EC2 also failed to affect diabetes-induced decline in 6PGDH, it ameliorated G6PDH but produced further decline in GST in the liver of aged diabetic rats. In the kidney of aged rats, G6PDH and GST were found to be comparable among the groups, but diabetes up-regulated 6PGDH and GR; these alterations were prevented by SMe1EC2. In the heart of aged diabetic rats, while GST remained unchanged, the recorded increase in G6PD, 6PGD, GR was prevented by SMe1EC2. Furthermore, an unchanged GR and remarkable increases in G6PD, 6PGD and GST were found in the lung of the aged diabetic group. These alterations were completely prevented by SMe1EC2. The results suggest that in aged rats SMe1EC2 can ameliorate the response of the kidney, heart and lung but not that of the liver against diabetes-induced glucotoxicity by interfering with the activity of redox network enzymes.

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