scholarly journals Lactate dehydrogenase and glycerol-3-phosphate dehydrogenase cooperatively regulate growth and carbohydrate metabolism during Drosophila melanogaster larval development

Development ◽  
2019 ◽  
Vol 146 (17) ◽  
pp. dev175315 ◽  
Author(s):  
Hongde Li ◽  
Madhulika Rai ◽  
Kasun Buddika ◽  
Maria C. Sterrett ◽  
Arthur Luhur ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Lactate Dehydrogenase ◽  
Larval Development ◽  
Carbohydrate Metabolism ◽  
Glycerol 3 Phosphate Dehydrogenase

scholarly journals Lactate and glycerol-3-phosphate metabolism cooperatively regulate growth and redox balance during Drosophila melanogaster larval development

2019 ◽  
Author(s):  
Hongde Li ◽  
Kasun Buddika ◽  
Maria C. Sterrett ◽  
Cole R. Julick ◽  
Rose C. Pletcher ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Larval Development ◽  
Carbohydrate Metabolism ◽  
Synthetic Lethality ◽  
Aerobic Glycolysis ◽  
Redox Balance ◽  
Coordinate Regulation ◽  
Metabolic Robustness ◽  
Dramatic Growth

ABSTRACTThe dramatic growth that occurs during Drosophila larval development requires rapid conversion of nutrients into biomass. Many larval tissues respond to these biosynthetic demands by increasing carbohydrate metabolism and lactate dehydrogenase (dLDH) activity. The resulting metabolic program is ideally suited to synthesize macromolecules and mimics the manner by which cancer cells rely on aerobic glycolysis. To explore the potential role of Drosophila dLDH in promoting biosynthesis, we examined how dLdh mutations influence larval development. Our studies unexpectantly found that dLdh mutants grow at a normal rate, indicating that dLDH is dispensable for larval biomass production. However, subsequent metabolomic analyses suggested that dLdh mutants compensate for the inability to produce lactate by generating excess glycerol-3-phosphate (G3P), the production of which also influences larval redox balance. Consistent with this possibility, larvae lacking both dLDH and G3P dehydrogenase (GPDH1) exhibit developmental delays, synthetic lethality, and aberrant carbohydrate metabolism. Considering that human cells also generate G3P upon Lactate Dehydrogenase A (LDHA) inhibition, our findings hint at a conserved mechanism in which the coordinate regulation of lactate and G3P synthesis imparts metabolic robustness upon growing animal tissues.

scholarly journals Role of glycerol 3-phosphate dehydrogenase in glyceride metabolism. Effect of diet on enzyme activities in chicken liver

1975 ◽  
Vol 146 (1) ◽  
pp. 223-229 ◽  
Author(s):  
J W Harding ◽  
E A Pyeritz ◽  
E S Copeland ◽  
H B White
Keyword(s):  
Lactate Dehydrogenase ◽  
High Fat Diet ◽  
Acyl Carrier Protein ◽  
Fatty Acid Synthetase ◽  
Carrier Protein ◽  
High Fat ◽  
Carbohydrate Diet ◽  
Metabolic Role ◽  
Glycerol 3 Phosphate Dehydrogenase

1. The metabolic role of hepatic NAD-linked glycerol 3-phosphate dehydrogenase (EC 1.1.1.8) was investigated vis-a-vis glyceride synthesis, glyceride degradation and the maintainence of the NAD redox state. 2. Five-week-old chickens were placed on five dietary regimes: a control group, a group on an increased-carbohydrate-lowered-fat diet, a group on a high-fat-lowered-carbohydrate diet, a starved group and a starved-refed group. In each group the specific activity (mumol/min per g wet wt. of tissue) of hepatic glycerol 3-phosphate dehydrogenase was compared with the activities of the β-oxoacyl-(acyl-carrier protein) reductase component of fatty acid synthetase, glycerol kinase (EC 2.7.1.30) and lactate dehydrogenase (EC 1.1.1.27). 3. During starvation, the activities of glycerol 3-phosphate dehydrogenase, glycerol kinase and lactate dehydrogenase rose significantly. After re-feeding these activities returned to near normal. All three activities rose slightly on the high-fat diet. Lactate dehydrogenase activity rose slightly, whereas those of the other two enzymes fell slightly on the increased-carbohydrate-lowered-fat diet. 4. The activity of the β-oxoacyl-(acyl-carrier protein) reductase component of fatty acid synthetase, a lipid-synthesizing enzyme, contrasted strikingly with the other three enzyme activities. Its activity was slightly elevated on the increased-carbohydrate diet and significantly diminished on the high-fat diet and during starvation. 5. The changes in activity of the chicken liver isoenzyme of glycerol 3-phosphate dehydrogenase in response to dietary stresses suggest that the enzyme has an important metabolic role other than or in addition to glyceride biosynthesis.

scholarly journals Peculiarities of Carbohydrate Exchange in Patients with Generalized Periodontitis of Young Age Persons

2018 ◽  
Vol 25 (2) ◽  
Author(s):  
Halyna Kimak ◽  
Halyna Melnychuk ◽  
Hanna Ersteniuk
Keyword(s):  
Lactic Acid ◽  
Lactate Dehydrogenase ◽  
Carbohydrate Metabolism ◽  
Young Patients ◽  
Young Age ◽  
Lactate Dehydrogenase Activity ◽  
Significant Difference ◽  
Oral Liquid ◽  
Lactate Levels ◽  
Healthy Persons

There were studied 92 somatically healthy persons of young age (18-25 years old), with generalized periodontitis (GP) of initial-I degree of development, among them: 30 patients with chronic generalized periodontitis (CGP), who were included into group І; and 32 patients with exacerbation of the chronic generalized periodontitis (ECGP) – into group II; and 30 healthy patients. The carbohydrate metabolism indexes were studied, namely: the content of glucose, pyruvate (pyruvic acid) and lactate (lactic acid) and lactate dehydrogenase activity (LDG) in the oral liquid.We have determined that in the presence of CGP of the initial-I degree of development, and especially in its exacerbation, there is a significant increase of indicators of carbohydrate metabolism. In young patients with CGP indicators of glucose, pyruvate, lactate and LDG activity in the oral liquid increased by 2.0, 1.34, 1.58 and 1.37 (p<0.001, p<0.01) times respectively, and in case of ECGP they grew even more: by 2.71, 1.98, 1.76 and 2.07 (p<0.001) times, respectively.Among all the indicators, that characterize the carbohydrate metabolism, in addition to the level of pyruvate, in case of different course of GP a significant difference was revealed: in patients with ECGP compared with the data in CGP, glucose and lactate levels and LDG activity in the oral liquid were significantly higher - at 35.75% (p<0.05), 34.29% (p<0.01) and 36.59% (p<0.001) respectively.Detected violations of carbohydrate metabolism indeces in the oral liquid indicate the involvement of these processes in the pathogenesis of GP and the necessity of their correction. 

scholarly journals Combining metabolomics and experimental evolution reveals key mechanisms underlying longevity differences in laboratory evolved Drosophila melanogaster populations

2021 ◽  
Author(s):  
Mark Phillips ◽  
Kenneth R. Arnold ◽  
Zer Vue ◽  
Heather Beasley ◽  
Edgar Garza Lopez ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Carbohydrate Metabolism ◽  
Experimental Evolution ◽  
Statistical Power ◽  
Accelerated Aging ◽  
Experimental System ◽  
Tca Cycle ◽  
Dna And Rna ◽  
Metabolomic Data ◽  
Genetic Mechanisms

Experimental evolution with Drosophila melanogaster has been used extensively for decades to study aging and longevity. In recent years, the addition of DNA and RNA sequencing to this framework has allowed researchers to leverage the statistical power inherent to experimental evolution study the genetic basis of longevity itself. Here we incorporated metabolomic data into to this framework to generate even deeper insights into the physiological and genetic mechanisms underlying longevity differences in three groups of experimentally evolved D. melanogaster populations with different aging and longevity patterns. Our metabolomic analysis found that aging alters mitochondrial metabolism through increased consumption of NAD+ and increased usage of the TCA cycle. Combining our genomic and metabolomic data produced a list of biologically relevant candidate genes. Among these candidates, we found significant enrichment for genes and pathways associated with neurological development and function, and carbohydrate metabolism. While we do not explicitly find enrichment for aging canonical genes, neurological dysregulation and carbohydrate metabolism are both known to be associated with accelerated aging and reduced longevity. Taken together, our results in total provide very plausible genetic mechanisms for what might be driving longevity differences in this experimental system. More broadly, our findings demonstrate the value of combining multiple types of omic data with experimental evolution when attempting to dissect mechanisms underlying complex and highly polygenic traits like aging.

scholarly journals Re-evaluation of the glycerol-3-phosphate dehydrogenase/l-lactate dehydrogenase enzyme system. Evidence against the direct transfer of NADH between active sites

1991 ◽  
Vol 278 (3) ◽  
pp. 875-881 ◽  
Author(s):  
S P J Brooks ◽  
K B Storey
Keyword(s):  
Lactate Dehydrogenase ◽  
Active Sites ◽  
Reaction Rate ◽  
Experimental Results ◽  
Transfer Model ◽  
Rabbit Muscle ◽  
Direct Transfer ◽  
Theoretical Predictions ◽  
Glycerol 3 Phosphate Dehydrogenase

An investigation of the direct transfer of metabolites from rabbit muscle L-lactate dehydrogenase (LDH, EC 1.1.1.27) to glycerol-3-phosphate dehydrogenase (GPDH, EC 1.1.1.8) revealed discrepancies between theoretical predictions and experimental results. Measurements of the GPDH reaction rate at a fixed NADH concentration and in the presence of increasing LDH concentrations gave experimental results similar to those previously obtained by Srivastava, Smolen, Betts, Fukushima, Spivey & Bernhard [(1989) Proc. Natl. Acad. Sci. U.S.A. 86, 6464-6468]. However, a mathematical solution of the direct-transfer-mechanism equations as described by Srivastava et al. (1989) showed that the direct-transfer model did not adequately describe the experimental behaviour of the reaction rate at increasing LDH concentrations. In addition, experiments designed to measure the formation of an LDH4.NADH.GPDH2 complex, predicted by the direct-transfer model, indicated that no significant formation of tertiary complex occurred. An examination of other kinetic models, developed to describe the LDH/GPDH/NADH system better, revealed that the experimental results may be best explained by assuming that free NADH, and not E1.NADH, is the sole substrate for GPDH. These results suggest that direct transfer of NADH between rabbit muscle LDH and GPDH does not occur in vitro.

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