Drosophila lactate dehydrogenase and α-glycerolphosphate dehydrogenase: Distribution and change in activity during development

Rechsteiner, Martin

doi:10.1016/0022-1910(70)90208-8

Cited by 109 publications

(56 citation statements)

References 12 publications

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“…An analogous role of a GPDH in the regulation of NAD + /NADH ratios in larval tissues is proposed by several authors (e.g. Rechsteiner, 1970;Geer et a!., 1983). Further a GPDH converts dihydroxyacetone phosphate to glycerophosphate, a precursor for phospholipids and triglycerides (O'Brien and MacIntyre, 1978;Geer eta!., 1983).…”

Section: Discussionmentioning

confidence: 58%

Polymorphism at the Adh and αGpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters

et al. 1991

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The role of developmental time in the world-wide dine of Adh and a Gpdh allele frequencies of Drosophila melanogaster, and the relationship with weight and some biochemical characters, were investigated. Experimental strains were constructed with different combinations of Adh and aGpdh alleles but with similar genetic background. Developmental time, adult weight, protein-and triglyceride-content, and ADH and aGPDH enzyme activity were measured at a rearing temperature of 20, 25 and 29°C. Genotype effects were found in all studied characters. In general the developmental times of genotypes were: Ad/IFF < Adh' a GpdhFS = aGpdhSS. Developmental time and adult weight were strongly affected by rearing temperature.Triglyceride content and ADFI and a GPDH enzyme activity were slightly affected by temperature. Interactions between genotype and temperature effects were found for developmental rate, adult weight and protein content. No trade off was observed between developmental time on the one hand and adult weight, protein-and triglyceride-content, and ADH and a GPDH enzyme activity on the other hand. It is argued that developmental rate differences might be one of the underlying mechanisms of the world-wide dine of the Adh and a GPdh allele frequencies.Keywords: Adh, a Gpdh, developmental time, Drosophila melanogaster, temperature, weight. IntroductionThe alcohol dehydrogenase (Adh) and a-glycerophosphate dehydrogenase (a Gpdh) loci are two of the most extensively studied allozyme systems of Drosophila melanogaster. They provide an excellent opportunity to study interactions between physiological effects of gene-enzyme systems. Both loci have two common electrophoretic alleles: AdhF, Adhs, aGpdh' and aGpdhS. Nearly all natural populations are polymorphic for both loci. The frequencies of these alleles show world-wide clinal variation: the frequencies of Adhs and aGpdhF decrease with increasing latitude (Oakeshott et al., 1982). An important question is whether these dines are under the control of natural selection. Correlation analysis of climatic data revealed no consistent significant correlations (Anderson et a!., 1987). In the laboratory, stress from alcohol or temperature can cause differential selection of Adh and aGpdh alleles (e.g. Van Delden, 1982; Zera et a!., 1985). Under normal laboratory conditions equilibrium selection has been demonstrated for Adh (Bijisma-Meeles & Bijlsma, 1988) and aGpdh (Palabost-Charles, 1980). Selection at temperatures between 25 and 30°C may lead to an increase of the Adhs and aGpdh' alleles (Alahiotis, 1982;Van Delden, 1984). Vigue et al. (1982) and Oakeshott et al. (1985), however, found no effect of temperature on Adh or aGpdh allele frequencies. Van Delden (1984) and Van Delden & Kamping (1989) ascribe the advantage of the Adhs and aGpdhF alleles at a higher temperature, for the greater part, to linkage of both alleles with the inversion In(2L)t.Differences in developmental time between genotypes may be an important underlying mechanism of selection. D...

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Section: Discussionmentioning

confidence: 58%

Polymorphism at the Adh and αGpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters

et al. 1991

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“…16 The two major isozymes in D. melanogaster, GPDH-1 and GPDH-3, exhibit a differential tissue distribution in adults and a different temporal expression throughout development. [17][18][19] Each isozyme performs a distinct metabolic function: GPDH-1 is involved in the flight muscle metabolism. GPDH-2 and GPDH-3 provide precursor for lipid biosynthesis in the gonads, fat bodies, and abdomen in larvae and nymphs.…”

Section: Introductionmentioning

confidence: 99%

“…GPDH-2 and GPDH-3 provide precursor for lipid biosynthesis in the gonads, fat bodies, and abdomen in larvae and nymphs. 18,20 In T. infestans, it was demonstrated that GPDH involved in the glycerophosphate shuttle increases its activity 30-fold in adult thoracic muscles. 21 Triatoma infestans adult muscles should have higher glycolytic and respiratory capacity to support fly activity.…”

Section: Introductionmentioning

confidence: 99%

Differential Expression of Glycerol-3-Phosphate Dehydrogenase Isoforms in Flight Muscles of the Chagas Disease Vector Triatoma infestans (Hemiptera, Reduviidae)

Stroppa

Lagunas²,

Carriazo³

et al. 2013

The American Journal of Tropical Medicine and Hygiene

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Abstract. Flight muscles of Triatoma infestans have two glycerol-3-phosphate dehydrogenase (GPDH) isoforms: GPDH-1 is involved in flight metabolism and GPDH-2 provides lipid precursors. Total GPDH activity was greater in the natural population and almost only due to GPDH-1. Different expression and activity observed between GPDH isoforms in the natural population and the first laboratory generation was not detected in the second laboratory generation. This pattern may be caused by gradual adaptation to laboratory nutritional conditions. During development, the expression of GPDH-2 increased with a longer time of intake, which would imply an increment in lipid biosynthesis. The GPDH-1 transcript predominated with respect to that of GPDH-2 in the lower nutritional condition, suggesting the necessity of insects to fly during this nutritional status. The transcriptional pattern showed a delay at 22 C. The isoforms activities and transcript patterns in flight muscles suggest transcriptional adaptation to metabolic requirements originated by alternative splicing.

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“…The assay for LDH was developed with larvae, because Drosophila adults have very little, if any, LDH (21). 100 mg of larvae were homogenized in a ground-glass tissue grinder in 0.5 ml 0.05 Na pyrophosphate, pH 8.3.…”

Section: Malate Dehydrogenase (Mdh)mentioning

confidence: 99%

“…LDH is the enzyme used in mammalian systems to generate cytoplasmic NADH. In Drosophila, LDH is present in large amounts in larvae but is virtually absent in adults (21,28). This enzyme, if reexpressed in adults, could compensate for the aGPdh-I B° mutations.…”

Section: Search For Molecular Compensation For Agpdh-1 ~° Mutationsmentioning

confidence: 99%

THE α-GLYCEROPHOSPHATE CYCLE IN DROSOPHILA MELANOGASTER

O’Brien

Shimada

1974

The Journal of Cell Biology

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ABSTRACT"Null" mutations previously isolated at the aGpdh-1 locus of Drosophila rnelanogaster, because of disruption of the energy-producing a-glycerophosphate cycle, severely restrict the flight ability and relative viability of affected individuals.Two "null" alleles, aGpdh-18°-1-4, and otGpdh-1 ~°-~-5, when made hemizygous with a deficiency of the aGpdh-I locus, Df(2L)Gdh,4, were rendered homozygous by recombination with and selective elimination of the Dfl2L)GdhA chromosome. After over 25 generations, a homozygous aGpdh-1 ~°-1-4 stock regained the ability to fly despite the continued absence of measurable aGPDH activity. Inter se heterozygotes of three noncomplementing aGpdh-1 "null" alleles and the "adapted" aGpdh-1 B°-'-~ homozygotes were examined for metabolic enzymatic activities related to the energy-producing and pyridine nucleotide-regulating functions of the o~-glycerophosphate cycle in Drosophila. The enzyme functions tested included glyceraldehyde-3-phosphate dehydrogenase, cytoplasmic and soluble malate dehydrogenase, lactate dehydrogenase, mitochondrial NADH oxidation, oxidative phosphorylation, and respiratory control with the substrates a-glycerophosphate, succinate, and pyruvate. These activities in any of the mutant genotypes in early adult life were indistinguishable from those in the wild type. There was, however, a premature deterioration and atrophy of the ultrastructural integrity of flight muscle sarcosomes observed by electron microscopy in the "null" mutants. These observations were correlated with a decrease in state 3 mitochondrial oxidation with a-glycerophosphate, succinate, and pyruvate, as well as with loss of respiratory control in adults as early as 2 wk after eclosion. Such observations, which normally are seen in aged dipterans, were accompanied by premature mortality of the mutant heterozygotes. The adapted aGpdh-I B°-14 was identical with wild type in each of the aging characters with the single exception of lowered rates of mitochondrial oxidative phosphorylation.

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Drosophila lactate dehydrogenase and α-glycerolphosphate dehydrogenase: Distribution and change in activity during development

Cited by 109 publications

References 12 publications

Polymorphism at the Adh and αGpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters

Polymorphism at the Adh and αGpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters

Differential Expression of Glycerol-3-Phosphate Dehydrogenase Isoforms in Flight Muscles of the Chagas Disease Vector Triatoma infestans (Hemiptera, Reduviidae)

THE α-GLYCEROPHOSPHATE CYCLE IN DROSOPHILA MELANOGASTER

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