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PubMed1999

Fitness of wild-caught Drosophila melanogaster females: allozyme variants of GPDH, ADH, PGM, and EST.

We have collected several hundred Drosophila melanogaster flies (near Davis, California), isolated them individually, without anesthesia, at the collecting site, and estimated the fitness components of the wild-caught females under different environmental conditions. The fitness parameters measured are fecundity, oviposition rate, and productivity (egg-to-adult viability, development rate, and number of progeny). The environmental variables are two temperatures (22 degrees C and 28 degrees C) and two densities ('scant' and 'crowded'). After the fitness measurements are completed for each individual female, its genotype is determined at four loci encoding enzymes: GPDH and ADH, located on chromosome II; and PGM and EST-C, located on chromosome III. Density has a large significant effect on productivity; temperature has significant effects on fecundity, oviposition rate, and development rate. The experiments show that allozyme polymorphisms are associated with selection effects. Fitness differences between allozyme genotypes occur for all fitness components, except oviposition rate. But which genotype is superior depends on the environmental conditions; heterozygotes exhibit higher fitness than homozygotes in a number of cases, but inferior in others. A unique feature of the present experiments is that the experimental flies are wild-caught females rather than laboratory-bred individuals.

Alcohol Dehydrogenase↗
PubMed1992

Interaction between the Adh and alpha Gpdh loci in Drosophila melanogaster: adult survival at high temperature.

The role of high temperature resistance in the world-wide cline of Adh and alpha Gpdh allele frequencies of Drosophila melanogaster was investigated. Experimental strains were used with different combinations of Adh and alpha Gpdh alleles but with similar genetic background. The survival time of adult males, reared at different pre-adult temperatures, was measured at 35 degrees C. To investigate the relationship between survival and protein content, triglycerides content and ADH and alpha GPDH enzyme activity, the latter characters were measured before and after 12 h exposure to 35 degrees C. Three-way ANOVA of survival at 35 degrees C showed significant effects of rearing temperature and Adh genotype, interaction between Adh and alpha Gpdh, interaction between Adh and rearing temperature and interaction between Adh, alpha Gpdh and rearing temperature, alpha GPDH enzyme activity did not change significantly. Although protein content, triglycerides content and ADH enzyme activity decreased significantly at 35 degrees C, no correlation was observed between survival and these traits. It is concluded that the world-wide cline of Adh and alpha Gpdh allele frequencies cannot simply be explained by the genotypic differences in resistance to high temperature of adult Drosophila melanogaster.

Alcohol Dehydrogenase↗
PubMed1989

Gene expression in adult metafemales of Drosophila melanogaster.

The expression of selected X-linked and autosomal genes was examined in metafemales (3X:2A) compared to diploid sisters. Three enzyme activities (glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, beta-hydroxyacid dehydrogenase) encoded by X-linked genes are not significantly different in the two classes of flies. In contrast, three autosomally encoded enzyme activities (alcohol dehydrogenase, alpha-glycerophosphate dehydrogenase, isocitrate dehydrogenase) are reduced in metafemales. Protein and DNA comparisons between metafemales and diploid sisters show a lowered level of total protein whereas the total DNA measurements are similar. Thus, the total cell number in metafemales is basically unchanged but gene expression is reduced. Phenotypic analysis of three autosomal loci, glass (gl), purple (pr) and pink-peach (pp), show that all three have lowered expression in metafemales while the X-linked loci, white-apricot (wa) and Bar (B), are dosage compensated. Quantitative dot blot analysis of messenger RNA levels of the second chromosomal locus, alcohol dehydrogenase (Adh), and the X chromosomal locus, rudimentary (r), show that Adh has reduced expression and r is partially compensated per total RNA in metafemales. It is proposed that the increased dosage of the X chromosome inversely affects both the X and autosomal gene expression but the simultaneous increased dosage of the structural genes on the X results in dosage compensation. The reduced levels of expression of autosomal genes could contribute to the great inviability of metafemales.

Alcohol Dehydrogenase↗
PubMed1990

[Influence of thyroid status on microsomal and peroxysomal enzyme induction by fibrates in rats].

The influence of thyroid hormones upon the inductive effects on microsomal enzymes and the hepatic proliferation produced by different fibrates was studied in the male rat. A pharmacological dose of triiodo-L-thyronine significantly lowers the total cytochrome P450 content induced by some equi-effective doses of clofibrate, ciprofibrate, bezafibrate and fenofibrate. The ethoxycoumarin O-deethylase activity (ECOD) is concomitantly decreased. On the contrary, L-T3 accentuates the specific inductive effect of fibrates on bilirubin-UDPGT activity. Hypothyroid has little or no influence upon the effect of fibrates towards cytochrome P450 content and ECOD activity. On the other hand, this thyroid status significantly lowers the CN- palmitoyl coenzyme A dehydrogenase, which is a marker enzyme of the peroxisome proliferation caused by the different fibrates. These results indicate a possible modulation of thyroid hormones within the fibrates induction mechanism in the rat.

Acyl-CoA Dehydrogenase↗
PubMed2000

[The key enzymes of metabolisms of glycerol in Candida glycerolgenesis].

The specific enzymes for glycerol formation and dissimilation in Candida glycerolgenesis were studied. C. glycerolgenesis hardly assimilated glycerol without glucose and a little amount of glucose remarkably stimulated this dissimilation pathway and the activity and expression of mitochondrial glycerol-3-phosphate dehydrogenase was induced strongly by glycerol-3-phosphate and repressed by glucose metabolism. During glycerol production fermented by C. glycerolgenesis, the activity of cytoplasmic glycerol 3-phosphate dehydrogenase maintained at a higher level and existed two peaks of activity, which appeared at 36 h and 60 h, respectively. The activity level of the first activity peak determines glycerol productivity and becomes a key enzyme of glycerol formation. The activity of glycerol 3-phosphatase maintained at a higher level just between 18 h and 48 h and appeared on peak activity at 36 h. In that period, the activity of glycerol 3-phosphatase was up to more than two times of cytoplasmic glycerol 3-phosphate dehydrogenase and that was inosculated with the phase of rapid accumulation of glycerol during glycerol production by C. glycerolgenesis. In the phase of slowly accumulation of glycerol between 48 h and 72 h, the activity of glycerol 3-phosphatase decreased below that of cytoplasmic glycerol 3-phosphate dehydrogenase. So, cytoplasmic glycerol 3-phosphate dehydrogenase is a key enzyme of glycerol formation in the phase of rapid accumulation of glycerol and glycerol 3-phosphatase becomes a more effective factor after glycerol fermentation reached into slowly accumulation phase. In a conclusion, it is a fundamental for C. glycerolgenesis over-producing high level of glycerol that its cytoplasmic glycerol 3-phosphate dehydrogenase maintains at high activity and the activity of glycerol 3-phosphatase is much higher than that of cytoplasmic glycerol 3-phosphate dehydrogenase.

Candida↗