Disease relevance of Gpdh

• In situ hybridization of this clone to the polytene chromosomes of wild type flies and flies bearing chromosomal aberrations that delimit the Gpdh+ locus have allowed us to decisively place the gene in the distal region of 26A on the left arm of the second chromosome [1].
• Polymorphism at the Adh and alpha Gpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters [2].

High impact information on Gpdh

• I review the evolution of two genes, Gpdh and Sod [3].
• The process of transcript terminus formation inside the retrotransposon insertion reduces the level of the Gpdh transcript that contains exon 8 and increases the level of the transcript that contains exons 1-7 [4].
• Retrotransposon insertion induces an isozyme of sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster [4].
• To understand the underlying molecular basis of these isoforms, we have sequenced a 5.8-kilobase region of the Drosophila genome that contains the entire Gpdh locus [5].
• Two other enzyme loci exhibited a correlated variation with Adh-F--i.e., an increase of the S allele of glycerol-3-phosphate dehydrogenase (NAD+) (sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase, EC 1.1.1.8) and of the F allele of glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADP+ 1-oxidoreductase, EC 1.1.1.49) [6].

Biological context of Gpdh

• Predicted Adh and Gpdh equilibrium allele frequencies were consistent with those found in adjacent free-living populations [7].
• For both Adh and Gpdh, nonzero selection coefficients were estimated that were homogeneous across populations and indicated heterozygote advantage [7].
• A distinctive and geographically widespread category of low-activity variant at the Gpdh locus in Drosophila melanogaster is shown to have defective P elements inserted between the TATA box and the transcription start site [8].
• RNase protection mapping and comparison of the genomic sequence from three different cDNA clones reveal that three protein isoforms of glycerol-3-phosphate dehydrogenase are produced by alternative processing of 3' exons [5].
• Drosophila sn-glycerol-3-phosphate dehydrogenase isozymes are generated by alternate pathways of RNA processing resulting in different carboxyl-terminal amino acid sequences [9].

Anatomical context of Gpdh

• The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria [10].
• We have compared the DNA sequence of the 5'-flanking region of the aP2 gene to the promoter regions of two other genes activated during adipocyte differentiation, glycerol-3-phosphate dehydrogenase and adipsin, and find a 13-base region of homology (Formula: see text) present in multiple copies in the 5'-flanking region of each gene [11].
• Xenopus laevis oocytes injected with poly(A)+ RNA isolated from Drosophila melanogaster direct the synthesis of catalytically active glycerol-3-phosphate dehydrogenase (NAD+) (EC 1.1.1.8) [12].
• However, the concentration of GPDH in the thorax greatly exceeds that found in the abdomen [13].
• The principle GPDH-containing tissue of larvae is fat body [13].

Associations of Gpdh with chemical compounds

• In flight muscle, there is only one GPDH isoform, GPDH-1, which is distinguished from isoforms found in other tissues by having three C-terminal amino acids: glutamine, asparagine, and leucine [14].
• GPDH activity and transcript abundance increased in response to ethanol and additional amounts of several different carbohydrates [15].
• In Drosophila, multiple isoforms of alpha-glycerol-3-phosphate dehydrogenase (sn-glycerol-3-phosphate: NAD+ 2-oxidoreductase, EC 1.1.1.8) are produced in a tissue- and stage-specific manner [5].
• We observe small but statistically significant reductions in triglyceride content for adult Gpdh genotypes possessing 33-80% reductions from normal activity [16].
• Glycerol 3-phosphate dehydrogenase and center o of complex III in the presence of antimycin had the greatest maximum capacities to generate superoxide on the cytosolic side of the inner membrane [17].

Physical interactions of Gpdh

• Conserved (CT)n.(GA)n repeats in the non-coding regions at the Gpdh locus are binding sites for the GAGA factor in drosophila melanogaster and its sibling species [18].

Other interactions of Gpdh

• Effect of dietary carbohydrates and ethanol on expression of genes encoding sn-glycerol-3-phosphate dehydrogenase, aldolase, and phosphoglycerate kinase in Drosophila larvae [15].
• However, McDonald-Kreitman tests based on intraspecific gene comparisons indicate that positive selection on amino acids has accompanied Est-5 gene duplication and divergence in D. pseudoobscura [19].
• Fitness of wild-caught Drosophila melanogaster females: allozyme variants of GPDH, ADH, PGM, and EST [20].
• Nevertheless, adult alphaGPDH, and larval IDH and 6PGDH activities exhibited significant differences between the two populations [21].
• The position of the alpha-glycerophosphate dehydrogenase (alpha-Gpdh) gene in 26A5-7 has been confirmed and a putative transcriptional unit for the beta-galactosidase-1 (beta-Gal-1) gene has been identified in the 26A7-9 interval [22].

Analytical, diagnostic and therapeutic context of Gpdh

• Survey of the Gpdh gene region by the Southern blot analysis revealed the following features of this gene duplication: (1) The duplication was not observed in chromosome lines that carry In(2L)t, a cosmopolitan chromosomal inversion in this species [23].
• Cloning and sequence analysis of Gpdh in Callosobruchus chinensis (Coleoptera: Bruchidae) [24].
• The gene was obtained by screening a genomic library with Drosophila melanogaster Gpdh and PCR amplification [24].
• Null and low activity alleles at the genetic locus coding for L-Glycerol-3-phosphate dehydrogenase (alpha-GPDH, NAD+ oxidoreductase, E.C. 1.1.1.8) in Drosophila melanogaster have been analyzed by a combination of rocket immunoelectrophoresis, interallelic complementation, and two-dimensional gel electrophoresis [25].
• Mutants which express no apparent alpha-GPDH activity were analyzed by two-dimensional gels and immunoelectrophoresis in an attempt to identify and characterize the inactive proteins [26].

References