Low protein to carbohydrate ratio diet delays onset of Parkinsonism like phenotype in Drosophila melanogaster parkin null mutants

2016 ◽  
Vol 160 ◽  
pp. 19-27 ◽  
Author(s):  
Rijan Bajracharya ◽  
J. William O. Ballard
Keyword(s):  
Drosophila Melanogaster ◽  
Low Protein ◽  
Null Mutants

A genetic analysis of the alpha-glycerophosphate oxidase locus in Drosophila melanogaster.

Genetics ◽  
1988 ◽  
Vol 120 (3) ◽  
pp. 755-766
Author(s):  
M B Davis ◽  
R J MacIntyre
Keyword(s):  
Drosophila Melanogaster ◽  
Genetic Analysis ◽  
Structural Gene ◽  
Mitochondrial Enzyme ◽  
Synthetic Lethal ◽  
Lethal Phenotype ◽  
Cytoplasmic Enzyme ◽  
Glycerophosphate Dehydrogenase ◽  
Null Mutants

Abstract The gene for alpha-glycerophosphate oxidase, the nuclear encoded mitochondrial enzyme of the alpha-glycerophosphate cycle (alpha GP); has been mapped in Drosophila melanogaster. Several interstitial deficiencies in region 50c-53AB of chromosome 2R were used to localize the structural gene to 52D2-5. In addition, mutations of alpha GPO were generated; alpha GPO mutants are viable yet flightless. Interactions of alpha GPO with alpha-glycerophosphate dehydrogenase (alpha GPDH), the cytoplasmic enzyme of the alpha GP cycle, were investigated through the synthesis of a series of alpha GPDHnull-alpha GPOnull double mutants. Of the six double null mutants constructed, four alpha GPDH-alpha GPO double nulls are viable and flightless. Two double mutants, however, exhibit an allelic-dependent synthetic lethal phenotype.

scholarly journals Drosophila melanogaster Scramblases modulate synaptic transmission

2006 ◽  
Vol 173 (1) ◽  
pp. 69-82 ◽  
Author(s):  
Usha Acharya ◽  
Michael Beth Edwards ◽  
Ramon A. Jorquera ◽  
Hugo Silva ◽  
Kunio Nagashima ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Synaptic Transmission ◽  
Blood Cells ◽  
Neuromuscular Synapses ◽  
Neurotransmitter Secretion ◽  
Reserve Pool ◽  
Null Mutants

Scramblases are a family of single-pass plasma membrane proteins, identified by their purported ability to scramble phospholipids across the two layers of plasma membrane isolated from platelets and red blood cells. However, their true in vivo role has yet to be elucidated. We report the generation and isolation of null mutants of two Scramblases identified in Drosophila melanogaster. We demonstrate that flies lacking either or both of these Scramblases are not compromised in vivo in processes requiring scrambling of phospholipids. Instead, we show that D. melanogaster lacking both Scramblases have more vesicles and display enhanced recruitment from a reserve pool of vesicles and increased neurotransmitter secretion at the larval neuromuscular synapses. These defects are corrected by the introduction of a genomic copy of the Scramb 1 gene. The lack of phenotypes related to failure of scrambling and the neurophysiological analysis lead us to propose that Scramblases play a modulatory role in the process of neurotransmission.

scholarly journals THE α-GLYCEROPHOSPHATE IN DROSOPHILA MELANOGASTER II. GENETIC ASPECTS

Genetics ◽  
1972 ◽  
Vol 71 (1) ◽  
pp. 127-138
Author(s):  
Stephen J O'Brien ◽  
Ross J Macintyre
Keyword(s):  
Drosophila Melanogaster ◽  
Energy Production ◽  
Null Alleles ◽  
Electrophoretic Variant ◽  
Electrophoretic Variants ◽  
Glycerophosphate Dehydrogenase ◽  
Naturally Occurring ◽  
Relative Viability ◽  
Null Mutants ◽  
Independent Mutant

ABSTRACT Seven alleles of the α-Glycerophosphate dehydrogenase-1 (αGpdh-1) locus of Drosophila melanogaster have been described. These include two naturally occurring electrophoretic variants, one EMS-induced electrophoretic variant, and four EMS-induced "null" or "zero" mutants. With the electrophoretic variants, the locus was mapped to II-20.5 ± 2.5. A complementation matrix was prepared utilizing the null mutants. Three of the four mutants and a deletion of the locus (Grell 1967) exhibit dosage dependency. The dosage independent mutant exhibits complementation with two of the other null alleles. Flies genetically deficient in α-glycerophosphate dehydrogenase are fertile, but their relative viability is severely diminished. Such flies also lose the ability to sustain flight, an observation consistent with the enzyme's function in energy production. The levels of mitochondrial α-glycerophosphate oxidase, measured in flies genetically deficient in the cytoplasmic enzyme, were normal.

Author response for "Location and arrangement of campaniform sensilla in Drosophila melanogaster"

2020 ◽  
Author(s):  
Gesa F. Dinges ◽  
Alexander S. Chockley ◽  
Till Bockemühl ◽  
Kei Ito ◽  
Alexander Blanke ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Author Response ◽  
Campaniform Sensilla

Hepatic Ultrastructure Changes Induced by Lithocholic Acid

1967 ◽  
Vol 25 ◽  
pp. 162-163 ◽  
Author(s):  
F. G. Zaki
Keyword(s):  
Endoplasmic Reticulum ◽  
Lithocholic Acid ◽  
Smooth Endoplasmic Reticulum ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Electron Microscopic ◽  
Hydropic Degeneration ◽  
Hepatic Cells ◽  
Low Protein ◽  
Microscopic Studies

Addition of lithocholic acid (LCA), a naturally occurring bile acid in mammals, to a low protein diet fed to rats induced marked inflammatory reaction in the hepatic cells followed by hydropic degeneration and ductular cell proliferation. These changes were accompanied by dilatation and hyperplasia of the common bile duct and formation of “gallstones”. All these changes were reversible when LCA was withdrawn from the low protein diet except for the hardened gallstones which persisted.Electron microscopic studies revealed marked alterations in the hepatic cells. Early changes included disorganization, fragmentation of the rough endoplasmic reticulum and detachment of its ribosomes. Free ribosomes, either singly or arranged in small clusters were frequently seen in most of the hepatic cells. Vesiculation of the smooth endoplasmic reticulum was often encountered as early as one week after the administration of LCA (Fig. 1).

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