Disease relevance of GstD1

• Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease [1].
• For functional analysis P.tridactylis photolyase was expressed and purified as glutathione S-transferase fusion protein from Escherichia coli cells [2].
• We also used a yeast three-hybrid system and glutathione S-transferase pull-down analyses to demonstrate a robust, direct interaction between HIV-1 Nef and AP2 [3].
• The amino acid sequence identity of class-Theta subunits is highly conserved in rat, the fruitfly Drosophila, maize (Zea mays) and Methylobacterium, which suggests that this family is representative of the ancient progenitor GST gene and originates from the endosymbioses of a purple bacterium leading to the mitochondrion [4].

High impact information on GstD1

• Drosophila glutathione S-transferase 1-1 had no obvious homology to any mammalian or parasitic glutathione S-transferases [5].
• The active enzyme, designated as Drosophila glutathione S-transferase 1-1, had a specific activity toward 1-chloro-2,4-dinitrobenzene comparable to that for the mammalian glutathione S-transferases but did not have as broad a substrate specificity pattern [5].
• We have characterized a Drosophila glutathione S-transferase (RX:glutathione R-transferase, EC 2.5.1.18) cDNA encoding a protein of 209 amino acids [5].
• Drosophila glutathione S-transferase 1-1 shares a region of sequence homology with the maize glutathione S-transferase III [5].
• Addition of thyroid hormone leads to dissociation of Alien from the receptor, as shown by the yeast two-hybrid system, glutathione S-transferase pull-down, and coimmunoprecipitation experiments [6].

Chemical compound and disease context of GstD1

• Each housefly GST cDNA was inserted into a bacterial plasmid expression system and a glutathione transferase activity was expressed in Escherichia coli [7].

Biological context of GstD1

• Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products [8].
• DmGST1 is encoded by a member of a multigene family [9].
• We have characterized a cluster of glutathione S-transferase genes located at 87B on the Drosophila polytene chromosome near the heat shock genes, hsp70 [10].
• The Drosophila glutathione S-transferase (gstD) genes are a family of divergently transcribed, intronless genes and pseudogenes [11].
• The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster [10].

Anatomical context of GstD1

• Gst-D1 expression in the midgut epithelium became restricted to the region that later formed the third midgut constriction [12].
• Spatial expression of Drosophila glutathione S-transferase-D1 in the alimentary canal is regulated by the overlying visceral mesoderm [12].
• This clone was obtained upon screening a cDNA library derived from larval fat body of a pesticide resistant strain of H. virescens with a cDNA probe for Drosophila melanogaster glutathione S-transferase [13].
• Here it is reported that Glutathione S-transferase-D1 (Gst-D1) had three distinctive expression domains in the gut epithelia: the inner epithelium of the proventriculus, the anterior border of the hindgut epithelium, and the midgut epithelium [12].
• This spatial restriction within the midgut epithelium required abdominal-A activity in the overlying visceral mesoderm, suggesting that Gst-D1 will be a useful marker to analyze the mechanism of gene regulation across the mesoderm and endoderm [12].

Associations of GstD1 with chemical compounds

• But no significant change in the amount of glutathione S-transferases GstD1 and GstD5 mRNAs had occurred [14].
• We report that the glutathione S-transferase activity in Kco cells as determined by conjugation with 1-chloro-2,4-dinitrobenzene is elevated slightly to two-fold under heat shock [9].
• The deduced amino acid sequence of the Lu GST1 subunit showed no significant similarity to that of the mammalian GSTs to the Alpha, Mu and Pi classes, but shows some similarity (33%) over the first 100 residues with the rat subunit 12 Theta-class GST [15].
• Transfection with 4-hydroxynonenal-metabolizing glutathione S-transferase isozymes leads to phenotypic transformation and immortalization of adherent cells [16].
• Recombinant rArl1 fused to glutathione-S-transferase (GST) to create GST-rArl1 binds GTP-gamma-S in a dose-dependent manner [17].

Analytical, diagnostic and therapeutic context of GstD1

• Sequence analysis of a genomic clone for GST1 revealed that it is encoded by an intronless gene [9].
• Purification, molecular cloning and heterologous expression of a glutathione S-transferase from the Australian sheep blowfly (Lucilia cuprina) [15].
• The interaction was confirmed using in vitro glutathione S-transferase pulldown and in vivo immunoprecipitation (IP) assays [18].
• Immunofluorescence microscopy of NRK cells revealed discrete perinuclear labelling that could be competed out by GST-rArl1 but not GST [17].
• The fusion Drosomycin protein with a carrier of Glutathione S-transferase (GST) was initially purified by affinity chromatography followed by Enterokinase cleavage [19].

References