Ligandin and Glutathione S-Transferases: Historical Milestones

2006 ◽  
pp. 15-24
Keyword(s):  
Glutathione S Transferases

Partial purification of Glutathione-S-transferases in Plutella xylostella (L.) show imparting resistance against Flubendiamide

2012 ◽  
Vol 2 (9) ◽  
pp. 3-5
Author(s):  
Dipali B Borkar ◽  
◽  
Vishal L Bagde ◽  
S. S. Munje S. S. Munje ◽  
M.P. Moharil M.P. Moharil
Keyword(s):  
Plutella Xylostella ◽  
Partial Purification ◽  
Glutathione S Transferases

Comparing the Genetic Detox Ability and Heavy Metal Burden in a Cohort of Samples of Egyptian Children and those with Autistic Spectrum Disorder

2019 ◽  
Author(s):  
Blaurock-Busch E
Keyword(s):  
Heavy Metal ◽  
Autism Spectrum ◽  
Control Group ◽  
Potentially Toxic Metals ◽  
Gstt1 Null Genotype ◽  
Egyptian Children ◽  
Glutathione S Transferases ◽  
Metal Burden ◽  
Detoxification Pathway

The heavy metal burden of patients with Autism spectrum disorders (ASD) has been widely discussed [1-5]. Present knowledge suggests that ASD patients, compared to ‘normal’s’ show a greater metal burden, which may be a cause of the ASD pathogenesis, possibly due to a limited detoxification potential. We thus aimed to evaluate if the metal burden of ASD children is due to comprised detoxification ability, and if missing of enzymes such as the glutathione-S-transferases provide an explanation, or if additional factors play a role. Genetically, we noticed a slight difference in the detoxification ability of the ASD group compared to the Control group. In the ASD group, carrier of the genotype GSTT1 null genotype (i.e. the homozygous loss) are 1.7 times more common as in the Control group and the GSTT1 allele is more frequent in the ASD patient collective. These findings are not statistically significant but indicate a trend. In addition, our data indicates that levels of potentially toxic metals in blood and hair of both groups demonstrate a similar immediate and long-term exposure. However, 36% of the ASD group showed signs of zinc deficiency compared to 11% of the Control group and this points towards inefficiency of the Phase I detoxification pathway. More research is needed to explore the role of other elements in the detoxification pathway.

Synthesis, cytotoxicity, antioxidant and antimicrobial activity of indole based novel small molecule

2020 ◽  
Vol 17 ◽  
Author(s):  
Aslıhan Kurt-Kızıldoğan ◽  
Çiğdem Otur ◽  
Can Yılmaz ◽  
Sevki Arslan ◽  
Dogukan Mutlu ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cell Lines ◽  
Cancer Cell ◽  
Cytotoxic Effect ◽  
Antimicrobial Properties ◽  
Cancer Cell Lines ◽  
Coupling Reactions ◽  
Human Liver Cancer ◽  
Glutathione S Transferases ◽  
Antioxidant And Antimicrobial Activity

Background:: Indoles probably represent one of the most important heterocyclic structures that have been attracting the interest of many scientists in drug discovery. Methods:: Pd-catalyst Sonogashira coupling reactions, MTT Assay, Antioxidant capacity test, Antimicrobial test, GST enzyme activity test. Results and Discussion:: 1-ethyl-2-phenyl-3-(phenylethynyl)-1H-indole had antioxidant and antimicrobial properties. It displayed significant induction in glutathione S-transferases (GST) enzyme activity in human liver cancer cell lines (HepG2), but cytotoxic effect on all tested cancer cell lines could not be observed. Conclusion:: All of these results showed that 1-ethyl-2-phenyl-3-(phenylethynyl)-1H-indole had antioxidant and antimicrobial properties without cytotoxic effect, which could make it a promising active component.

scholarly journals Isoelectric focusing of glutathione S-transferases from rat liver and kidney

1978 ◽  
Vol 175 (3) ◽  
pp. 937-943 ◽  
Author(s):  
Barbara F. Hales ◽  
Valerie Jaeger ◽  
Allen H. Neims
Keyword(s):  
Substrate Specificity ◽  
Isoelectric Focusing ◽  
Transferase Activity ◽  
Sprague Dawley ◽  
Substrate Specificities ◽  
Liver Cytosol ◽  
Sprague Dawley Rats ◽  
Isoelectric Points ◽  
Liver And Kidney ◽  
Glutathione S Transferases

The glutathione S-transferases that were purified to homogeneity from liver cytosol have overlapping but distinct substrate specificities and different isoelectric points. This report explores the possibility of using preparative electrofocusing to compare the composition of the transferases in liver and kidney cytosol. Hepatic cytosol from adult male Sprague–Dawley rats was resolved by isoelectric focusing on Sephadex columns into five peaks of transferase activity, each with characteristic substrate specificity. The first four peaks of transferase activity (in order of decreasing basicity) are identified as transferases AA, B, A and C respectively, on the basis of substrate specificity, but the fifth peak (pI6.6) does not correspond to a previously described transferase. Isoelectric focusing of renal cytosol resolves only three major peaks of transferase activity, each with narrow substrate specificity. In the kidney, peak 1 (pI9.0) has most of the activity toward 1-chloro-2,4-dinitrobenzene, peak 2 (pI8.5) toward p-nitrobenzyl chloride, and peak 3 (pI7.0) toward trans-4-phenylbut-3-en-2-one. Renal transferase peak 1 (pI9.0) appears to correspond to transferase B on the basis of pI, substrate specificity and antigenicity. Kidney transferase peaks 2 (pI8.5) and 3 (pI7.0) do not correspond to previously described glutathione S-transferases, although kidney transferase peak 3 is similar to the transferase peak 5 from focused hepatic cytosol. Transferases A and C were not found in kidney cytosol, and transferase AA was detected in only one out of six replicates. Thus it is important to recognize the contribution of individual transferases to total transferase activity in that each transferase may be regulated independently.

scholarly journals Effect of gallic acid on the larvae of Spodoptera litura and its parasitoid Bracon hebetor

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Abhay Punia ◽  
Nalini Singh Chauhan ◽  
Drishtant Singh ◽  
Anup Kumar Kesavan ◽  
Sanehdeep Kaur ◽  
...  
Keyword(s):  
Gallic Acid ◽  
Spodoptera Litura ◽  
Negative Impact ◽  
Larval Mortality ◽  
Adult Emergence ◽  
Egg Hatching ◽  
Bracon Hebetor ◽  
Total Hemocyte Count ◽  
Glutathione S Transferases ◽  
Immense Potential

AbstractThe antibiosis effect of gallic acid on Spodoptera litura F. (Lepidoptera: Noctuidae) and its parasitoid evaluated by feeding six days old larvae on artificial diet incorporated with different concentrations (5 ppm, 25 ppm, 125 ppm, 625 ppm, 3125 ppm) of the phenolic compound revealed higher concentration (LC50) of gallic acid had a negative impact on the survival and physiology of S. litura and its parasitoid Bracon hebetor (Say) (Hymenoptera:Braconidae). The mortality of S. litura larvae was increased whereas adult emergence declined with increasing concentration of gallic acid. The developmental period was delayed significantly and all the nutritional indices were reduced significantly with increase in concentration. Higher concentration (LC50) of gallic acid adversely affected egg hatching, larval mortality, adult emergence and total development period of B. hebetor. At lower concentration (LC30) the effect on B. hebetor adults and larvae was non-significant with respect to control. Gene expression for the enzymes viz., Superoxide dismutase, Glutathione peroxidase, Peroxidase, Esterases and Glutathione S transferases increased while the total hemocyte count of S. litura larvae decreased with treatment. Our findings suggest that gallic acid even at lower concentration (LC30) can impair the growth of S. litura larvae without causing any significant harm to its parasitoid B. hebetor and has immense potential to be used as biopesticides.

scholarly journals Expression of glutathione S-transferases in rat brains.

1986 ◽  
Vol 261 (17) ◽  
pp. 7596-7599
Author(s):  
N Q Li ◽  
P Reddanna ◽  
K Thyagaraju ◽  
C C Reddy ◽  
C P Tu
Keyword(s):  
Glutathione S Transferases

scholarly journals Studies on the subunit composition of rat liver glutathione S-transferases.

1983 ◽  
Vol 258 (18) ◽  
pp. 11321-11325 ◽  
Author(s):  
A B Frey ◽  
T Friedberg ◽  
F Oesch ◽  
G Kreibich
Keyword(s):  
Rat Liver ◽  
Subunit Composition ◽  
Liver Glutathione ◽  
Glutathione S Transferases
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