In mammalian systems, detoxification enzymes of the GST (glutathione S-transferase) family regulate JNK (c-Jun N-terminal kinase) signal transduction by interaction with JNK itself or other proteins upstream in the JNK pathway. In the present study, we have studied GSTs and their interaction with components of the JNK pathway from Diptera. We have evaluated the effects of four Delta class Anoph...

Two cDNA species, aggst1-5 and aggst1-6, comprising the entire coding region of two distinct glutathione S-transferases (GSTs) have been isolated from a 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) resistant strain (ZANDS) of Anopheles gambiae. The nucleotide sequences of these cDNA species share 80.2% identity and their derived amino acid sequences are 82.3% similar. They have been cla...

The citrus red mite, Panonychus citri (McGregor), is a global citrus pest, and has developed severe resistance to several types of acaricides. However, the molecular mechanisms of resistance in this mite remain unknown. In this study, seven full-length cDNAs encoding glutathione S-transferases (GSTs) genes were identified and characterized in P. citri. The effects of pyridaben and fenpropathrin...

Glutathione transferases (GSTs) are a superfamily of enzymes which have in common the ability to catalyze nucleophilic addition thiol group reduced glutathione (GSH) onto electrophilic and hydrophobic substrates. This conjugation reaction, occurs spontaneously but is dramatically accelerated by enzyme, protects cells against damages caused harmful molecules. With some exceptions, GSTs catalytic...

The nitroaromatic explosive 2,4,6-trinitrotoluene (TNT) and the related 2,4-dinitrotoluene (DNT) are toxic environmental pollutants. The biotransformation and detoxication of these persistent compounds in higher organisms are of great significance from a health perspective as well as for the biotechnological challenge of bioremediation of contaminated soil. We demonstrate that different human g...

Glutathione transferase enzymes (GSTs) catalyze reactions in which electrophiles are conjugated to the tripeptide thiol glutathione. While many GST-catalyzed transformations result in the detoxication of xenobiotics, a few substrates, such as dihaloalkanes, undergo bioactivation to reactive intermediates. Many molecular epidemiological studies have tested associations between polymorphisms (esp...

The glutathione S-transferases (GSTs) are major phase II detoxification enzymes found mainly in the cytosol. They catalyze the initial step in the formation of N-acetylcysteine (mercapturic acid) derivatives of a diverse group of foreign compounds. In addition to their role in catalyzing the conjugation of electrophilic substrates to glutathione (GSH), these enzymes also carry out a range of ot...

The glutathione transferases (GSTs; also known as glutathione S-transferases) are major phase II detoxification enzymes found mainly in the cytosol. In addition to their role in catalysing the conjugation of electrophilic substrates to glutathione (GSH), these enzymes also carry out a range of other functions. They have peroxidase and isomerase activities, they can inhibit the Jun N-terminal ki...

objective: acetaminophen (apap) overdose causes acute liver injuries. studies show that stem cell factor (scf) and its receptor, c-kit, enhance liver recovery from apap-induced injuries in mice. in this study we explore the effect of scf on activity of glutathione s-transferase (gsts) enzymes which are considered to be important in apap metabolism. methods: we divided 45 balb/c mice into three...

The evolution of resistance by an insect to an insecticide may involve several mechanisms. Many studies have shown that insecticide-resistant insects have elevated levels of glutathione S-transferases activity in crude homogenates, which suggests a role for GSTs in resistance. This prompted us to select the GSTs from H.armigera, L.lineolaris and M.sexta due to their economic importance. The 3D ...