Glutathione S-transferases in housefly (Musca domestica): Location of GST-1 and GST-2 families
References (40)
- et al.
Conjugation of chloro-dinitrobenzene with reduced glutathione in the absence and presence of glutathione transferase from larvae of the Southern Armyworm, Spodoptera eridania
Pestic. Biochem. Physiol.
(1990) - et al.
A distinct human testis and brain mu class glutathione S-transferase
- et al.
Studies on glutathione S-transferase in Helicoverpa (= Heliothis) zea
Insect Biochem.
(1991) - et al.
Characterization of multiple glutathione transferases from the house fly, Musca domestica (L.)
Pestic. Biochem. Physiol.
(1984) - et al.
Insect glutathione S-transferases
- et al.
Glutathione S-transferase isozymes in Aedes aegypti: purification, characterization and isozyme-specific regulation
Insect Biochem.
(1991) - et al.
Glutathione S-transferases 1 and 2 in susceptible and insecticide resistant Aedes aegypti
Pestic. Biochem. Physiol.
(1989) - et al.
Glutathione S-transferase, the first enzymatic step in mercapturic acid formation
J. Biol. Chem.
(1974) - et al.
Differential expression of glutathione transferases by native and culture human lymphocytes
Biochem. Pharmac.
(1988) Protective role of glutathione and glutathione transferases in mutagenesis and carcinogenesis
Mutation Res.
(1988)
Glutathione S-transferase in the Australian Sheep Blowfly, Lucilia cuprina (Wiedemann)
Pestic. Biochem. Physiol.
Purification and properties of glutathione S-transferases from the larvae of the Australian sheep blowfly, Lucilia cuprina (Wiedemann)
Insect Biochem.
Increase glutathione S-transferase activity and glutathione content in an insecticide resistant strain of Tribolium castaneum (Herbst)
Pestic. Biochem. Physiol.
Reduced glutathione in the housefly: concentration during development and variation in strains
Insect. Biochem.
Separation of the main isozymes of human erythrocytes, heart and lung glutathione transferase
J. Chromat.
Purification of human muscle glutathione transferase: evidence that glutathione S-transferase tau corresponds to a locus distinct from GST1, GST2 and GST3
Arch. Biochem. Physiol.
Induction of detoxifying enzymes by allelochemicals and host plants in the fall armyworm
Pestic. Biochem. Physiol.
Interactions of allelochemicals with detoxication enzymes of insecticide susceptible and resistant fall armyworm
Pestic. Biochem. Physiol.
Characterization and localization of glutathione S-transferases in rat brain and binding of hormones, neurotransmitters and drugs
J. Neurochem.
Glutathione S-transferases: amino acid sequence comparison, classification and phylogenic relationship
Envir. Carcino. Ecotox. Revs C
Cited by (46)
Characterisation of GST genes from the Hyphantria cunea and their response to the oxidative stress caused by the infection of Hyphantria cunea nucleopolyhedrovirus (HcNPV)
2020, Pesticide Biochemistry and PhysiologyCitation Excerpt :Insect GSTs belong to a family of phase II enzymes associated with significant detoxification of xenobiotic compounds, and they play a role in intracellular transport, hormone biosynthesis, and protection against oxidative stress (Enayati et al., 2005). Sigma GSTs, in particular, have a significant role in protection against oxidative stress (Franciosa and Berge, 1995; Singh et al., 2001). Insect GSTs are a large family of multifunctional enzymes, which are classified based on their location within the cell, namely, microsomal and cytosolic (zeta, theta, omega and epsilon classes).
Identification, genomic organization and expression pattern of glutathione transferase in Pardosa pseudoannulata
2019, Comparative Biochemistry and Physiology - Part D: Genomics and ProteomicsCitation Excerpt :Sigma of mammals is able to catalyze the isomerization of prostaglandin H2 (PGH2) to prostaglandin D2 (PGD2) (Kanaoka et al., 1997; Jowsey et al., 2001). However, among the two insects, M. domestica and D. melanogaster, Sigma are localized in the indirect flight muscle family promotes the filament attachment of the indirect flight muscle and participate in the detoxification of lipid peroxidation products (Franciosa and Bergé, 1995; Singh et al., 2010). PpGSTS1 was specifically expressed in the appendages, which is likely to be associated with metabolism of free radicals after jumping muscles or appendage movement.
Cadmium exposure on tissue-specific cadmium accumulation and alteration of hemoglobin expression in the 4th-instar larvae of Propsilocerus akamusi (Tokunaga) under laboratory conditions
2017, Ecotoxicology and Environmental SafetyCitation Excerpt :This is consistent with previous research that found that larvae contaminated with Cd had significantly enhanced metal loads in their hemolymph (Kafel et al., 2012; Leonard et al., 2009). Nevertheless, Cd is rapidly cleared from the hemolymph (Martin and Rainbow, 1998) and the hemolymph plays an important role in protecting the other organs through immunological and antioxidant defenses (Franciosa and Berge, 1995; An and Choi, 2010). Thus, the hemolymph was identified as a temporary target organ of Cd accumulation, with the Cd then being transferred to other internal tissues, such as the Malpighian tubules and gut, via the hemolymph.
Effects of multigenerational cadmium exposure of insects (Spodoptera exigua larvae) on anti-oxidant response in haemolymph and developmental parameters
2012, Environmental PollutionCitation Excerpt :This is important because Cd may be transferred to other internal tissues via the haemolymph. Additionally, the haemolymph helps to protect the other organismal systems, through immunological and anti-oxidant defences (Franciosa and Berge, 1995; An and Choi, 2010). The aim of our study was to compare the differences in anti-oxidant defence and developmental parameters between herbivorous insects derived from multigenerational rearing on a diet contaminated with cadmium to those reared on a non-contaminated diet.
Developmental studies on the Sigma and Delta-1 glutathione transferases of Lucilia cuprina
2012, Comparative Biochemistry and Physiology - Part D: Genomics and ProteomicsCitation Excerpt :The Sigma GST, with its association with the flight muscle is unsurprisingly found in greatest quantity in thorax. Sigma GST is also associated with nervous tissue (Franciosa and Berge, 1995) so its appearance in other bodily tissues is to be expected. The results recorded here are compatible with those reported for M. domestica by these workers who, using immunoassay, demonstrated the distribution of Sigma GST in head: thorax: abdomen to be approximately 10:80:10 (Franciosa and Berge, 1995).