Glutathione transferase isoenzymes from frog (Xenopus laevis) liver and embryo

Angelucci, Stefania; Sacchetta, Paolo; Luca, Antonella De; Moio, Pasquale; Amicarelli, Fernanda; Ilio, Carmine Di

doi:10.1016/s0304-4165(01)00238-0

Cited by 19 publications

(10 citation statements)

References 22 publications

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“…88) Three common bands detected in SDS-PAGE were also confirmed by HPLC analysis of purified proteins, and the molecular mass of each subunit was determined by LC-ESI-MS to be 22, 24, and 25 kDa. These GSTs were confirmed to be μ-, α-, and σ-classes by Western blot analysis.…”

Section: Glutathione-s-transferases (Gst)mentioning

confidence: 83%

Bioconcentration and metabolism of pesticides and industrial chemicals in the frog

Katagi

Ose

2014

J. Pestic. Sci.

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Exposure to pesticide residues is claimed to be one of the possible causes of frog decline. Knowledge of basic information on the uptake, metabolism and depuration processes of pesticides in the frog is needed to understand the relationship between exposure and toxic effects from their actual body burden, together with their bioconcentration. The hydrophobicity of pesticides and industrial chemicals was one of the most important factors controlling bioconcentration, similarly to fish, when frogs are exposed to contaminated water. Skin absorption was also a key route in the uptake process especially in the adult frog. The metabolic profiles in the frog, mainly examined by an intraperitoneal injection technique, were common to other aquatic species without any frog-specific transformation reaction. The effects of developmental stage, sex, species and environmental factors such as temperature were observed for bioconcentration and metabolism.

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Section: Glutathione-s-transferases (Gst)mentioning

confidence: 83%

Bioconcentration and metabolism of pesticides and industrial chemicals in the frog

Katagi

Ose

2014

J. Pestic. Sci.

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“…This isoform is not expressed in metamorphosing X. laevis, which is attributed to the fact that this species does not change from an aquatic environment to a terrestrial one [4]. Certain GST isoenzymes such as GSTA2 (rat) and GSTA1 (mouse) are induced by pro-oxidant xenobiotics through the Nrf2 transcription factor, which mediates oxidative stress responses [36].…”

Section: Discussionmentioning

confidence: 99%

Changes in the antioxidant metabolism in the embryonic development of the common South American toad Bufo arenarum: Differential responses to pesticide in early embryos and autonomous‐feeding larvae

Ferrari

Anguiano

Lascano

et al. 2008

J Biochem & Molecular Tox

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Amphibians may be critically challenged by aquatic contaminants during their embryonic development. Many classes of compounds, including organophosphorus pesticides, are able to cause oxidative stress that affects the delicate cellular redox balance regulating tissue modeling. We determined the progression of antioxidant defenses during the embryonic development of the South American common toad, Bufo arenarum. Superoxide dismutase (SOD) and catalase (CAT) activities were high in the unfertilized eggs, and remained constant during the first stages of development. SOD showed a significant increase when the gills were completely active and opercular folds began to form. Reductase (GR) activity was low in the oocytes and increased significantly when gills and mouth were entirely developed and the embryos presented a higher exposure to pro-oxidant conditions suggesting an environmental control. Reduced glutathione (GSH) content was also initially low, and rose continuously pointing out an increasing participation of GSH-related enzymes in the control of oxidative stress. GSH peroxidases and GSH-S-transferases showed relatively high and constant activities, probably related to lipid peroxide control. B. arenarum embryos have plenty of yolk platelets containing lipids, which provide the energy and are actively transferred to the newly synthesized membranes during the early embryonic development. Exposure to the pro-oxidant pesticide malathion during 48 h did not significantly affect the activity of antioxidant enzymes in early embryos, but decreased the activities of CAT, GR, and the pool of GSH in larvae. Previous work indicated that lipid peroxide levels were kept low in malathion-exposed larvae, thus we conclude that oxidative stress is overcome by the antioxidant defenses. The increase in the antioxidant metabolism observed in the posthatching phase of development of B. arenarum embryo, thus constitutes a defense against natural and human-generated pro-oxidants present in the aquatic environment.

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“…On the contrary, BbGSTP2-2 is essentially expressed in adult toad tissues, including liver and kidney [10][11][12][13]. We have also investigated the expression of GSTs in Xenopus laevis [14]. A new Mu-class GST has been cloned, expressed and characterized previously from this amphibian species [15].…”

Section: Introductionmentioning

confidence: 99%

“…A new Mu-class GST has been cloned, expressed and characterized previously from this amphibian species [15]. Unlike B. bufo, X. laevis does not apparently express Pi-class GSTs [14]; however, analysis of the expressed sequence tag (EST) database suggests that a previously uncharacterized Pi-class GST isoform might be encoded by this amphibian species. Screening of a cDNA liver tumour library from X. laevis resulted in the isolation of a cDNA encoding Pi-class GST and its nucleotide sequence has been Abbreviations used: CDNB, 1-chloro-2,4-dinitrobenzene; GST, glutathione transferase; EST, expressed sequence tag; IPTG, isopropyl β-Dthiogalactoside; LB, Luria-Bertani; RT-PCR, reverse transcription-PCR; tPBO, trans-4-phenyl-3-buten-2-one.…”

Section: Introductionmentioning

confidence: 99%

A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site

Luca

Favaloro

Carletti

et al. 2003

Biochemical Journal

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Screening of a liver tumour cDNA library from Xenopus laevis resulted in the isolation of a full-length cDNA clone encoding a novel Pi-class amphibian glutathione transferase (GST) isoenzyme (designated as XlGSTP1-1). The gene encodes a protein of 212 amino acids with a calculated molecular mass of 24428 Da. The product of the gene has been overexpressed in Escherichia coli and characterized. XlGSTP1-1 has one of the highest specific activities towards 1-chloro-2,4-dinitrobenzene (1310 micromol/min per mg of protein) obtained with any GST. A notable feature of XlGSTP1-1 is the presence in the H-site of Phe(111) and Pro(208) in place of tyrosine and glycine residues respectively, present in other mammalian Pi-class GSTs. Site-directed mutagenesis indicate that Phe(111) is involved in substrate specificity of XlGSTP1-1. We provide evidence showing that XlGSTP1-1 is present only in the embryo and its expression might be associated with cellular proliferation.

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Glutathione transferase isoenzymes from frog (Xenopus laevis) liver and embryo

Cited by 19 publications

References 22 publications

Bioconcentration and metabolism of pesticides and industrial chemicals in the frog

Bioconcentration and metabolism of pesticides and industrial chemicals in the frog

Changes in the antioxidant metabolism in the embryonic development of the common South American toad Bufo arenarum: Differential responses to pesticide in early embryos and autonomous‐feeding larvae

A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site

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