Comparison of renal and hepatic glutathione <i>S</i>-transferases in the rat

Kaplowitz, Neil; Clifton, Gil; Kuhlenkamp, John; Wallin, J. D.

doi:10.1042/bj1580243

Cited by 37 publications

(13 citation statements)

References 16 publications

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“…GSH S-transferase activity was determined with 1-chloro-2,4-dinitrobenzene as the substrate (Habig et al, 1974). The enzyme assays with other substrates such as 4-nitropyridine N-oxide, 1,2epoxy-3-(p-nitrophenoxy)propane and p-nitrobenzyl chloride were performed by the method described elsewhere (Fjellstedt et al, 1973;Habig et al, 1974), and bilirubin and probenecid binding to the enzyme protein was done by the method of Ketley et al (1975) and Kaplowitz et al (1976). The unit of enzyme activity was defined as lumol of substrate conjugated or cleaved/min at 250C for GSH S-transferase and at 370C for GSH peroxidase.…”

Section: Materials and Methods Materialsmentioning

confidence: 99%

Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens

Saneto¹,

Awasthi²,

Srivastava³

1980

Biochemical Journal

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Since the eye is constantly exposed to potentially damaging chemical compounds present in the atmosphere and vascular system, we investigated the physiological role of glutathione S-transferase (GSH S-transferase) in detoxification mechanisms operative in the ocular lens. We have purified an anionic and a cationic GSH S-transferase from the bovine lens to homogeneity through a combination of gel filtration, ion-exchange and affinity chromatography. The anionic (pI 5.6) and cationic (pI 7.4) S-transferases were found to have distinct kinetic parameters (apparent Km and Vmax. pH optimum and energy of activation). However, both species were demonstrated to have similar molecular weights and amino acid compositions. Double-immunodiffusion and immunotitration studies showed that both lens S-transferases were immunologically similar. The very close similarity in amino acid compositions and immunological properties strongly indicates that these two transferases either originate from the same gene or at least share common antigenic determinants and originate from similar genes. The bovine lens GSH S-transferases had no glutathione peroxidase activity with either t-butyl hydroperoxide or cumene hydroperoxide as substrate. However, the antibody raised against the homogeneous anionic glutathione S-transferase from the bovine lens was found to precipitate both glutathione S-transferase and glutathione peroxidase activities out of solution in the supernatant of a crude bovine liver homogenate.

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Section: Materials and Methods Materialsmentioning

confidence: 99%

Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens

Saneto¹,

Awasthi²,

Srivastava³

1980

Biochemical Journal

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“…It should be mentioned that several other GST inhibitors have been discovered belonging to different structural classes, including diethyl maleate, p ‐aminohippurate (Figure ) and probenecid, clofibrate, misonidazole, piriprost (Figure ), GSH conjugates of tetrachloro‐1,4‐benzoquinone derivatives, gossypol, and sulfasalazine (Figure ) …”

Section: Intrinsic Substrates and Metabolism‐related Drugsmentioning

confidence: 99%

Small‐molecule inhibitors of multidrug resistance‐associated protein 1 and related processes: A historic approach and recent advances

Stefan

Wiese

2018

Medicinal Research Reviews

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Multidrug resistance-associated protein 1 (MRP1, ABCC1) is an ATP-binding cassette (ABC) transport protein. This efflux pump uses the energy of ATP hydrolysis to export structurally diverse antineoplastic agents in human cancers. The upregulation of MRP1 (either inherent or acquired) is one major reason for the occurrence of the phenomenon called multidrug resistance (MDR). MDR is characterized by a reduced outcome of chemotherapy due to the active intracellular clearance of cytostatic drugs below the necessary effect concentration. Much effort has been made to overcome MDR, which implied high-throughput screenings of already known pharmacological and natural compounds, modification of intrinsic substrates, as well as design and synthesis of new inhibitors. This review is meant not only to summarize the most recent results over the past 10 years, but also to highlight major achievements regarding reversal of MRP1-mediated MDR, from the time of its discovery until today. The focus lies on small-molecule compounds that feature either direct MRP1 inhibition/transport blockage, toxicity against MRP1-overexpressing cells, inhibition/modification of intracellular processes necessary for MRP1 function, or modification of MRP1-related metabolic and genomic mechanisms. Considering all aspects, this review might be useful to (re)consider possible strategies to overcome MRP1-mediated MDR. Furthermore, it may be the basis for developing new, even better, highly potent, less toxic, and selective (as well as broad-spectrum) MRP1 inhibitors that will enter clinical evaluations in different malignancies and finally conduce to overcome MDR in general.

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“…Enzyme DIII,, and DIV,, seem to be more sensitive and show linear competitive kinetics as previously observed for rat [50] and human [46] liver transferases.…”

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confidence: 53%

Heterogeneity of dog-liver glutathione S-transferases. Evidence for a unique temperature dependence of the catalytic process

Wiener

1986

Eur J Biochem

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Dog liver glutathione S-transferase activities are associated with five cytosolic proteins and to approximately 1.5% with microsomal proteins determined on the basis of activity conjugating to l-chloro-2,4-&nitrobenzene. The four major cytosolic enzymes were purified to apparent homogeneity by sequential use of ion-exchange, hydrophobic, hydroxyapatite and affinity chromatography. The isolated transferases are binary combinations of three classes of subunits: c1 (Mr = 26000), fi ( M , = 27000), y ( M , = 28500). They were classified by roman numerals assigned in order of increasing isoelectric point as DI,, (PI 6.4), DII, (PI 6.9), DIII,,, (PI 8.1), and DIV,, (PI 8.7). Additionally, traces of conjugating activity may be attributed to a, fi monomeric or dimeric protein with cationic character.The differences in catalytic specificity, temperature and pH dependence of activity, and sensitivity and kinetic response to inhibitory ligands may reflect the intrinsic structural heterogeneity of the transferases. At physiological glutathione concentrations D I?, accounted for roughly 60% of the total 1 -chloro-2,4-dinitrobenzene-conjugating activity, the rank order of activity being DI,, > D1Iua > DIV,, > DIII~,. The glutathione-dependent denitration of organic nitrates seems to be restricted to the cationic enzymes, whereas 1,2-dichloro-4-nitrobenzene-conjugating activity is exclusively associated with the anionic transferases, D I,, % DII,,. Arrhenius plots from initial rate experiments performed over a range of temperatures (15 -40°C) exhibit an upward bend for DI,,, an apparently constant slope for D II,, and D III,,, and a downward bend for D IVDy.

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Comparison of renal and hepatic glutathione S-transferases in the rat

Cited by 37 publications

References 16 publications

Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens

Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens

Small‐molecule inhibitors of multidrug resistance‐associated protein 1 and related processes: A historic approach and recent advances

Heterogeneity of dog-liver glutathione S-transferases. Evidence for a unique temperature dependence of the catalytic process

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