Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases

Armstrong, Richard N.

doi:10.1021/tx960072x

Cited by 1,046 publications

(967 citation statements)

References 109 publications

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“…These enzymes are potentially crucial in regulating susceptibility to cancer, due to their ability in metabolizing reactive metabolites of carcinogens. Among them pi-and alpha-GST have attracted interest mainly because of high expression in different pathologies such as cancer, liver and kidney diseases (12)(13)(14). The decrease in the levels of GSH in blood haemolysates observed in our study may be due to the increased utilization of GSH by glutathione S-transferases (GST) in detoxification of endogenous or exogenous exposed carcinogens.…”

Section: Discussionmentioning

confidence: 99%

Free radical injury and antioxidant status in patients with benign prostate hyperplasia and prostate cancer

Srivastava

Mittal

2005

Indian J Clin Biochem

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Reactive oxygen species and other free radicals are known to be the mediators of phenotypic and genotypic changes that lead from mutation to neoplasia. There are some primary antioxidants such as glutathione peroxidase (GPx), glutathione S-transferases (GSTs) and reduced glutathione, which protect against cellular and molecular damage caused by the reactive oxygen metabolites (ROMs). The present study was conducted to determine the level of malondialdehyde (MDA), as an index of lipid peroxidation, along with the GPx, GSTs activities and level of reduced glutathione in 45 prostate cancer (PC) patients, 55 benign prostate hyperplasia (BPH) patients as compared to the controls. Significant higher levels of MDA and GSTs activities in the serum, (P<0.005) and significant lower levels of reduced GSH concentration and GPx activity in blood haemolysates (P<0.05) of PC and BPH patients were observed as compared to the controls. The relatively higher GSTs activity and low level of reduced GSH may be due to the response of increased reactive oxygen metabolites production in the blood. The higher MDA and lower GPx activities may be inadequate to detoxify high levels of H202 into HzO leading to the formation of the *OH radical followed by MDA. This result hypothesizes that oxidant-antioxidant imbalance may be one of the major factor responsible for the development of prostate cancer and benign prostate hyperplasia.

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Section: Discussionmentioning

confidence: 99%

Free radical injury and antioxidant status in patients with benign prostate hyperplasia and prostate cancer

Srivastava

Mittal

2005

Indian J Clin Biochem

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“…The glutathione transferases are a multifunctional family of enzymes, broadly distributed in nature, that play a critical role in cellular detoxification [44][45][46][47][48][49]. GSTs have the general function of conjugating glutathione (GSH) to electrophilic substances to reduce their toxicity.…”

Section: Ure2 As a Glutathione Transferasementioning

confidence: 99%

The yeast prion protein Ure2: Structure, function and folding

Lian

Jiang

Zhang

et al. 2006

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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The Saccharomyces cerevisiae protein Ure2 functions as a regulator of nitrogen metabolism and as a glutathione-dependent peroxidase. Ure2 also has the characteristics of a prion, in that it can undergo a heritable conformational change to an aggregated state; the prion form of Ure2 loses the regulatory function, but the enzymatic function appears to be maintained. A number of factors are found to affect the prion properties of Ure2, including mutation and expression levels of molecular chaperones, and the effect of these factors on structure and stability are being investigated. The relationship between structure, function and folding for the yeast prion Ure2 are discussed.

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“…In addition, several structurally similar compounds with varying functional groups connecting the two aromatic rings (18)(19)(20)(21)(22) were synthesized starting from 4, 7 or 8 (Scheme 5).…”

Section: Resultsmentioning

confidence: 99%

Synthesis, nitric oxide release, and anti-leukemic activity of glutathione-activated nitric oxide prodrugs: Structural analogues of PABA/NO, an anti-cancer lead compound

Chakrapani

Wilde

Citro

et al. 2008

Bioorganic & Medicinal Chemistry

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Diazeniumdiolate anions and their prodrug forms are reliable sources of nitric oxide (NO) that have generated interest as promising therapeutic agents. A number of structural analogues of, an anti-cancer lead compound that is designed to release NO upon activation by glutathione, were prepared. The nitric oxide release patterns of these O 2 -(2,4-dinitrophenyl) diazeniumdiolates in the presence of glutathione were tested and it was found that in the absence of competing pathways, these compounds release nearly quantitative amounts of NO. The ability of PABA/NO and its structural analogues to inhibit human leukemia cell proliferation was determined and it was found that compounds releasing elevated amounts of NO displayed superior cytotoxic effects.

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Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases

Cited by 1,046 publications

References 109 publications

Free radical injury and antioxidant status in patients with benign prostate hyperplasia and prostate cancer

Free radical injury and antioxidant status in patients with benign prostate hyperplasia and prostate cancer

The yeast prion protein Ure2: Structure, function and folding

Synthesis, nitric oxide release, and anti-leukemic activity of glutathione-activated nitric oxide prodrugs: Structural analogues of PABA/NO, an anti-cancer lead compound

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