GSH depletion, protein S-glutathionylation and mitochondrial transmembrane potential hyperpolarization are early events in initiation of cell death induced by a mixture of isothiazolinones in HL60 cells

Stefano, Anna Di; Frosali, Simona; Leonini, Alessandra; Ettorre, Anna; Priora, Raffaella; Simplicio, Francesca Cherubini Di; Simplicio, P. Di

doi:10.1016/j.bbamcr.2005.12.012

Cited by 61 publications

(38 citation statements)

References 43 publications

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“…It has been observed in the primary rat cortical neurons that a reduction in the level of GSH is dependent on the enhancement in oxidative stress (Hood et al, 2010). Generation of ROS has been observed before the onset of cell death and its increased generation in necrosis is responsible for cell death (Di Stefano et al, 2006). Our results showed that escopoletin treatment resulted in the generation of ROS which in turn induced non apoptotic cell death in DU145 cells.…”

Section: Discussionsupporting

confidence: 51%

Induction of cell death in prostate cancer cells by escopoletin, a promising treatment strategy

Chen

Zhang

Fazhu

et al. 2015

Bangladesh J Pharmacol

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<p>Escopoletin, a phenolic compound belonging to anthocyanin family shows promising antioxidant activities. In the present study, anti-cancer effects of escopoletin treatment in DU145 cells were investigated. The sulphorhodamine-B staining and annexin V and propidium iodide were respectively used for the analysis of cell viability and death. The results revealed a significantly higher cytotoxicity by escopoletin that caused cell death in DU145 cells. Escopoletin treatment in DU145 cells markedly inhibited cell growth through non-apoptotic cell death and induced significant reactive oxygen species (ROS) production. It also induced G1 cell cycle arrest and cyclin D1 accumulation through the enhanced expression of p21. However, the effect of escopoletin on DU145 cells was reversed by pretreatment with glutathione antioxidant. This suggests that escopoletin induced generation of ROS is responsible for the increased cytotoxicity in DU145 cells. Thus, escopoletin exhibits potential therapeutic efficacy for the treatment of prostate cancer.</p><p> </p>

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Section: Discussionsupporting

confidence: 51%

Induction of cell death in prostate cancer cells by escopoletin, a promising treatment strategy

Chen

Zhang

Fazhu

et al. 2015

Bangladesh J Pharmacol

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“…Redox modification of Cys residues of an enzyme provides a mechanism for regulating enzyme activity, especially during oxidative stress {Ghezzi, 2005 #33602]. S-glutathionylation has been reported to regulate the activity of various enzymes [16,17], although no data has been reported regarding the oxidative regulation of human SULTs. Our recent work [19,20] demonstrated that hyperoxia, physical stress, and chemical (parathion) stress regulate rat SULT1A1 enzyme activity in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…Oxidative stress is a well-known cause of changes in GSSG/GSH ratios and levels in vivo [10]. S-glutathionylation regulates the activity of various enzymes [16,17], although no data has been reported regarding in vivo SULT regulation. Only in vitro redox regulation using E. coli-expressed rat aryl sulfotransferase IV (AST-IV or rSULT1A1) has been reported [18].…”

Section: Introductionmentioning

confidence: 99%

Redox regulation of human estrogen sulfotransferase (hSULT1E1)

Maiti¹,

Zhang²,

Chen³

2007

Biochemical Pharmacology

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Sulfotransferases (SULTs) are enzymes that catalyze the sulfation of hydroxyl-containing compounds. Sulfation regulates hormone activities and detoxifies xenobiotics. Human estrogen sulfotransferase (hSULT1E1) catalyzes the sulfation of estrogens and regulates estrogen bioactivities. Oxidative regulation provides a biological mechanism for regulating enzyme activities in vivo. The oxidative regulation of human SULTs has not been reported. In this study, we used amino acid modification, manipulation of intracellular redox state, and site-directed mutagenesis to study the redox regulation of human SULTs and specifically the mechanism of hSULT1E1 inhibitory regulation by oxidized glutathione (GSSG). Of the four major human SULTs, hSULT1A1, hSULT1A3, and hSULT2A1 do not undergo redox regulation; hSULT1E1, on the other hand, can be redox regulated. GSSG inactivated hSULT1E1 activity in an efficient, time-and concentrationdependant manner. The co-enzyme adenosine 3′-phosphate 5′-phosphosulfate protected hSULT1E1 from GSSG-associated inactivation. A reduced glutathione (GSH) inducer (N-acetyl cysteine) significantly increased while a GSH depletor (buthionine sulfoxamine) significantly decreased hSULT1E1 activity, but both failed to affect the amount of hSULT1E1 protein in human hepatocyte carcinoma Hep G2 cells. Crystal structure suggested that no Cys residues exist near the active sites of hSULT1A1, hSULT1A3, and hSULT2A1, but Cys residues do exist within the active site of hSULT1E1. Site-directed mutagenesis demonstrated that Cys83 is critical for the redox regulation of hSULT1E1. This first report on the redox regulation of human SULTs suggests that the redox regulation of hSULT1E1 may interrupt the regulation and function of estrogens under various physiological and pathological conditions.

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“…Some reports document that TPIs can be regulated by S-glutathionylation, through the formation of a mixed disulfide between SH residues of the protein and glutathione oxidized GSSG (21,22,44). The S-glutathionylation is an antioxidant device that reduces the impact of oxidants on proteins, and at the same time it is also a regulatory system for many enzyme activities (20,(45)(46)(47).…”

Section: Discussionmentioning

confidence: 99%

Triosephosphate Isomerases in Italian Ryegrass (Lolium multiflorum): Characterization and Susceptibility to Herbicides

Buono¹,

Prinsi²,

Espen³

et al. 2009

J. Agric. Food Chem.

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The effect of treatments with four herbicides and a safener on the activity of triosephosphate isomerase (TPI) extracted from shoots of Italian ryegrass was investigated. It was found that atrazine and fluorodifen, herbicides which interfere with photosynthesis, caused a decrease in measured enzyme activity. In addition, the in vitro effect of oxidized glutathione (GSSG), a compound produced in situations of oxidative stress, on TPI activity was investigated. It was shown that GSSG was a strong inhibitor of enzyme activity, at low concentrations in a dose-timedependent manner. The enzyme extracts were submitted to chromatographic purifications and to two-dimensional electrophoresis. Some spots had molecular masses ranging between 20 and 30 kDa and were characterized and identified by LC-ESI-MS/MS as TPIs. The mass spectrometry also made it possible to identify the presence of cysteine residues that could be subjected to S-glutathionylation, which regulate the enzyme activity.

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GSH depletion, protein S-glutathionylation and mitochondrial transmembrane potential hyperpolarization are early events in initiation of cell death induced by a mixture of isothiazolinones in HL60 cells

Cited by 61 publications

References 43 publications

Induction of cell death in prostate cancer cells by escopoletin, a promising treatment strategy

Induction of cell death in prostate cancer cells by escopoletin, a promising treatment strategy

Redox regulation of human estrogen sulfotransferase (hSULT1E1)

Triosephosphate Isomerases in Italian Ryegrass (Lolium multiflorum): Characterization and Susceptibility to Herbicides

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