Influence of the activity of glutathione reductase on the response of cultured lens epithelial cells from young and old rabbits to hydrogen peroxide

Reddan, John R.; Giblin, Frank J.; Dziedzic, Dorothy C.; McCready, Janet P.; Schrimscher, Lisa; Reddy, Venkat N.

doi:10.1016/s0014-4835(88)80078-2

Cited by 22 publications

(18 citation statements)

References 30 publications

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“…6) compared to cells from the other cell line, OB3L. One of the factors that may contribute to the increased susceptibility of line OB3L to H # O # insult is that these cells have a lower level of GR than line N\N 1003A (Reddan et al, 1988).…”

Section: Discussionmentioning

confidence: 98%

Thioltransferase is Present in the Lens Epithelial Cells as a Highly Oxidative Stress-resistant Enzyme

Lou

Wang²,

et al. 1998

Experimental Eye Research

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Section: Discussionmentioning

confidence: 98%

Thioltransferase is Present in the Lens Epithelial Cells as a Highly Oxidative Stress-resistant Enzyme

Lou

Wang²,

et al. 1998

Experimental Eye Research

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“…One of the major defenses of the lens against physiological levels of H2O2 is the glutathione redox cycle [6,7], However, cat alase is thought to play an important role in H2O2 detoxification when H2O2 exceeds the physiological level [5], High levels of H2O2 have been detected in the aqueous humor of humans with cataracts [2] and elevated lev els of H2O2 have been reported in the aqueous humor of animals exposed to cataractogenic doses of ultraviolet light or Xirradiation [4], The relative roles of catalase and of the glutathione redox cycle in H2O2 detoxifica tion have been investigated in cultured rab bit lens epithelial cells [11]. A significant contribution of catalase was noted when the H2O2 concentration exceeded the physiolog ical level of 0.03 mM.…”

Section: Discussionmentioning

confidence: 99%

“…Cultured lens epithelial cells from older rabbits are less effective in detoxifying H2O2 than cells from younger rabbits due in part to a less efficient glutathione redox cycle [7], A decrease in the ability of the lens epi thelium to detoxify H2C>2 would subject the interior of the lens to oxidative insult and could be a major contributing factor in the development of senile cataract.…”

Section: Discussionmentioning

confidence: 99%

“…This level of H2C>2 is known to bring about a decrease in the level of glutathione and in the subsequent growth of the cells [7], Disturbances in intracellular thiols, notably glutathione, and in calcium homeostasis can lead to cytotoxicity [14], The mitochondria contain the majority of the free calcium and are depositories of glu tathione. The H2C>2-induced mitochondrial damage noted here may influence the distri bution of glutathione and free calcium and account in part for the observed cytotoxicity.…”

Section: Discussionmentioning

confidence: 99%

“…The systems protecting the lens against oxidative damage are primarily concen trated in the epithelium [6,7]. The epithe lium contains catalase and superoxide dismutase, and has an active glutathione redox cycle [6].…”

Section: Introductionmentioning

confidence: 99%

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Histochemical Localization of Catalase in Cultured Lens Epithelial Cells

et al. 1989

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The diaminobenzidine (DAB) technique was used to investigate the localization of the peroxidatic activity of catalase in cultured lens epithelial cells at the ultrastructural level. Cultured rabbit, bovine and mouse lens epithelial cells incubated in an alkaline DAB reaction mixture contained catalase-positive microperoxisomes which were randomly distributed throughout the cytoplasm. The reaction product of catalase was abolished when cells were treated with 3-amino-l-H-l,2,4-triazole, a specific inhibitor of catalase, and was not detected when DAB or H₂O₂ was omitted from the incubation medium, or when the pH of the reaction mixture was lowered to 7.0. The fine structure of lens epithelial cells that were constantly exposed to 0.025 or 0.05 mM hydrogen peroxide was also determined. Lens epithelial cells that were constantly exposed to 0.05 mM H₂0₂ for 1–3 h exhibited damaged mitochondria, a phenomenon that did not occur when the cells were exposed to 0.025 mM peroxide

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Enzymatic metabolites of lycopene induce Nrf2‐mediated expression of phase II detoxifying/antioxidant enzymes in human bronchial epithelial cells

Lian

Wang

2008

Intl Journal of Cancer

144

102

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Lycopene can be cleaved by carotene 9 0 ,10 0 -oxygenase at its 9 0 ,10 0 double bond to form apo-10 0 -lycopenoids, including apo-10 0 -lycopenal, -lycopenol and -lycopenoic acid. The latter has been recently shown to inhibit lung carcinogenesis both in vivo and in vitro, however, the mechanism(s) underlying this protection is not well defined. In the present study, we report that treatment with apo-10 0 -lycopenoic acid, in a time-and dose-dependent manner, results in the nuclear accumulation of transcription factor Nrf2 (nuclear factor E 2 -related factor 2) protein in BEAS-2B human bronchial epithelial cells. The activation of Nrf2 by apo-10 0 -lycopenoic acid is associated with the induction of phase II detoxifying/antioxidant enzymes including heme oxygenase-1, NAD(P)H:quinone oxidoreductase 1, glutathione S-transferases, and glutamate-cysteine ligases in BEAS-2B cells. Furthermore, apo-10 0 -lycopenoic acid treatment increased total intracellular glutathione levels and suppressed both endogenous reactive oxygen species generation and H 2 O 2 -induced oxidative damage in BEAS-2B cells. In addition, both apo-10 0 -lycopenol and apo-10 0 -lycopenal induced heme oxygenase-1 gene expression in BEAS-2B cells. These data strongly suggest that the anti-carcinogenic and antioxidant functions of lycopene may be mediated by apo-10 0 -lycopenoids via activating Nrf2 and inducing phase II detoxifying/ antioxidant enzymes. ' 2008 Wiley-Liss, Inc.Key words: lycopene; apo-10 0 -lycopenoic acid; phase II enzymes; Nrf2; GSH; oxidative damageThe chemopreventive effect of lycopene, a carotenoid rich in tomato and tomato-based products, against cancers has been suggested in many epidemiological and animal studies. [1][2][3][4][5][6] One of explanations for the protective effect of lycopene is its ability to induce phase II detoxifying/antioxidant enzymes found in both in vitro and in vivo studies. [7][8][9] The induction of phase II detoxifying/antioxidant enzymes, such as heme oxygenase-1 (HO-1), NAD(P)H:quinone oxidoreductase 1 (NQO1), glutathione S-transferases (GSTs), glutathione reductase (GSR), glutamate-cysteine ligase (catalytic subunit, GCLC; and modifier subunit, GCLM), microsomal epoxide hydrolase 1 (mEH) and UDP glucuronosyltransferase 1 family, polypeptide A6 (UGT1A6), results in the detoxification of carcinogens and the inactivation of reactive oxygen species (ROS), contributing to the protective effect of chemopreventive agents. 10 Many of these enzymes are primarily regulated by the nuclear factor-E2 related factor 2 (Nrf2), a transcription factor that binds to the antioxidant response element (ARE) in the 5 0 -flanking region of target genes. 10 Under normal conditions, the majority of the Nrf2 is sequestered in the cytoplasm by Kelch-like erythroid Cap'n'Collar homologue-associated protein 1 (Keap 1), while only residual nuclear Nrf2 binds to the ARE, driving basal activities. Exposure to certain chemopreventive agents leads to the dissociation of the Nrf2-Keap1 complex in the cytoplasm and the translocatio...

show abstract

Influence of the activity of glutathione reductase on the response of cultured lens epithelial cells from young and old rabbits to hydrogen peroxide

Cited by 22 publications

References 30 publications

Thioltransferase is Present in the Lens Epithelial Cells as a Highly Oxidative Stress-resistant Enzyme

Thioltransferase is Present in the Lens Epithelial Cells as a Highly Oxidative Stress-resistant Enzyme

Histochemical Localization of Catalase in Cultured Lens Epithelial Cells

Enzymatic metabolites of lycopene induce Nrf2‐mediated expression of phase II detoxifying/antioxidant enzymes in human bronchial epithelial cells

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