Inhibition of aflatoxin B1-induced cell injury by selenium: an in vitro study

Shi, Chenyang; Hew, Yin-Chin; Ong, Choon‐Nam

doi:10.1177/096032719501400111

Cited by 16 publications

(8 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These results suggested that Se supplementation significantly protected PK15 cells from OTA-induced cytotoxicity. Our results are consistent with that of previous studies, which found that Se significantly reduced T-2-induced cytotoxicity in human hepatoma cell line [ 33 ] and protected cells from AFB1-induced cytotoxicity in Chinese hamster ovary cells [ 34 ].…”

Section: Discussionsupporting

confidence: 93%

Selenium Alleviates Porcine Nephrotoxicity of Ochratoxin A by Improving Selenoenzyme Expression In Vitro

et al. 2015

View full text Add to dashboard Cite

Ochratoxin A (OTA), a mycotoxin, is a potent nephrotoxin in humans and animals. Selenium (Se) is an essential micronutrient for humans and animals, and plays a key role in antioxidant defense. To date, little is known about the effect of Se on OTA-induced nephrotoxicity. In this study, the protective effects of selenomethionine against OTA-induced nephrotoxicity were investigated using the porcine kidney 15 (PK15) cells as a model. The results showed that OTA induced nephrotoxicity in a dose-dependent manner. Se at 0.5, 1, 2 and 4 μM had significant protective effects against OTA-induced nephrotoxicity. Furthermore, selenomethionine enhanced the activity and mRNA and protein expression of glutathione peroxidase 1 (GPx1), mRNA expression of GPx4, and mRNA expression of thioredoxin reductase 1 in the presence and absence of OTA. Among them, promoting effect of selenomethionine on GPx1 was maximal. Knock-down of GPx1 by using a GPx1-specific siRNA eliminated the protective effects of selenomethionine against OTA-induced nephrotoxicity. The results suggest that selenomethionine alleviates OTA-induced nephrotoxicity by improving selenoenzyme expression in PK15 cells. Therefore, selenomethionine supplementation may be an attractive strategy for protecting humans and animals from the risk of kidney damage induced by OTA.

show abstract

Section: Discussionsupporting

confidence: 93%

Selenium Alleviates Porcine Nephrotoxicity of Ochratoxin A by Improving Selenoenzyme Expression In Vitro

et al. 2015

View full text Add to dashboard Cite

show abstract

“…The metabolite GS‐Se‐SG formed after excessive selenite exposure suppresses cell proliferation by inhibiting protein synthesis [36]. More and more evidence emerges that selenium plays a critical role in the protection of cells against various kinds of oxidative stress such as UV and ionizing radiation [37,38]. The mechanistic basis for these actions has now been related to the role of selenium as a catalyst for reversible cysteine/disulfide transformations in a number of redox‐regulated proteins [24].…”

Section: Discussionmentioning

confidence: 99%

Catalytic selenols couple the redox cycles of metallothionein and glutathione

Chen

Maret

2001

European Journal of Biochemistry

View full text Add to dashboard Cite

Co-ordination of zinc to the thiol group of cysteine allows mobilization of zinc through oxidation of its ligand. This molecular property links the binding and release of zinc in metallothionein (MT) to the cellular redox state Proc. Natl Acad. Sci. USA 95, 3483± 3488]. Biological disulfides such as glutathione disulfide (GSSG) oxidize MT with concomitant release of zinc, while glutathione (GSH) reduces the oxidized protein to thionein, which then binds to available zinc. Neither of these two redox processes is very efficient, even at high concentrations of GSSG or GSH. However, the GSH/GSSG redox pair can efficiently couple with the MT/thionein system in the presence of a selenium compound that has the capacity to form a catalytic selenol(ate). This coupling provides a very effective means of modulating oxidation and reduction.Remarkably, selenium compounds catalyze the oxidation of MT even under overall reducing conditions such as those prevailing in the cytosol. In this manner, the binding and release of zinc from zinc±thiolate co-ordination sites is linked to redox catalysis by selenium compounds, changes in the glutathione redox state, and the availability of either a zinc donor or a zinc acceptor. The results also suggest that the pharmacological actions of selenium compounds in cancer prevention and other antiviral and anti-inflammatory therapeutic applications, as well as unknown functions of selenium-containing proteins, may relate to coupling between the thiol redox state and the zinc state.Keywords: glutathione; metallothionein; redox signaling; selenium; zinc.Metallothioneins (MTs) are a family of closely related zinc proteins [1]. In the mammalian proteins, each zinc atom is bound tetrahedrally to four cysteines so as to form extensive zinc±thiolate cluster networks between seven zinc atoms and 20 highly conserved cysteines. These zinc±thiolate clusters have been postulated to operate via a redox mechanism in which the sulfur ligands are oxidized with concomitant release of zinc [2]. The low redox potential of the clusters allows oxidation by a number of mild cellular oxidants, among which disulfides such as glutathione disulfide (GSSG) and compounds with selenium in its lower oxidation states feature prominently. In vitro experiments have shown that the GSH/GSSG redox couple modulates zinc transfer from MT to zinc-depleted enzymes [3]. Based on this, it has been suggested that changes in the redox state serve as a driving force and signal for zinc distribution from its cellular reservoir in MT when zinc is needed.The oxidation of MT leads to various intramolecular or intermolecular disulfide bonds [4], a mixture that we now call thionin and which has been found in liver cytosol [5,6]. It is not known how thionin is reduced to thionein, the apoform of MT, so that the redox cycle can be completed and Zn±MT regenerated. Whereas numerous studies have investigated the oxidative release of zinc from MT in detail, those that have addressed the reductive step are fewer and the results are inconsistent. Fo...

show abstract

“…[13][14][15][16][17][18][19][20][21][22] Se 4þ also has been shown to inhibit AFB 1 hepatocarcinogenesis. 23 Although the selenium has an antimutagenic and anticarcinogenic effect, its optimal concentration is not known. At high concentrations, it is toxic, mutagenic and carcinogenic, while at low concentrations, it is antimutagenic and anticarcinogenic.…”

Section: Introductionmentioning

confidence: 99%

Protective effects of selenium against sister chromatid exchange induced by AFG 1 in human lymphocytes in vitro

et al. 2010

View full text Add to dashboard Cite

Aflatoxins have been shown to be hepatotoxic, carcinogenic, mutagenic and teratogenic to different species of animals. Besides, at low concentrations, Selenium (Se4+) is antimutagenic and anticarcinogenic while it is toxic, mutagenic and carcinogenic at high concentrations. In this study, we aimed to evaluate the effect of Se4+ against aflatoxin GAFG1 (AFG1) on blood cultures in relation to induction of sister chromatid exchange (SCE). The results showed that at 0.4 and 0.8 parts per million (ppm) concentration of AFG1, the frequency of SCE increased in cultured human lymphocytes. When different concentration of Se4+ (0.08 and 8 ppm) were added to AFG1, the frequencies of SCE decreased. Howewer, when 800 ppm concentration of Se4+ together with 0.08 ppm AFG1 were added to cell division inhibited in the cultures. Results suggested that Se4+ could effectively inhibit AFG1-induced SCE. Besides, the protective role of Se4+ against AFG1-induced SCE is probably related to its doses.

show abstract

Inhibition of aflatoxin B1-induced cell injury by selenium: an in vitro study

Cited by 16 publications

References 19 publications

Selenium Alleviates Porcine Nephrotoxicity of Ochratoxin A by Improving Selenoenzyme Expression In Vitro

Selenium Alleviates Porcine Nephrotoxicity of Ochratoxin A by Improving Selenoenzyme Expression In Vitro

Catalytic selenols couple the redox cycles of metallothionein and glutathione

Protective effects of selenium against sister chromatid exchange induced by AFG 1 in human lymphocytes in vitro

Contact Info

Product

Resources

About