Genetic variants in selenoprotein genes increase risk of colorectal cancer

Méplan, Catherine; Hughes, David J.; Pardini, Barbara; Naccarati, Alessio; Souček, Pavel; Vodičková, Ľudmila; Hlavata, I.; Vrána, David; Vodička, Pavel; Hesketh, John E.

doi:10.1093/carcin/bgq076

Cited by 131 publications

(130 citation statements)

References 40 publications

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“…Associations between six single-nucleotide polymorphisms (SNPs) of the earlier-mentioned five genes and CRC have been reported in different ethnic groups (Smith et al, 2001;Landi et al, 2003Landi et al, , 2005Krzesniak et al, 2004;Jiang et al, 2005;McGreavey et al, 2005;Murtaugh et al, 2005;Slattery et al, 2005Slattery et al, , 2006Berndt et al, 2006;Huang et al, 2006;Koh et al, 2006;Kuriki et al, 2006;Matsuo et al, 2006;Moreno et al, 2006;Theodoropoulos et al, 2006;Tranah et al, 2006;Hansen et al, 2007;Kang et al, 2007;Stern et al, 2007;Vogel et al, 2007;Yin et al, 2007;Kury et al, 2008;Funke et al, 2009;Khatami et al, 2009;Tsilidis et al, 2009;Yang et al, 2009;Engin et al, 2010;Meplan et al, 2010;Loh et al, 2011;Wu et al, 2011;Crous-Bou et al, 2012;Gil et al, 2012). These six variants comprised rs12917 and rs2308321 of MGMT, rs1229984 of ADH1B, rs4880 of SOD2, rs2228001 of XPC, and rs1801282 of PPARG.…”

Section: Introductionmentioning

confidence: 99%

Association Between Six Genetic Polymorphisms and Colorectal Cancer: A Meta-Analysis

Chen

Wang

Liao

et al. 2014

Genetic Testing and Molecular Biomarkers

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Objective: The aim of this study was to determine whether six genetic polymorphisms confer susceptibility to colorectal cancer (CRC). Methods: A systematic search for candidate genes of CRC was performed among several online databases, including PubMed, Embase, Web of Science, the Cochrane Library, CNKI, and Wanfang online libraries. After a comprehensive filtering procedure, we harvested five genes, including MGMT (rs12917 and rs2308321), ADH1B (rs1229984), SOD2 (rs4880), XPC (rs2228001), and PPARG (rs1801282). Using the REVMAN and Stata software, six meta-analyses were conducted for associations between CRC and the just-mentioned genetic variants. Results: A total of 34 comparative studies among 17,289 cases and 54,927 controls were involved in our meta-analyses. Significant association was found between ADH1B rs1229984 polymorphism and CRC ( p = 0.03, odds ratio [OR] = 1.18, 95% confidence interval [CI] = 1.01-1.36). We also found significant association between PPARG rs1801282 polymorphism and CRC ( p = 0.004, OR = 1.498, 95% CI = 1.139-1.970), and this significant association is specific in Caucasians ( p = 0.004, OR = 1.603, 95% CI = 1.165-2.205). Conclusions: The current meta-analysis has established that ADH1B (rs1229984) and PPARG (rs1801282) are two risk variants of CRC.

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Section: Introductionmentioning

confidence: 99%

Association Between Six Genetic Polymorphisms and Colorectal Cancer: A Meta-Analysis

Chen

Wang

Liao

et al. 2014

Genetic Testing and Molecular Biomarkers

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“…3 Variations in selenoprotein genes have been found to be associated with increased cancer risk. 4,5 Transgenic mice with reduced selenoprotein expression manifest precancerous changes. 6,7 Human studies have shown reduced cancer risk and DNA damage after selenium supplementation among those with lower basal plasma selenium.…”

Section: Introductionmentioning

confidence: 99%

Impact of heat treatment on size, structure, and bioactivity of elemental selenium nanoparticles

Zhang¹,

Taylor²,

Wan³

et al. 2012

IJN

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Background: Elemental selenium nanoparticles have emerged as a novel selenium source with the advantage of reduced risk of selenium toxicity. The present work investigated whether heat treatment affects the size, structure, and bioactivity of selenium nanoparticles. Methods and results: After a one-hour incubation of solution containing 80 nm selenium particles in a 90°C water bath, the nanoparticles aggregated into larger 110 nm particles and nanorods (290 nm × 70 nm), leading to significantly reduced bioavailability and phase II enzyme induction in selenium-deficient mice. When a solution containing 40 nm selenium nanoparticles was treated under the same conditions, the nanoparticles aggregated into larger 72 nm particles but did not transform into nanorods, demonstrating that the thermostability of selenium nanoparticles is size-dependent, smaller selenium nanoparticles being more resistant than larger selenium nanoparticles to transformation into nanorods during heat treatment. Conclusion:The present results suggest that temperature and duration of the heat process, as well as the original nanoparticle size, should be carefully selected when a solution containing selenium nanoparticles is added to functional foods.

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“…In the murine intestine, GPx4 mRNA is one of the most abundant selenoprotein transcripts (8); genetic variant analysis of the human GPX4 gene links it to malignant disease risk in the gastrointestinal tract (9,11). Investigation of intestinal GPx4 has so far been limited to the mRNA level (33,36) and to the measurement of GPx4 activity in mouse tissue homogenates (44).…”

Section: Discussionmentioning

confidence: 99%

“…A constant level of GPx4 mRNA during periods of limited selenium availability as against the concomitant degradation of other GPx isoforms such as GPx1 reflects the high ranking of GPx4 in the so-called selenoprotein hierarchy (32) and argues for an important role of this protein in enterocytes. Intriguingly, a function of GPx4 as a candidate mediator of selenium-dependent chemoprevention in the colon arises from studies on the association of a single nucleotide polymorphism (rs713041) in the human GPX4 gene with colorectal adenoma and colorectal cancer risk (9,11,18). The enzymatic capacity of GPx4 extends beyond those of other hydroperoxide-degrading GPx isoforms.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, a role for GPx4 in the prevention of mutagenesis has been suggested; GPx4 repairs oxidatively damaged DNA by reduction of thymine hydroperoxide (16), and increased levels of mutagenic DNA adducts have been detected in murine embryonic fibroblast cells from GPx4 ϩ/Ϫ mice (17). A functional variant of the human GPX4 gene has been identified (18), which is associated with increased risk of colorectal adenoma and colorectal cancer (9,11). The relevance of an adequate GPx4 expression for colon tissue homeostasis in humans notwithstanding information on protein expression, localization, and regulation of GPx4 in enterocytes is limited.…”

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confidence: 99%

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Induction of Glutathione Peroxidase 4 Expression during Enterocytic Cell Differentiation

Speckmann¹,

Bidmon²,

Pinto³

et al. 2011

Journal of Biological Chemistry

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Glutathione peroxidase 4 (GPx4), an abundant selenoenzyme, is ubiquitously expressed in a tissue-, cell-and differentiationdependent manner, and it is localized in cytoplasmic, mitochondrial, and nuclear cellular compartments. Here, we report cytoplasmic and nuclear localization of GPx4 in Caco-2 intestinal epithelial cells. Enterocytic differentiation of Caco-2 cells triggers an increase in GPx4 mRNA and protein levels, mediated by enhanced promoter activity. We identified a combined cAMP response element (CREB) and CCAAT/enhancer binding protein (C/EBP) site as critical for the differentiation-triggered GPx4 promoter activity. Induction of GPx4 correlated with C/EBP␣ transcript levels during differentiation, suggesting a role of C/EBP␣ as regulator of enterocytic GPx4 expression. Consistent with the in vitro results, GPx4 protein was detected in cytoplasmic and nuclear compartments of enterocytes in human intestinal epithelia. GPx4 is uniformly expressed in colonic crypts and is differentially expressed along the cryptto-villus axis in the small intestine with a more pronounced expression of GPx4 in the upper villi, which contain fully differentiated enterocytes. These data suggest that intestinal GPx4 expression is modulated by the enterocytic differentiation program, and the results support a direct role of nuclear GPx4 in the (selenium-dependent) prevention of oxidative damage in the gastrointestinal tract.The essential trace element selenium is of fundamental importance to human health, acting through low molecular weight selenium compounds as well as selenocysteine-containing selenoproteins (1). Adequate selenium intake, maintaining optimized expression and/or activity of selenoproteins, has been proposed to be beneficial with respect to prevention of several oxidative stress-related neurodegenerative and cardiovascular diseases and, most notably, cancer (1, 2). Secondary end point analyses of the Nutritional Prevention of Cancer study provided compelling evidence that dietary supplementation with 200 g selenium/day in form of high selenium yeast lowered the incidence of lung, prostate, and colorectal cancer as well as cancer mortality (3). Since the publication of this landmark trial, the anticarcinogenic capacity of selenium compounds has been further substantiated, particularly with regard to the gastrointestinal tract (4 -7). Mice with genetically impaired biosynthesis of selenoproteins due to a mutant selenocysteine transfer RNA gene have been shown to be more susceptible to colon cancer than wild-type mice, thus suggesting a key role for selenoproteins as mediators of the cancer-protective effects of selenium in the colon (5). Selenoproteins that are abundantly expressed in the healthy gastrointestinal tract and putatively relevant in malignant transformation comprise thioredoxin reductases, selenoprotein P, and glutathione peroxidases (GPx) 3 (8 -11). To date, five selenium-dependent GPx isoenzymes have been identified in humans: GPx1 and GPx2 are highly expressed in the intestinal epithelium, havi...

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Genetic variants in selenoprotein genes increase risk of colorectal cancer

Cited by 131 publications

References 40 publications

Association Between Six Genetic Polymorphisms and Colorectal Cancer: A Meta-Analysis

Association Between Six Genetic Polymorphisms and Colorectal Cancer: A Meta-Analysis

Impact of heat treatment on size, structure, and bioactivity of elemental selenium nanoparticles

Induction of Glutathione Peroxidase 4 Expression during Enterocytic Cell Differentiation

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