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Roger A. Sunde - One of the best experts on this subject based on the ideXlab platform.
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impact of glutathione peroxidase 1 gpx1 genotype on selenoenzyme and transcript expression when repleting selenium deficient mice
2018Co-Authors: Roger A. Sunde, Edward T Zemaitis, Andrew B Blink, Julia A LawingerAbstract:Glutathione peroxidase (Gpx1) is the major selenoprotein in most tissues in animals. Knockout (KO) of Gpx1 decreases Gpx1 activity to near zero and substantially reduces liver selenium (Se) levels, but has no overt effects in otherwise healthy mice. To investigate the impact of deletion of Gpx1 on Se metabolism, Se flux, and apparent Se requirements, KO, Gpx1 heterozygous (Het), and Gpx1 wild-type (WT) mice were fed Se-deficient diet for 17 weeks, then repleted with graded levels of Se (0–0.3 μg Se/g as Na2SeO3) for 7 days, and selenoprotein activities and transcripts were determined in blood, liver, and kidney. Se deficiency decreased the activities of plasma GPX3, liver Gpx1, liver Txnrd, and liver Gpx4 to 3, 0.3, 11, and 50% of WT Se-adequate levels, respectively, but the Gpx1 genotype had no effect on growth or changes in activity or expression of selenoproteins other than Gpx1. Se repletion increased selenoprotein transcripts to Se-adequate levels after 7 days; Se response curves and apparent Se requirements for selenoprotein transcripts were similar to those observed in studies starting with Se-adequate mice. With short-term Se repletion, selenoenzyme activities resulted in three Se response curve patterns: (1) liver and kidney Gpx1, Gpx4, and Txnrd activities were sigmoidal or hyperbolic with breakpoints (0.08–0.19 μg Se/g) that were double those observed in studies starting with Se-adequate mice; (2) red blood cell Gpx1 activity was not significantly changed; and (3) plasma GPX3 activity only increased substantially with 0.3 μg Se/g. Plasma GPX3 is secreted from kidney. In this short-term study, kidney GPX3 mRNA reached plateau levels at 0.1 μg Se/g, and other kidney selenoenzyme activities reached plateau levels at ≤ 0.2 μg Se/g, so sufficient Se should have been present in kidney. Thus, the delayed increase in plasma GPX3 activity suggests that newly synthesized and secreted kidney GPX3 is preferentially retained in kidney or rapidly cleared by binding to basement membranes in kidney or in other tissues. This repletion study shows that loss of capacity to incorporate Se into Gpx1 in Gpx1 KO mice does not dramatically alter expression of other Se biomarkers, nor the short-term flux of Se from intestine to liver to kidney.
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Selenium regulation of selenoprotein enzyme activity and transcripts in a pilot study with Founder strains from the Collaborative Cross - Fig 2
2018Co-Authors: Roger A. SundeAbstract:Plasma GPX3 activity (A), RBC Gpx1 activity (B), liver Gpx1 activity (C), liver Gpx4 activity (D), and liver Txnrd (E) activity in male B6 mice fed 0 (-Se) or 0.2 μg Se/g (+Se) diet for 8 wk. Activities are expressed as enzyme unit/g protein. Values are mean ± SEM (n = 3/treatment); means with asterisks are significantly different from Se-adequate values (P
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Selenium regulation of selenoprotein enzyme activity and transcripts in a pilot study with Founder strains from the Collaborative Cross - Fig 3
2018Co-Authors: Roger A. SundeAbstract:Relative expression of plasma GPX3 activity (A), RBC Gpx1 activity (B), liver Gpx1 activity (C), liver Gpx4 activity (D), and liver Txnrd (E) activity. Activities are expressed as a percentage of activities in Se-adequate B6 mice. Left portion of each panel shows the relative activity in B6 mice fed 0 μg Se/g (-Se) and 0.2 μg Se/g (+Se) relative to +Se B6 mice; values are mean ± SEM (n = 3/treatment). Right portion of each panel shows the relative activities in -Se and +Se Founder mice as box-and-whisker plots, where the box delineates 25 to 75%, the bar in the box the median, and the error bars 10 and 90%; also shown are individual values linked by lines for each of the 8 strains. Means with asterisks are significantly different from Se-adequate values (P
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minimum selenium requirements increase when repleting second generation selenium deficient rats but are not further altered by vitamin e deficiency
2017Co-Authors: Roger A. Sunde, Kevin M Thompson, Kevin L Fritsche, Jacqueline K EvensonAbstract:Second-generation selenium-deficient weanling rats fed graded levels of dietary Se were used (a) to study the impact of initial Se deficiency on dietary Se requirements; (b) to determine if further decreases in selenoperoxidase expression, especially glutathione peroxidase 4 (Gpx4), affect growth or gross disease; and (c) to examine the impact of vitamin E deficiency on biochemical and molecular biomarkers of Se status. Rats were fed a vitamin E-deficient and Se-deficient crystalline amino acid diet (3 ng Se/g diet) or that diet supplemented with 100 μg/g all-rac-α-tocopheryl acetate and/or 0, 0.02, 0.05, 0.075, 0.1, or 0.2 μg Se/g diet as Na2SeO3 for 28 days. Se-supplemented rats grew 6.91 g/day as compared to 2.17 and 3.87 g/day for vitamin E-deficient/Se-deficient and vitamin E-supplemented/Se-deficient groups, respectively. In Se-deficient rats, liver Se, plasma GPX3, red blood cell Gpx1, liver Gpx1 and Gpx4 activities, and liver Gpx1 mRNA levels decreased to 50 % higher than in previous studies that started with Se-adequate rats, demonstrating that dietary Se requirements determined using initially Se-deficient animals can result in overestimation of Se requirements.
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Effect of dietary Se on significantly-regulated selenoprotein transcripts in turkey heart.
2017Co-Authors: Rachel M. Taylor, Roger A. SundeAbstract:Plotted are relative transcript levels for GPX1 (A), GPX3 (B), GPX4 (C), SELENOH (D), SELENOP1 (E), and SELENOT (F) in poults supplemented with graded levels of dietary Se for 28 d. Values shown are means ± SEM (n = 5/treatment). Means without a common letter are significantly different (p
Jun Qian - One of the best experts on this subject based on the ideXlab platform.
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GPX3 methylation in bone marrow predicts adverse prognosis and leukemia transformation in myelodysplastic syndrome
2017Co-Authors: Jingdong Zhou, Lei Yang, Xiangmei Wen, Jing Yang, Hong Guo, Jiang Lin, Tingjuan Zhang, Zhaoqun Deng, Jun QianAbstract:Epigenetic inactivation of GPX3 has been identified in various cancers including leukemia. Moreover, aberrant DNA methylation was also found as a dominant mechanism of disease progression in myelodysplastic syndrome (MDS). This study intended to explore GPX3 promoter methylation and its clinical relevance in 110 patients with MDS. GPX3 methylation was examined by real-time quantitative methylation-specific PCR (RQ-MSP) and bisulfite sequencing PCR (BSP). GPX3 methylation was identified in 15% (17/110) MDS patients, and significantly higher than controls, and lower than acute myeloid leukemia (AML) patients (P = 0.024 and 0.041). GPX3 methylated patients had older age and higher frequency of DNMT3A mutation (P = 0.015 and 0.066). Cases with GPX3 methylation showed significantly shorter overall survival (OS) time than those with GPX3 unmethylation analyzed with Kaplan-Meier analysis (P = 0.012). Moreover, Cox regression analysis revealed that GPX3 methylation might act as an independent prognostic indicator in MDS (HR = 1.847, P = 0.072). GPX3 methylation density was significantly increased during the progression from MDS to secondary acute myeloid leukemia (sAML) in three follow-up paired patients. Our study concludes that GPX3 methylation in bone marrow is associated with adverse prognosis and leukemia transformation in MDS.
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GPX3 promoter is methylated in chronic myeloid leukemia
2015Co-Authors: Dongming Yao, Jingdong Zhou, Yingying Zhang, Lei Yang, Xiangmei Wen, Jing Yang, Hong Guo, Qin Chen, Jiang Lin, Jun QianAbstract:Hypermethylation of GPX3 (glutathione peroxidase 3) promoter has been identified in various cancers. However, the pattern of GPX3 promoter methylation in chronic myeloid leukemia (CML) remains unknown. Our study was aimed to investigate the methylation status of GPX3 promoter and its clinical relevance in CML. Real-time quantitative methylation-specific PCR and bisulfite sequencing PCR was performed to detect the level of GPX3 methylation in 80 CML patients and 44 controls. GPX3 promoter in CML patients was significantly methylated compared with controls (P = 0.007). GPX3 highly methylated patients showed significantly older age than GPX3 lowly methylated patients (P = 0.037). However, patients with GPX3 methylation had significantly lower white blood cells than those with low GPX3 methylation (P = 0.006). BCR-ABL transcript in GPX3 highly methylated patients was a little lower than that in GPX3 lowly methylated patients (P = 0.161). No significant differences were observed in the frequency of GPX3 methylation in the different stages of CML (P = 1.000). Significantly negative correlation was observed between GPX3 expression and GPX3 methylation (R = -0.442, P = 0.004). GPX3 mRNA level in K562 cell line was significantly increased after 5-aza-2’-deoxycytidine treatment, and GPX3 methylation level was decreased. GPX3 hypermethylation is frequent in CML and is negatively associated with its expression.
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GPX3 hypermethylation serves as an independent prognostic biomarker in non m3 acute myeloid leukemia
2015Co-Authors: Jingdong Zhou, Dongming Yao, Yingying Zhang, Xiangmei Wen, Jing Yang, Hong Guo, Qin Chen, Jiang Lin, Jun QianAbstract:Hypermethylation of GPX3 (glutathione peroxidase 3) promoter has been identified in various solid tumors. However, the pattern of GPX3 promoter methylation in acute myeloid leukemia (AML) remains unknown. The current study was intended to investigate the clinical significance of GPX3 promoter methylation in de novo AML patients and further determine its role in regulating GPX3 expression. GPX3 promoter methylation status was detected in 181 de novo AML patients and 44 normal controls by real-time quantitative methylation-specific PCR and bisulfite sequencing PCR. Real-time quantitative PCR was carried out to assess GPX3 expression. GPX3 promoter was significantly methylated in AML patients compared with normal controls (P=0.022). The patients with GPX3 methylation presented significantly older age than those with GPX3 unmethylation (P=0.011). GPX3 methylated patients had significantly lower frequency of C/EBPA mutation and higher incidence of FLT3-ITD mutation (P=0.037 and 0.030, respectively). The non-M3 patients with GPX3 methylation had significantly lower overall survival than those with GPX3 unmethylation (P=0.036). No significant correlation was observed between GPX3 expression and its promoter methylation (R=0.110, P=0.284). However, GPX3 mRNA level was significantly increased after 5-aza-2’-deoxycytidine treatment in leukemic cell line THP1. Our data suggest that GPX3 methylation predicts adverse clinical outcome in non-M3 AML patients. Moreover, GPX3 expression is regulated by its promoter methylation in leukemic cell line THP1.
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down regulation of GPX3 is associated with favorable intermediate karyotypes in de novo acute myeloid leukemia
2015Co-Authors: Jingdong Zhou, Dongming Yao, Yingying Zhang, Lei Yang, Xiangmei Wen, Jing Yang, Hong Guo, Jiang Lin, Jun QianAbstract:Decreased glutathione peroxidase 3 (GPX3) expression has been identified in numerous solid tumors. However, GPX3 expression pattern in acute myeloid leukemia (AML) remains poorly known. Our study was intended to explore GPX3 expression status and further analyze the clinical relevance of GPX3 expression in AML. GPX3 mRNA level was detected by real-time quantitative PCR in 122 de novo AML patients and 44 normal controls. GPX3 transcript level was significantly decreased compared with normal controls (P 0.05). Reduced GPX3 expression is associated with favorable/intermediate karyotypes but not with survival in de novo AML patients.
Jingdong Zhou - One of the best experts on this subject based on the ideXlab platform.
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GPX3 methylation in bone marrow predicts adverse prognosis and leukemia transformation in myelodysplastic syndrome
2017Co-Authors: Jingdong Zhou, Lei Yang, Xiangmei Wen, Jing Yang, Hong Guo, Jiang Lin, Tingjuan Zhang, Zhaoqun Deng, Jun QianAbstract:Epigenetic inactivation of GPX3 has been identified in various cancers including leukemia. Moreover, aberrant DNA methylation was also found as a dominant mechanism of disease progression in myelodysplastic syndrome (MDS). This study intended to explore GPX3 promoter methylation and its clinical relevance in 110 patients with MDS. GPX3 methylation was examined by real-time quantitative methylation-specific PCR (RQ-MSP) and bisulfite sequencing PCR (BSP). GPX3 methylation was identified in 15% (17/110) MDS patients, and significantly higher than controls, and lower than acute myeloid leukemia (AML) patients (P = 0.024 and 0.041). GPX3 methylated patients had older age and higher frequency of DNMT3A mutation (P = 0.015 and 0.066). Cases with GPX3 methylation showed significantly shorter overall survival (OS) time than those with GPX3 unmethylation analyzed with Kaplan-Meier analysis (P = 0.012). Moreover, Cox regression analysis revealed that GPX3 methylation might act as an independent prognostic indicator in MDS (HR = 1.847, P = 0.072). GPX3 methylation density was significantly increased during the progression from MDS to secondary acute myeloid leukemia (sAML) in three follow-up paired patients. Our study concludes that GPX3 methylation in bone marrow is associated with adverse prognosis and leukemia transformation in MDS.
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GPX3 promoter is methylated in chronic myeloid leukemia
2015Co-Authors: Dongming Yao, Jingdong Zhou, Yingying Zhang, Lei Yang, Xiangmei Wen, Jing Yang, Hong Guo, Qin Chen, Jiang Lin, Jun QianAbstract:Hypermethylation of GPX3 (glutathione peroxidase 3) promoter has been identified in various cancers. However, the pattern of GPX3 promoter methylation in chronic myeloid leukemia (CML) remains unknown. Our study was aimed to investigate the methylation status of GPX3 promoter and its clinical relevance in CML. Real-time quantitative methylation-specific PCR and bisulfite sequencing PCR was performed to detect the level of GPX3 methylation in 80 CML patients and 44 controls. GPX3 promoter in CML patients was significantly methylated compared with controls (P = 0.007). GPX3 highly methylated patients showed significantly older age than GPX3 lowly methylated patients (P = 0.037). However, patients with GPX3 methylation had significantly lower white blood cells than those with low GPX3 methylation (P = 0.006). BCR-ABL transcript in GPX3 highly methylated patients was a little lower than that in GPX3 lowly methylated patients (P = 0.161). No significant differences were observed in the frequency of GPX3 methylation in the different stages of CML (P = 1.000). Significantly negative correlation was observed between GPX3 expression and GPX3 methylation (R = -0.442, P = 0.004). GPX3 mRNA level in K562 cell line was significantly increased after 5-aza-2’-deoxycytidine treatment, and GPX3 methylation level was decreased. GPX3 hypermethylation is frequent in CML and is negatively associated with its expression.
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GPX3 hypermethylation serves as an independent prognostic biomarker in non m3 acute myeloid leukemia
2015Co-Authors: Jingdong Zhou, Dongming Yao, Yingying Zhang, Xiangmei Wen, Jing Yang, Hong Guo, Qin Chen, Jiang Lin, Jun QianAbstract:Hypermethylation of GPX3 (glutathione peroxidase 3) promoter has been identified in various solid tumors. However, the pattern of GPX3 promoter methylation in acute myeloid leukemia (AML) remains unknown. The current study was intended to investigate the clinical significance of GPX3 promoter methylation in de novo AML patients and further determine its role in regulating GPX3 expression. GPX3 promoter methylation status was detected in 181 de novo AML patients and 44 normal controls by real-time quantitative methylation-specific PCR and bisulfite sequencing PCR. Real-time quantitative PCR was carried out to assess GPX3 expression. GPX3 promoter was significantly methylated in AML patients compared with normal controls (P=0.022). The patients with GPX3 methylation presented significantly older age than those with GPX3 unmethylation (P=0.011). GPX3 methylated patients had significantly lower frequency of C/EBPA mutation and higher incidence of FLT3-ITD mutation (P=0.037 and 0.030, respectively). The non-M3 patients with GPX3 methylation had significantly lower overall survival than those with GPX3 unmethylation (P=0.036). No significant correlation was observed between GPX3 expression and its promoter methylation (R=0.110, P=0.284). However, GPX3 mRNA level was significantly increased after 5-aza-2’-deoxycytidine treatment in leukemic cell line THP1. Our data suggest that GPX3 methylation predicts adverse clinical outcome in non-M3 AML patients. Moreover, GPX3 expression is regulated by its promoter methylation in leukemic cell line THP1.
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down regulation of GPX3 is associated with favorable intermediate karyotypes in de novo acute myeloid leukemia
2015Co-Authors: Jingdong Zhou, Dongming Yao, Yingying Zhang, Lei Yang, Xiangmei Wen, Jing Yang, Hong Guo, Jiang Lin, Jun QianAbstract:Decreased glutathione peroxidase 3 (GPX3) expression has been identified in numerous solid tumors. However, GPX3 expression pattern in acute myeloid leukemia (AML) remains poorly known. Our study was intended to explore GPX3 expression status and further analyze the clinical relevance of GPX3 expression in AML. GPX3 mRNA level was detected by real-time quantitative PCR in 122 de novo AML patients and 44 normal controls. GPX3 transcript level was significantly decreased compared with normal controls (P 0.05). Reduced GPX3 expression is associated with favorable/intermediate karyotypes but not with survival in de novo AML patients.
Laurent Chavatte - One of the best experts on this subject based on the ideXlab platform.
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selenoprotein gene nomenclature
2016Co-Authors: Raymond F. Burk, Brigelius Flohe Regina, Sergi Castellano, Elspeth A Bruford, Elias S J Arner, Bradley A. Carlson, Marla J Berry, Laurent ChavatteAbstract:Abstract The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These proteins are involved in a variety of functions, most notably redox homeostasis. Selenoprotein enzymes with known functions are designated according to these functions: TXNRD1, TXNRD2, and TXNRD3 (thioredoxin reductases), GPX1, GPX2, GPX3, GPX4 and GPX6 (glutathione peroxidases), DIO1, DIO2, and DIO3 (iodothyronine deiodinases), MSRB1 (methionine-R-sulfoxide reductase 1) and SEPHS2 (selenophosphate synthetase 2). Selenoproteins without known functions have traditionally been denoted by SEL or SEP symbols. However, these symbols are sometimes ambiguous and conflict with the approved nomenclature for several other genes. Therefore, there is a need to implement a rational and coherent nomenclature system for selenoprotein-encoding genes. Our solution is to use the root symbol SELENO followed by a letter. This nomenclature applies to SELENOF (selenoprotein F, the 15 kDa selenoprotein, SEP15), SELENOH (selenoprotein H, SELH, C11orf31), SELENOI (selenoprotein I, SELI, EPT1), SELENOK (selenoprotein K, SELK), SELENOM (selenoprotein M, SELM), SELENON (selenoprotein N, SEPN1, SELN), SELENOO (selenoprotein O, SELO), SELENOP (selenoprotein P, SeP, SEPP1, SELP), SELENOS (selenoprotein S, SELS, SEPS1, VIMP), SELENOT (selenoprotein T, SELT), SELENOV (selenoprotein V, SELV) and SELENOW (selenoprotein W, SELW, SEPW1). This system, approved by the HUGO Gene Nomenclature Committee, also resolves conflicting, missing and ambiguous designations for selenoprotein genes and is applicable to selenoproteins across vertebrates.
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selenoprotein gene nomenclature
2016Co-Authors: Raymond F. Burk, Brigelius Flohe Regina, Sergi Castellano, Elspeth A Bruford, Elias S J Arner, Bradley A. Carlson, Marla J Berry, Laurent ChavatteAbstract:Abstract The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These proteins are involved in a variety of functions, most notably redox homeostasis. Selenoprotein enzymes with known functions are designated according to these functions: TXNRD1, TXNRD2, and TXNRD3 (thioredoxin reductases), GPX1, GPX2, GPX3, GPX4 and GPX6 (glutathione peroxidases), DIO1, DIO2, and DIO3 (iodothyronine deiodinases), MSRB1 (methionine-R-sulfoxide reductase 1) and SEPHS2 (selenophosphate synthetase 2). Selenoproteins without known functions have traditionally been denoted by SEL or SEP symbols. However, these symbols are sometimes ambiguous and conflict with the approved nomenclature for several other genes. Therefore, there is a need to implement a rational and coherent nomenclature system for selenoprotein-encoding genes. Our solution is to use the root symbol SELENO followed by a letter. This nomenclature applies to SELENOF (selenoprotein F, the 15 kDa selenoprotein, SEP15), SELENOH (selenoprotein H, SELH, C11orf31), SELENOI (selenoprotein I, SELI, EPT1), SELENOK (selenoprotein K, SELK), SELENOM (selenoprotein M, SELM), SELENON (selenoprotein N, SEPN1, SELN), SELENOO (selenoprotein O, SELO), SELENOP (selenoprotein P, SeP, SEPP1, SELP), SELENOS (selenoprotein S, SELS, SEPS1, VIMP), SELENOT (selenoprotein T, SELT), SELENOV (selenoprotein V, SELV) and SELENOW (selenoprotein W, SELW, SEPW1). This system, approved by the HUGO Gene Nomenclature Committee, also resolves conflicting, missing and ambiguous designations for selenoprotein genes and is applicable to selenoproteins across vertebrates.
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the differential expression of glutathione peroxidase 1 and 4 depends on the nature of the secis element
2012Co-Authors: Lynda Latreche, Stephane Duhieu, Zahia Touathamici, Olivier Jeanjean, Laurent ChavatteAbstract:Selenocysteine insertion into selenoproteins involves the translational recoding of UGA stop codons. In mammals, selenoprotein expression further depends on selenium availability, which has been particularly described for glutathione peroxidase 1 and 4 (Gpx1 and Gpx4). The SECIS element located in the 3′UTR of the selenoprotein mRNAs is a modulator of UGA recoding efficiency in adequate selenium conditions. One of the current models for the UGA recoding mechanism proposes that the SECIS binds SECIS-binding protein 2 (SBP2), which then recruits a selenocysteine-specific elongation factor (EFsec) and tRNASec to the ribosome, where L30 acts as an anchor. The involvement of the SECIS in modulation of UGA recoding activity was investigated, together with SBP2 and EFsec, in Hek293 cells cultured with various selenium levels. Luciferase reporter constructs, in transiently or stably expressing cell lines, were used to analyze the differential expression of Gpx1 and Gpx4. We showed that, upon selenium fluctuation,...
Brigelius Flohe Regina - One of the best experts on this subject based on the ideXlab platform.
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selenoprotein gene nomenclature
2016Co-Authors: Raymond F. Burk, Brigelius Flohe Regina, Sergi Castellano, Elspeth A Bruford, Elias S J Arner, Bradley A. Carlson, Marla J Berry, Laurent ChavatteAbstract:Abstract The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These proteins are involved in a variety of functions, most notably redox homeostasis. Selenoprotein enzymes with known functions are designated according to these functions: TXNRD1, TXNRD2, and TXNRD3 (thioredoxin reductases), GPX1, GPX2, GPX3, GPX4 and GPX6 (glutathione peroxidases), DIO1, DIO2, and DIO3 (iodothyronine deiodinases), MSRB1 (methionine-R-sulfoxide reductase 1) and SEPHS2 (selenophosphate synthetase 2). Selenoproteins without known functions have traditionally been denoted by SEL or SEP symbols. However, these symbols are sometimes ambiguous and conflict with the approved nomenclature for several other genes. Therefore, there is a need to implement a rational and coherent nomenclature system for selenoprotein-encoding genes. Our solution is to use the root symbol SELENO followed by a letter. This nomenclature applies to SELENOF (selenoprotein F, the 15 kDa selenoprotein, SEP15), SELENOH (selenoprotein H, SELH, C11orf31), SELENOI (selenoprotein I, SELI, EPT1), SELENOK (selenoprotein K, SELK), SELENOM (selenoprotein M, SELM), SELENON (selenoprotein N, SEPN1, SELN), SELENOO (selenoprotein O, SELO), SELENOP (selenoprotein P, SeP, SEPP1, SELP), SELENOS (selenoprotein S, SELS, SEPS1, VIMP), SELENOT (selenoprotein T, SELT), SELENOV (selenoprotein V, SELV) and SELENOW (selenoprotein W, SELW, SEPW1). This system, approved by the HUGO Gene Nomenclature Committee, also resolves conflicting, missing and ambiguous designations for selenoprotein genes and is applicable to selenoproteins across vertebrates.
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selenoprotein gene nomenclature
2016Co-Authors: Raymond F. Burk, Brigelius Flohe Regina, Sergi Castellano, Elspeth A Bruford, Elias S J Arner, Bradley A. Carlson, Marla J Berry, Laurent ChavatteAbstract:Abstract The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These proteins are involved in a variety of functions, most notably redox homeostasis. Selenoprotein enzymes with known functions are designated according to these functions: TXNRD1, TXNRD2, and TXNRD3 (thioredoxin reductases), GPX1, GPX2, GPX3, GPX4 and GPX6 (glutathione peroxidases), DIO1, DIO2, and DIO3 (iodothyronine deiodinases), MSRB1 (methionine-R-sulfoxide reductase 1) and SEPHS2 (selenophosphate synthetase 2). Selenoproteins without known functions have traditionally been denoted by SEL or SEP symbols. However, these symbols are sometimes ambiguous and conflict with the approved nomenclature for several other genes. Therefore, there is a need to implement a rational and coherent nomenclature system for selenoprotein-encoding genes. Our solution is to use the root symbol SELENO followed by a letter. This nomenclature applies to SELENOF (selenoprotein F, the 15 kDa selenoprotein, SEP15), SELENOH (selenoprotein H, SELH, C11orf31), SELENOI (selenoprotein I, SELI, EPT1), SELENOK (selenoprotein K, SELK), SELENOM (selenoprotein M, SELM), SELENON (selenoprotein N, SEPN1, SELN), SELENOO (selenoprotein O, SELO), SELENOP (selenoprotein P, SeP, SEPP1, SELP), SELENOS (selenoprotein S, SELS, SEPS1, VIMP), SELENOT (selenoprotein T, SELT), SELENOV (selenoprotein V, SELV) and SELENOW (selenoprotein W, SELW, SEPW1). This system, approved by the HUGO Gene Nomenclature Committee, also resolves conflicting, missing and ambiguous designations for selenoprotein genes and is applicable to selenoproteins across vertebrates.
