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Search on : Selenomethionine [Words]
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[PMID]: 29518925
[Au] Autor:Lu X; He Z; Lin Z; Zhu Y; Yuan L; Liu Y; Yin X
[Ad] Address:School of Earth and Space Sciences, University of Science and Technology of China, Hefei 230026, China. lusokey@163.com.
[Ti] Title:Effects of Chinese Cooking Methods on the Content and Speciation of Selenium in Selenium Bio-Fortified Cereals and Soybeans.
[So] Source:Nutrients;10(3), 2018 Mar 07.
[Is] ISSN:2072-6643
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:Cereals and soybeans are the main food sources for the majority of Chinese. This study evaluated the effects of four common cooking methods including steaming, boiling, frying, and milking on selenium (Se) content and speciation in seven selenium bio-fortified cereals and soybeans samples. The Se concentrations in the selected samples ranged from 0.91 to 110.8 mg/kg and selenomethionine (SeMet) was detected to be the main Se species. Total Se loss was less than 8.1% during the processes of cooking except milking, while 49.1% of the total Se was lost in milking soybean for soy milk due to high level of Se in residuals. It was estimated that about 13.5, 24.0, 3.1, and 46.9% of SeMet were lost during the processes of steaming, boiling, frying, and milking, respectively. Meanwhile, selenocystine (SeCys2) and methylselenocysteine (SeMeCys) were lost completely from the boiled cereals. Hence, steaming and frying were recommended to cook Se-biofortified cereals in order to minimize the loss of Se.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Process

  2 / 2791 MEDLINE  
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[PMID]: 29506230
[Au] Autor:Cemin HS; Vieira SL; Stefanello C; Kindlein L; Ferreira TZ; Fireman AK
[Ad] Address:Department of Animal Science, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 7712, Porto Alegre, RS, Brazil, 91540-000.
[Ti] Title:Broiler responses to increasing selenium supplementation using Zn-L-selenomethionine with special attention to breast myopathies.
[So] Source:Poult Sci;, 2018 Feb 28.
[Is] ISSN:1525-3171
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:A study was conducted to evaluate growth performance, carcass and breast yields, and the occurrence and severity of white striping (WS) and wooden breast (WB) myopathies of broilers fed diets supplemented with increasing dietary levels of an organic source of selenium (Zn-L-SeMet). Broilers were fed 6 treatments with 12 replications of 26 birds in a 4-phase feeding program from 1 to 42 days. Corn-soy-based diets were supplemented with 0, 0.2, 0.4, 0.6, 0.8, and 1.0 ppm of Zn-L-SeMet. At 42 d, 6 birds were randomly selected from each pen (n = 72) and processed for carcass and breast yields. Breast fillets were scored for WS and WB at 42 days. Increasing Zn-L-SeMet led to quadratic responses (P < 0.05) for FCR from 1 to 7 d, BWG from 22 to 35 d, and for both responses from 8 to 21 d and 36 to 42 d, as well as in the overall period of 42 days. Carcass and breast yields presented a quadratic improvement (P < 0.01) with increasing Zn-L-SeMet supplementation and Se requirements were estimated at 0.85 and 0.86 ppm, respectively. In the overall period, estimates of Se requirements were 0.64 ppm for BWG and 0.67 ppm for FCR. White striping and WB scores presented quadratic increases (P < 0.01), and maximum scores were observed at 0.68 and 0.67 ppm, respectively. Broilers fed diets formulated without Se supplementation had a higher percentage of normal fillets compared to other Se supplementation levels (quadratic, P < 0.05). In conclusion, increasing Se supplementation to reach maximum growth performance led to higher degrees of severity of WS and WB. Selenium requirements determined in the present study were significantly higher than the present commercial recommendations.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[St] Status:Publisher
[do] DOI:10.3382/ps/pey001

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[PMID]: 29482023
[Au] Autor:Naderi M; Salahinejad A; Ferrari MCO; Niyogi S; Chivers DP
[Ad] Address:Department of Biology, University of Saskatchewan, 112 Science Place, Saskatoon, SK S7N 5E2, Canada. Electronic address: Mohammad.naderi@usask.ca.
[Ti] Title:Dopaminergic dysregulation and impaired associative learning behavior in zebrafish during chronic dietary exposure to selenium.
[So] Source:Environ Pollut;237:174-185, 2018 Feb 23.
[Is] ISSN:1873-6424
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:A growing body of evidence indicates that exposure to selenium (Se) can cause neurotoxicity, and this can occur because of its interference with several neurotransmitter systems in humans and animals. Dopamine is a critical modulator of a variety of brain functions and a prime target for environmental neurotoxicants. However, effects of environmentally relevant concentrations of Se on dopaminergic system and its neurobehavioral effects are still largely unknown. For this purpose, we exposed zebrafish, a model organism, to different concentrations of dietary l-selenomethionine (control, 3.5, 11.1, 27.4, and 63.4 µg Se/g dry weight) for a period of 60 days. Cognitive performance of fish was evaluated using a plus maze associative learning paradigm. Oxidative stress, as the main driver of Se neurotoxicity, was assessed by measuring the ratio of reduced to oxidized glutathione (GSH:GSSG), lipid peroxidation (LPO) levels, and mRNA expression of several antioxidant enzymes in the zebrafish brain. Dopamine levels in the brain and the expression of genes involved in dopamine synthesis, storage, reuptake, metabolism, and receptor activation were examined. Moreover, transcription of several synaptic plasticity-related immediate-early and late response genes was determined. Overall, fish fed with the two highest concentrations of dietary Se displayed impaired associative learning. Se exposure also induced oxidative stress in the zebrafish brain, as indicated by a reduction in GSH:GSSG ratio, increased LPO levels, and up-regulation of antioxidant genes in fish treated with the two highest concentrations of Se. An increase in brain dopamine levels associated with altered expression of dopaminergic cell markers was evident in different treatment groups. Moreover, Se exposure led to the down-regulation of immediate-early and late response genes in fish that exhibiting learning impairment. Taken together, the results of this study imply that the induction of oxidative stress and dysregulation of dopaminergic neurotransmission may underlie Se-induced impairment of associative learning in zebrafish.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180226
[Lr] Last revision date:180226
[St] Status:Publisher

  4 / 2791 MEDLINE  
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[PMID]: 29199992
[Au] Autor:Oulavallickal T; Brewster JL; McKellar JLO; Fairhurst MJ; Tenci NA; Gerth ML
[Ad] Address:Department of Biochemistry, University of Otago, PO Box 56, Dunedin, Otago 9054, New Zealand.
[Ti] Title:The Pseudomonas syringae pv. actinidiae chemoreceptor protein F (PscF) periplasmic sensor domain: cloning, purification and X-ray crystallographic analysis.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 12):701-705, 2017 Dec 01.
[Is] ISSN:2053-230X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Nitrate- and nitrite-sensing (NIT) domains are found associated with a wide variety of bacterial receptors, including chemoreceptors. However, the structure of a chemoreceptor-associated NIT domain has not yet been characterized. Recently, a chemoreceptor named PscF was identified from the plant pathogen Pseudomonas syringae pv. actinidiae that is predicted to contain a periplasmic NIT domain. The PscF sensor domain (PscF-SD; residues 42-332) was cloned into an appropriate expression vector, recombinantly produced in Escherichia coli BL21-Gold(DE3) cells and purified via immobilized metal-affinity and size-exclusion chromatography. Purified PscF-SD was screened for crystallization; the best crystal diffracted to a maximum resolution of 1.46 Šin space group P2 2 2 . However, the data could not be phased using the only available NIT-domain structure (Klebsiella oxytoca NasR; PDB entry 4akk) as the search model. Therefore, a data set from a selenomethionine-labelled protein crystal was also collected. The selenomethionine-labelled protein crystal diffracted to a resolution of 2.46 Šin space group P2 2 2 . These data will be used to attempt to solve the structure using the single-wavelength anomalous diffraction technique. The structure is expected to provide insights into the ligand specificity of NIT domains and the role of NIT domains in chemotaxis.
[Mh] MeSH terms primary: Bacterial Proteins/chemistry
Bacterial Proteins/genetics
Pseudomonas syringae/chemistry
[Mh] MeSH terms secundary: Bacterial Proteins/isolation & purification
Chemotactic Factors
Chromatography, Affinity
Chromatography, Gel
Cloning, Molecular
Crystallography, X-Ray
Nitrates/chemistry
Nitrates/metabolism
Nitrites/chemistry
Nitrites/metabolism
Periplasm/metabolism
Protein Domains
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Bacterial Proteins); 0 (Chemotactic Factors); 0 (Nitrates); 0 (Nitrites)
[Em] Entry month:1802
[Cu] Class update date: 180222
[Lr] Last revision date:180222
[Js] Journal subset:IM
[Da] Date of entry for processing:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17016831

  5 / 2791 MEDLINE  
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[PMID]: 29439710
[Au] Autor:Qian G; Liu D; Hu J; Gan F; Hou L; Zhai N; Chen X; Huang K
[Ad] Address:College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, 210095, Jiangsu Province, China.
[Ti] Title:SeMet attenuates OTA-induced PCV2 replication promotion by inhibiting autophagy by activating the AKT/mTOR signaling pathway.
[So] Source:Vet Res;49(1):15, 2018 Feb 13.
[Is] ISSN:1297-9716
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Porcine circovirus type 2 (PCV2) is recognized as the causative agent of porcine circovirus-associated diseases. PCV2 replication could be promoted by low doses of ochratoxin A (OTA) as in our previous study and selenium has been shown to attenuate PCV2 replication. However, the underlying mechanism remains unclear. The aim of the study was to investigate the effects of selenomethionine (SeMet), the major component of organic selenium, on OTA-induced PCV2 replication promotion and its potential mechanism. The present study demonstrates that OTA could promote PCV2 replication as measured by cap protein expression, viral titer, viral DNA copies and the number of infected cells. In addition, OTA could activate autophagy as indicated by up-regulated light chain 3 (LC3)-II and autophagy-related protein 5 expressions and autophagosome formation. Further, OTA could down-regulate p-AKT and p-mTOR expressions and OTA-induced autophagy was inhibited when insulin was applied. SeMet at 2, 4 and 6 µM had significant inhibiting effects against OTA-induced PCV2 replication promotion. Furthermore, SeMet could attenuate OTA-induced autophagy and up-regulate OTA-induced p-AKT and p-mTOR expression inhibition. Rapamycin, an inhibitor of AKT/mTOR, could reverse the effects of SeMet on OTA-induced autophagy and the PCV2 replication promotion. In conclusion, SeMet could block OTA-induced PCV2 replication promotion by inhibiting autophagy by activating the AKT/mTOR pathway. Therefore, SeMet supplementation could be an effective prophylactic strategy against PCV2 infections and autophagy may be a potential marker to develop novel anti-PCV2 drugs.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180218
[Lr] Last revision date:180218
[St] Status:In-Data-Review
[do] DOI:10.1186/s13567-018-0508-z

  6 / 2791 MEDLINE  
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[PMID]: 29439473
[Au] Autor:Bierla K; Lobinski R; Szpunar J
[Ad] Address:Institute of Analytical Sciences, IPREM, UMR 5254, CNRS-UPPA, Hélioparc, 2 Avenue Angot, 64053 Pau, France. katarzyna.bierla@univ-pau.fr.
[Ti] Title:Determination of Proteinaceous Selenocysteine in Selenized Yeast.
[So] Source:Int J Mol Sci;19(2), 2018 Feb 11.
[Is] ISSN:1422-0067
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:A method for the quantitation of proteinaceous selenocysteine (SeCys) in Se-rich yeast was developed. The method is based on the reduction of the Se-Se and S-Se bridges with dithiotretiol, derivatization with iodoacetamide (carbamidomethylation), followed by HPLC-ICP MS. The chromatographic conditions were optimized for the total recovery of the proteinaceous selenocysteine, the minimum number of peaks in the chromatogram (reduction of derivatization products of other Se-species present) and the baseline separation. A typical chromatogram of a proteolytic digest of selenized yeast protein consisted of up to five peaks (including SeMet, carbamidomethylated (CAM)-SeCys, and Se(CAM)2) identified by retention time matching with available standards and electrospray MS. Inorganic selenium non-specifically attached to proteins and selenomethionine could be quantified (in the form of Se(CAM)2) along with SeCys. Selenocysteine, selenomethionine, inorganic selenium, and the water soluble-metabolite fraction accounted for the totality of selenium species in Se-rich yeast.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180214
[Lr] Last revision date:180214
[St] Status:In-Process

  7 / 2791 MEDLINE  
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[PMID]: 29407817
[Au] Autor:Jamwal A; Lemire D; Driessnack M; Naderi M; Niyogi S
[Ad] Address:Department of Biology, University of Saskatchewan, 112 Science Place, Saskatoon, SK, Canada. Electronic address: ankur.jamwal@usask.ca.
[Ti] Title:Interactive effects of chronic dietary selenomethionine and cadmium exposure in rainbow trout (Oncorhynchus mykiss): A preliminary study.
[So] Source:Chemosphere;197:550-559, 2018 Apr.
[Is] ISSN:1879-1298
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The present study investigated the interactive effects of dietary cadmium (Cd) and selenium (Se) on the tissue-specific (liver, kidney, and muscle) accumulation of these two elements, hepatic oxidative stress response, and morphometrics in rainbow trout (Oncorhynchus mykiss) during chronic exposure. Fish were exposed to elevated dietary Cd (45 µg g dry wt.), and medium (10 µg g dry wt.) or high (45 µg g dry wt.) dietary selenium (added as selenomethionine), both alone and in combination, for 30 days. Exposure to dietary Cd alone caused oxidative stress in fish as reflected by reduced thiol redox (GSH:GSSG), increased lipid peroxidation, and induction of anti-oxidative enzymes (catalase, superoxide dismutase, and glutathione peroxidase) in the liver. Also, an increase in tissue-specific Cd burden and impaired morphometrics (hepato-somatic index and condition factor) were also recorded in fish following exposure to dietary Cd. In contrast, the dietary co-exposure to Cd and Se (at both medium and high doses) resulted in a decrease in Cd burden in the liver and kidney of fish. However, co-exposure to medium, but not high, dose of dietary Se completely alleviated Cd-induced oxidative stress and impaired morphometrics in fish, indicating that the reduced Cd tissue burden might not have been the primary factor behind the amelioration of Cd toxicity by Se. Overall, our study demonstrated that the protective effect of Se against the chronic Cd toxicity in fish is mainly mediated by the anti-oxidative properties of Se, but this protective effect is dose-specific and occurs only at a moderate exposure dose.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180213
[Lr] Last revision date:180213
[St] Status:In-Process

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[PMID]: 29277661
[Au] Autor:Kim H; Park J; Kim S; Shin DH
[Ad] Address:College of Pharmacy, Ewha W. University, 52, Ewhayeodae-gil, Seoul, 03760, Republic of Korea.
[Ti] Title:Crystal structure of d-glycero-α-d-manno-heptose-1-phosphate guanylyltransferase from Yersinia pseudotuberculosis.
[So] Source:Biochim Biophys Acta;1866(3):482-487, 2018 Mar.
[Is] ISSN:0006-3002
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:The Gram-negative bacterium Yersinia pseudotuberculosis is the causative agent of yersiniosis. d-glycero-α-d-manno-heptose-1-phosphate guanylyltransferase (HddC) is the fourth enzyme of the GDP-d-glycero-α-d-manno-heptose biosynthesis pathway which is important for the virulence of the microorganism. Therefore, HddC is a potential target of antibiotics against yersiniosis. In this study, HddC from the synthesized HddC gene of Y. pseudotuberculosis has been expressed, purified, crystallized. Synchrotron X-ray data from a selenomethionine-substituted HddC crystal were also collected and its structure was determined at 2.0Å resolution. Structure analyses revealed that it belongs to the glycosyltransferase A type superfamily members with the signature motif GXGXR for nucleotide binding. Despite of remarkable structural similarity, HddC uses GTP for catalysis instead of CTP and UTP which are used for other major family members, cytidylyltransferase and uridylyltransferase, respectively. We suggest that EXXPLGTGGA and L(S/A/G)X(S/G) motifs are probably essential to bind with GTP and a FSFE motif with substrate.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180207
[Lr] Last revision date:180207
[St] Status:In-Data-Review

  9 / 2791 MEDLINE  
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[PMID]: 28458184
[Au] Autor:Carroll L; Pattison DI; Fu S; Schiesser CH; Davies MJ; Hawkins CL
[Ad] Address:The Heart Research Institute, 7 Eliza St, Newtown, NSW 2042, Australia; Sydney Medical School, University of Sydney, Sydney, NSW 2006, Australia; Department of Biomedical Sciences, Panum Institute, University of Copenhagen, Blegdamsvej 3, Copenhagen N 2200, Denmark.
[Ti] Title:Catalytic oxidant scavenging by selenium-containing compounds: Reduction of selenoxides and N-chloramines by thiols and redox enzymes.
[So] Source:Redox Biol;12:872-882, 2017 Aug.
[Is] ISSN:2213-2317
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Myeloperoxidase produces strong oxidants during the immune response to destroy invading pathogens. However, these oxidants can also cause tissue damage, which contributes to the development of numerous inflammatory diseases. Selenium containing compounds, including selenomethionine (SeMet) and 1,4-anhydro-5-seleno-D-talitol (SeTal), react rapidly with different MPO-derived oxidants to form the respective selenoxides (SeMetO and SeTalO). This study investigates the susceptibility of these selenoxides to undergo reduction back to the parent compounds by intracellular reducing systems, including glutathione (GSH) and the glutathione reductase and thioredoxin reductase systems. GSH is shown to reduce SeMetO and SeTalO, with consequent formation of GSSG with apparent second order rate constants, k , in the range 10 -10 M s . Glutathione reductase reduces both SeMetO and SeTalO at the expense of NADPH via formation of GSSG, whereas thioredoxin reductase acts only on SeMetO. The presence of SeMet and SeTal also increased the rate at which NADPH was consumed by the glutathione reductase system in the presence of N-chloramines. In contrast, the presence of SeMet and SeTal reduced the rate of NADPH consumption by the thioredoxin reductase system after addition of N-chloramines, consistent with the rapid formation of selenoxides, but only slow reduction by thioredoxin reductase. These results support a potential role of seleno compounds to act as catalytic scavengers of MPO-derived oxidants, particularly in the presence of glutathione reductase and NADPH, assuming that sufficient plasma levels of the parent selenoether can be achieved in vivo following supplementation.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1705
[Cu] Class update date: 180124
[Lr] Last revision date:180124
[St] Status:In-Process

  10 / 2791 MEDLINE  
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[PMID]: 29193386
[Au] Autor:Milaczewska A; Kot E; Amaya JA; Makris TM; Zajac M; Korecki J; Chumakov A; Trzewik B; Kedracka-Krok S; Minor W; Chruszcz M; Borowski T
[Ad] Address:Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239, Krakow, Poland.
[Ti] Title:On the Structure and Reaction Mechanism of Human Acireductone Dioxygenase.
[So] Source:Chemistry;, 2017 Nov 28.
[Is] ISSN:1521-3765
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:Acireductone dioxygenase (ARD) is an intriguing enzyme from the methionine salvage pathway that is capable of catalysing two different oxidation reactions with the same substrate depending on the type of the metal ion in the active site. To date, the structural information regarding the ARD-acireductone complex is limited and possible reaction mechanisms are still under debate. The results of joint experimental and computational studies undertaken to advance knowledge about ARD are reported. The crystal structure of an ARD from Homo sapiens was determined with selenomethionine. EPR spectroscopy suggested that binding acireductone triggers one protein residue to dissociate from Fe , which allows NO (and presumably O ) to bind directly to the metal. Mössbauer spectroscopic data (interpreted with the aid of DFT calculations) was consistent with bidentate binding of acireductone to Fe and concomitant dissociation of His88 from the metal. Major features of Fe vibrational spectra obtained for the native enzyme and upon addition of acireductone were reproduced by QM/MM calculations for the proposed models. A computational (QM/MM) study of the reaction mechanisms suggests that Fe promotes O-O bond homolysis, which elicits cleavage of the C1-C2 bond of the substrate. Higher M /M redox potentials of other divalent metals do not support this pathway, and instead the reaction proceeds similarly to the key reaction step in the quercetin 2,3-dioxygenase mechanism.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180111
[Lr] Last revision date:180111
[St] Status:Publisher
[do] DOI:10.1002/chem.201704617


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