Готові списки джерел за темами / Selenoprote

Добірка наукової літератури з теми "Selenoprote"

Автор: Grafiati
Опубліковано: 18 травня 2024

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Статті в журналах з теми "Selenoprote"

1

Mahmoud, Kholoud Gamal, Rasha Mohamed Gamal Elshafiey, Radwa Mahmoud Elsharaby, and Amany Mahmoud Elbarky. "Selenoprotein-p as Biomarker of Selenium Status in Obese Children and Adolescents." Asian Journal of Pediatric Research 13, no. 4 (December 21, 2023): 169–79. http://dx.doi.org/10.9734/ajpr/2023/v13i4306.

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Background: The child and adolescent obesity have become a major public health problem. Selenoprotien p1 (SEPP1) is widely acknowledged to be among the most delicate functional indicators of Se status and it plays a role in the metabolism of Se and in anti-oxidative defense. So, we aimed to assess Selenoprotein-p level in obese children and adolescents. Methods: This cross-sectional comparative work included 60 children: 30 obese children and the control group consisted of 30 children who were healthy and matched in terms of gender and age. A comprehensive taking of history and clinical assessment with anthropometric measurements were conducted on all children and adolescents. Basic investigations and serum selenoprotien-p1 level were performed. Results: Serum selenoprotien-p1 (SEPP1) levels were substantially decreased in obese children contrasted to controls. Conclusions: Selenoprotien p1 levels were substantially decreased in obese children and adolescent. Selenoprotien p1 could be a sensitive functional biomarker of selenium status.
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2

Zhang, Chi, and Qi Bin Huang. "A Preliminary Study on the Antioxidant Activity of Selenoprotein in Cordyceps militaris Rich in Selenium." Advanced Materials Research 396-398 (November 2011): 157–61. http://dx.doi.org/10.4028/www.scientific.net/amr.396-398.157.

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Utilize different solvents to extract and salt out soluble protein from the Cordyceps rich in selenium which is artificially cultivated, thus obtaining different types of selenoproteins contained in it, and then pyrogallol autoxidation method is applied to determine their antioxidant activity, meanwhile, double-channel atomic fluorescence is used to detect the materials and their selenium content. The results show that: various proteins of Cordyceps rich in selenium all contain selenium, followed by alkali-soluble selenoprotein > alcohol-soluble selenoprotein > salt-soluble selenoprotein > water-soluble selenoprotein; their ability to remove superoxide anion is followed by water-soluble protein> alkali-soluble protein > salt-soluble protein> alcohol-soluble protein, the clearance rate of selenoprotein with different salting points on superoxide anion is shown as follows: salting selenoprotein with the rate of 70% > salting selenoprotein with the rate of 100% > salting selenoprotein with the rate of 90% > salting selenoprotein with the rate of 80%> salting selenoprotein with the rate of 50%> salting selenoprotein with the rate of 60% ; therefore, selenoprotein of Cordyceps rich in selenium is a kind of natural resource with good antioxidant activity as well as broad application prospects.
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3

Lu, Zhuang, Pengzu Wang, Teng Teng, Baoming Shi, Anshan Shan, and Xin Gen Lei. "Effects of Dietary Selenium Deficiency or Excess on Selenoprotein Gene Expression in the Spleen Tissue of Pigs." Animals 9, no. 12 (December 11, 2019): 1122. http://dx.doi.org/10.3390/ani9121122.

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To evaluate the effects of dietary Se deficiency and excess on the mRNA levels of selenoproteins in pig spleen tissues, 20 healthy uncastrated boars (Duroc × Landrace × Yorkshire, 10 ± 0.72 kg) were randomly divided into four groups (5 pigs per group). The pigs were fed a Se deficient corn-soybean basal feed (Se content <0.03 mg/kg) or basal feed with added sodium selenite at 0.3, 1.0, or 3.0 mg Se/kg diet, respectively. The experiment lasted 16 weeks. The spleen tissue was collected to examine the mRNA expression levels of 24 selenoprotein genes at the end of the study. Compared with pigs in other groups, those fed with the 1.0 mg Se/kg diet had higher mRNA levels of glutathione peroxidase 1 (Gpx1), glutathione peroxidase 2 (Gpx2), deiodinase type II (Dio2), thioredoxin reductase 3 (Txnrd3), selenoprotein H (Selh), selenoprotein N, 1 (Sepn1), selenoprotein P1 (Sepp1), and selenoprotein V (Selv) in the spleen (p < 0.05). Dietary Se deficiency resulted in lower mRNA levels of Gpx1, Gpx2, glutathione peroxidase 3 (Gpx3), Dio2, thioredoxin reductase 2 (Txnrd2), Txnrd3, Selh, selenoprotein I (Seli), selenoprotein K (Selk), selenoprotein M (Selm), Sepn1, Sepp1, and Selv in the spleen than the other three groups. Dietary Se levels did not affect the mRNA levels of glutathione peroxidase 4 (Gpx4), deiodinase type I (Dio1), deiodinase type III (Dio3), selenophosphate synthetase 2 (Sephs2), thioredoxin reductase 1 (Txnrd1), selenoprotein O (Selo), selenoprotein S (Sels), selenoprotein W (Selw), selenoprotein X (Selx), and selenoprotein 15 (Sel15) in the spleen (p > 0.05). Dietary Se levels can affect the transcription levels of 14 selenoprotein genes in the spleen of pigs.
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4

Burk, R. F., K. E. Hill, R. Read, and T. Bellew. "Response of rat selenoprotein P to selenium administration and fate of its selenium." American Journal of Physiology-Endocrinology and Metabolism 261, no. 1 (July 1, 1991): E26—E30. http://dx.doi.org/10.1152/ajpendo.1991.261.1.e26.

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Selenoprotein P is a glycoprotein that contains greater than 60% of the selenium in rat plasma. Physiological experiments were undertaken to gain insight into selenoprotein P function. Selenium-deficient rats were injected with doses of selenium ranging from 25 to 200 micrograms/kg, and the appearance of selenoprotein P was compared with the appearance of glutathione peroxidase activity in plasma and in liver. Selenoprotein P concentration increased to 35% of control by 6 h, whereas glutathione peroxidase activity increased minimally or not at all. Moreover, in rats given 100 and 200 micrograms selenium/kg, selenoprotein P reached 75% of its concentration in control rats at 24 h, whereas glutathione peroxidase activity reached only 6% of control. Cycloheximide pretreatment blocked the appearance of selenoprotein P in response to selenium injection. Male and female rats had similar concentrations of selenoprotein P. Partially purified selenoprotein P and plasma glutathione peroxidase labeled with 75Se were administered intravenously to selenium-deficient and control rats. 75Se given as selenoprotein P disappeared more rapidly from plasma than did 75Se given as glutathione peroxidase. Selenium deficiency did not significantly affect 75Se disappearance from plasma. At 2 h, brain, but not other tissues, took up more 75Se in selenium-deficient rats than in control rats when 75Se was given as selenoprotein P. This suggests that brain has a specific uptake mechanism for selenium given in the form of selenoprotein P. These results demonstrate that several physiological properties distinguish selenoprotein P from glutathione peroxidase. However, they do not clearly indicate its function.
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5

Squires, Jeffrey E., Ilko Stoytchev, Erin P. Forry, and Marla J. Berry. "SBP2 Binding Affinity Is a Major Determinant in Differential Selenoprotein mRNA Translation and Sensitivity to Nonsense-Mediated Decay." Molecular and Cellular Biology 27, no. 22 (September 10, 2007): 7848–55. http://dx.doi.org/10.1128/mcb.00793-07.

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ABSTRACT Selenoprotein mRNAs are potential targets for degradation via nonsense-mediated decay due to the presence of in-frame UGA codons that can be decoded as either selenocysteine or termination codons. When UGA decoding is inefficient, as occurs when selenium is limiting, termination occurs at these positions. Based on the predicted exon-intron structure, 14 of the 25 human selenoprotein mRNAs are predicted to be sensitive to nonsense-mediated decay. Among these, sensitivity varies widely, resulting in a hierarchy of preservation or degradation of selenoprotein mRNAs and, thus, of selenoprotein synthesis. Potential factors in dictating the hierarchy of selenoprotein synthesis are the Sec insertion sequence RNA-binding proteins, SBP2 and nucleolin. To investigate the mechanistic basis for this hierarchy and the role of these two proteins, we carried out knockdowns of SBP2 expression and assessed the effects on selenoprotein mRNA levels. We also investigated in vivo binding of selenoprotein mRNAs by SBP2 and nucleolin via immunoprecipitation of the proteins and quantitation of bound mRNAs. We report that SBP2 exhibits strong preferential binding to some selenoprotein mRNAs over others, whereas nucleolin exhibits minimal differences in binding. Thus, SBP2 is a major determinant in dictating the hierarchy of selenoprotein synthesis via differential selenoprotein mRNA translation and sensitivity to nonsense-mediated decay.
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6

Whanger, P. D. "Selenoprotein expression and function—Selenoprotein W." Biochimica et Biophysica Acta (BBA) - General Subjects 1790, no. 11 (November 2009): 1448–52. http://dx.doi.org/10.1016/j.bbagen.2009.05.010.

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7

Hayek, Hassan, Gilbert Eriani, and Christine Allmang. "eIF3 Interacts with Selenoprotein mRNAs." Biomolecules 12, no. 9 (September 9, 2022): 1268. http://dx.doi.org/10.3390/biom12091268.

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Анотація:
The synthesis of selenoproteins requires the co-translational recoding of an in-frame UGASec codon. Interactions between the Selenocysteine Insertion Sequence (SECIS) and the SECIS binding protein 2 (SBP2) in the 3′untranslated region (3′UTR) of selenoprotein mRNAs enable the recruitment of the selenocysteine insertion machinery. Several selenoprotein mRNAs undergo unusual cap hypermethylation and are not recognized by the translation initiation factor 4E (eIF4E) but nevertheless translated. The human eukaryotic translation initiation factor 3 (eIF3), composed of 13 subunits (a-m), can selectively recruit several cellular mRNAs and plays roles in specialized translation initiation. Here, we analyzed the ability of eIF3 to interact with selenoprotein mRNAs. By combining ribonucleoprotein immunoprecipitation (RNP IP) in vivo and in vitro with cross-linking experiments, we found interactions between eIF3 and a subgroup of selenoprotein mRNAs. We showed that eIF3 preferentially interacts with hypermethylated capped selenoprotein mRNAs rather than m7G-capped mRNAs. We identified direct contacts between GPx1 mRNA and eIF3 c, d, and e subunits and showed the existence of common interaction patterns for all hypermethylated capped selenoprotein mRNAs. Differential interactions of eIF3 with selenoprotein mRNAs may trigger specific translation pathways independent of eIF4E. eIF3 could represent a new player in the translation regulation and hierarchy of selenoprotein expression.
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8

Sunde, Roger A., Anna M. Raines, Kimberly M. Barnes, and Jacqueline K. Evenson. "Selenium status highly regulates selenoprotein mRNA levels for only a subset of the selenoproteins in the selenoproteome." Bioscience Reports 29, no. 5 (June 25, 2009): 329–38. http://dx.doi.org/10.1042/bsr20080146.

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Анотація:
Gpx (glutathione peroxidase)-1 enzyme activity and mRNA levels decrease dramatically in Se (selenium) deficiency, whereas other selenoproteins are less affected by Se deficiency. This hierarchy of Se regulation is not understood, but the position of the UGA selenocysteine codon is thought to play a major role in making selenoprotein mRNAs susceptible to nonsense-mediated decay. Thus in the present paper we studied the complete selenoproteome in the mouse to uncover additional selenoprotein mRNAs that are highly regulated by Se status. Mice were fed on Se-deficient, Se-marginal and Se-adequate diets (0, 0.05 and 0.2 μg of Se/g respectively) for 35 days, and selenoprotein mRNA levels in liver and kidney were determined using microarray analysis and quantitative real-time PCR analysis. Se-deficient mice had liver Se concentrations and liver Gpx1 and thioredoxin reductase activities that were 4, 3 and 3% respectively of the levels in Se-adequate mice, indicating that the mice were Se deficient. mRNAs for Selh (selenoprotein H) and Sepw1 (selenoprotein W) as well as Gpx1 were decreased by Se deficiency to <40% of Se-adequate levels. Five and two additional mRNAs were moderately down-regulated in Sedeficient liver and kidney respectively. Importantly, nine selenoprotein mRNAs in liver and fifteen selenoprotein mRNAs in the kidney were not significantly regulated by Se deficiency, clearly demonstrating that Se regulation of selenoprotein mRNAs is not a general phenomenon. The similarity of the response to Se deficiency suggests that there is one underlying mechanism responsible. Importantly, the position of the UGA codon did not predict susceptibility to Se regulation, clearly indicating that additional features are involved in causing selenoprotein mRNAs to be sensitive to Se status.
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9

Fatoki, Toluwase Hezekiah, Omodele Ibraheem, Amos Olalekan Abolaji, and David Morakinyo Sanni. "In Silico study of anticarcinogenic potential of the selenoprotein BthD from Drosophila melanogaster. Identifying the anticancer peptide CRSUR from the conserved region." Nova Biotechnologica et chimica 19, no. 1 (June 30, 2020): 37–51. http://dx.doi.org/10.36547/nbc.v19i1.576.

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Drosophila melanogaster is used as a model system in biomedical studies. Selenoprotein is the major biological form of selenium in eukaryotes. Selenoproteins are generally involved in catabolic pathways in bacteria and archaea, whereas it participates in anabolic and antioxidant processes in eukaryotic. In this study, anticancer potential of selenoprotein BthD of D. melanogaster was investigated using bioinformatics methods. Results showed that selenoprotein BthD of D. melanogaster may have dual properties as evident by its orthology with selenoprotein H (SelH) of Homo sapiens and conserved domain of fructokinase-like protein 2 of Vitis vinifera. These dual properties were also revealed in the phylogenetic analysis, while further structural modeling showed that selenoprotein BthD possibly exists as homotetramer in the native functional structure. The anticancer property of selenoprotein BthD was proposed to be by synergy of antioxidant or redox activities of thioredoxin and glutathione reductase (TGR) domain and the signaling function of fructokinase-like protein 2 domain both in Golgi apparatus and cytoplasm, through energy deprivation. The anticancer peptide CRSUR was identified from conserved region of selenoprotein BthD, of which its cyclic form showed potential anticancer properties predictively through E3 ubiquitin-protein ligase regulating NF-kappa-B signaling by unleashing cells for spontaneous formation of the ripoptosome.
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10

Urbano, Teresa, Marco Vinceti, Jessica Mandrioli, Annalisa Chiari, Tommaso Filippini, Roberta Bedin, Manuela Tondelli, et al. "Selenoprotein P Concentrations in the Cerebrospinal Fluid and Serum of Individuals Affected by Amyotrophic Lateral Sclerosis, Mild Cognitive Impairment and Alzheimer’s Dementia." International Journal of Molecular Sciences 23, no. 17 (August 30, 2022): 9865. http://dx.doi.org/10.3390/ijms23179865.

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Selenoprotein P, a selenium-transporter protein, has been hypothesized to play a role in the etiology of neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and Alzheimer’s dementia (AD). However, data in humans are scarce and largely confined to autoptic samples. In this case–control study, we determined selenoprotein P concentrations in both the cerebrospinal fluid (CSF) and the serum of 50 individuals diagnosed with ALS, 30 with AD, 54 with mild cognitive impairment (MCI) and of 30 controls, using sandwich enzyme-linked immunosorbent assay (ELISA) methods. We found a positive and generally linear association between CSF and serum selenoprotein P concentrations in all groups. CSF selenoprotein P and biomarkers of neurodegeneration were positively associated in AD, while for MCI, we found an inverted-U-shaped relation. CSF selenoprotein P concentrations were higher in AD and MCI than in ALS and controls, while in serum, the highest concentrations were found in MCI and ALS. Logistic and cubic spline regression analyses showed an inverse association between CSF selenoprotein P levels and ALS risk, and a positive association for AD risk, while an inverted-U-shaped relation with MCI risk emerged. Conversely, serum selenoprotein P concentrations were positively associated with risk of all conditions but only in their lower range. Overall, these findings indicate some abnormalities of selenoprotein P concentrations in both the central nervous system and blood associated with ALS and neurocognitive disorders, though in different directions. These alterations may reflect either phenomena of etiologic relevance or disease-induced alterations of nutritional and metabolic status.
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Більше джерел

Дисертації з теми "Selenoprote"

1

Ferreira, Diana Quit?ria Cabral. "Avalia??o do estado nutricional relativo ao sel?nio e da express?o g?nica de selenoprote?nas em pacientes com aterosclerose tratados com estatinas." Universidade Federal do Rio Grande do Norte, 2010. http://repositorio.ufrn.br:8080/jspui/handle/123456789/13489.

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Made available in DSpace on 2014-12-17T14:16:33Z (GMT). No. of bitstreams: 1 DianaQCF_DISSERT.pdf: 1652131 bytes, checksum: 3725280f12290a694c1544f741074448 (MD5) Previous issue date: 2010-05-24
Conselho Nacional de Desenvolvimento Cient?fico e Tecnol?gico
The aim of this study was to determine the effects of the use of rosuvastatin in patients with atherosclerosis, in relation to blood parameters of selenium and selenoproteins, and also observe possible changes in gene expression of selenoproteins in these patients. The sample consisted of 27 adult and elderly patients with a clinical diagnosis of coronary artery disease undergoing angioplasty, treated at Natal Hospital Center hospital, Natal, RN. Patients were treated with rosuvastatin 10 mg/day during four months. Anthropometric variables such as body mass index (BMI) and Waist circumference (WC) were measured before and after treatment, as well as lipid profile, blood glucose and liver enzymes (AST and ALT). The diet of the patients was also analyzed using 24-hour diet recall. We analyzed the concentrations of selenium in plasma and erythrocytes, and also the activity of Glutathione Peroxidase and gene expression by Real Time PCR of selenoproteins GPx1, SelP1 and SelN1. Patients had mean age of 61.0 ? 9.4 years, 59.3% were men and 40.7% were women. After four months of treatment there was significant reduction of CA and, according to BMI, most were overweight. The intake of macronutrients, cholesterol, polyunsaturated fatty acids, monounsaturated and saturated was adequate, but the energy and fiber intake was below the recommendations. Regarding the selenium intake was observed a high prevalence of inadequacy. As expected, after treatment with rosuvastatin, a significant reduction in total cholesterol, LDL and glucose, which was not observed for HDL. Selenium concentrations in plasma and erythrocytes showed no changes, keeping within the established cutoffs. We observed a significant increase in GPx enzyme activity and mRNA expression of GPX1 and SEPN1, but not for gene SEPP1. Thus, it was found that treatment with rosuvastatin did not reduce the expression of selenoproteins. More studies are needed to clarify the effects of rosuvastatin on gene expression of selenoproteins in patients with atherosclerosis
Este trabalho tem como objetivo verificar os efeitos do uso da rosuvastatina em pacientes com aterosclerose, em rela??o aos par?metros sangu?neos de sel?nio e selenoprote?nas, bem como observar poss?veis altera??es na express?o g?nica de selenoprote?nas nesses pacientes. A amostra foi constitu?da de 27 pacientes adultos e idosos com o diagn?stico cl?nico de doen?a arterial coronariana submetidos ? angioplastia, atendidos no Natal Hospital Center, Natal, RN. Os pacientes foram tratados com 10mg/dia de rosuvastatina durante 4 meses. Vari?veis antropom?tricas, como ?ndice de Massa Corporal (IMC) e Circunfer?ncia Abdominal (CA), foram medidas antes e ap?s o tratamento, bem como o perfil lip?dico, glicemia e enzimas hep?ticas (AST e ALT). A dieta dos pacientes tamb?m foi analisada utilizando o Recordat?rio alimentar de 24 horas. Foram analisadas as concentra??es do sel?nio no plasma e nos eritr?citos, e tamb?m a atividade da enzima Glutationa Peroxidase e a express?o g?nica por PCR em Tempo Real das selenoprote?nas GPx1, SelP1 e SelN1. Os pacientes apresentaram idade m?dia de 61,0?9,4 anos, sendo 59,3% homens e 40,7% mulheres. Ap?s os quatro meses de tratamento observou-se redu??o significativa da CA e, de acordo com o IMC, a maior parte estava com sobrepeso. A ingest?o dos macronutrientes, colesterol, ?cidos graxos polinsaturados, monoinsaturados e saturados foi adequada, por?m a de energia e fibras estava abaixo das recomenda??es. Com rela??o a ingest?o de sel?nio foi observada uma alta preval?ncia de inadequa??o. Como esperado, ap?s o tratamento com a rosuvastatina, houve redu??o significativa do colesterol total e LDL, bem como da glicemia, o que n?o foi observado para o HDL. As concentra??es de sel?nio no plasma e eritr?citos n?o apresentaram altera??es, se mantendo dentro dos pontos de corte estabelecidos. Foi observado um aumento significante na atividade enzim?tica da GPx e na express?o de mRNA do GPX1 e SEPN1, mas n?o para o gene SEPP1. Dessa forma, foi verificado que o tratamento com a rosuvastatina n?o diminuiu a express?o das selenoprote?nas. Mais estudos s?o necess?rios para esclarecer os efeitos da rosuvastatina sobre a express?o g?nica de selenoprote?nas em pacientes com aterosclerose
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2

Rida, Ahmad. "Biochemical and structural characterization of Selenoprotein N and study of his dysfunction in pancreatic tissue." Electronic Thesis or Diss., Strasbourg, 2023. http://www.theses.fr/2023STRAJ128.

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Анотація:
Chez l'homme, des mutations dans le gène SELENON, codant pour la sélénoprotéine N (SelenoN), provoquent un groupe de maladies musculaires héréditaires appelés myopathies liées à SELENON. Les mécanismes pathologiques à l'origine de ces myopathies sont mal compris, car la fonction catalytique de SelenoN reste incomprise. L'utilisation de modèles animaux a révélé l'importance de SelenoN dans le développement, la maintenance et la régénération des muscles. En outre, il a été démontré que SelenoN joue un rôle important dans le contrôle du stress oxydatif dans le réticulum endoplasmique et le maintien de l'homéostasie du calcium dans la cellule, ainsi qu'un lien a été établi avec la fonction mitochondriale. Malgré ces progrès passionnants concernant l'implication physiologique du SelenoN dans le tissu musculaire, l'activité catalytique de cette enzyme est encore inconnue et aucun traitement n'est disponible. Ce projet vise à développer des études in vitro et in vivo pour caractériser l'activité enzymatique de SelenoN et son contexte moléculaire et cellulaire. Tout d'abord, nous avons pu exprimer et purifier une forme recombinante pure et soluble de SelenoN. Les analyses ont montré que SelenoN lie une petite molécule, qui est en cours de caractérisation. La résolution de la structure 3D de SelenoN a permis de mieux comprendre l’organisation du site catalytique de la protéine. En parallèle, l'environnement cellulaire et les partenaires de SelenoN ont été étudiés en utilisant le marquage proximal (BioID) in cellulo, montrant une localisation spécifique dans le réticulum endoplasmique, liée au repliement des protéines et à la réponse au stress du RE. Enfin, l'utilisation in vivo du modèle SelenoN-/-mice a permis de mettre en évidence un phénotype métabolique dépendant du sexe. Ces études intégratives ont fourni des informations clés sur les bases moléculaires et physiopathologiques des myopathies liées à SelenoN et ouvriront la possibilité au développement des voies de thérapies
In humans, mutations in the SELENON gene, encoding selenoprotein N (SelenoN), cause a group of inherited muscular disorders termed SELENON-related myopathies. The pathogenic mechanisms behind these muscular diseases are poorly understood since the catalytic function of SelenoN remains elusive. The use of animal models revealed the importance of SelenoN in muscle development, maintenance, and regeneration. Moreover, SelenoN has been shown to play a role in oxidative stress control in the endoplasmic reticulum and maintenance of calcium homeostasis in the cell, as well as a link with mitochondrial function. Despite these exciting progresses regarding the physiological involvement of SelenoN in muscle tissue, the catalytic activity of this enzyme is still unknown, and no treatment is available. This project aims to develop in vitro and in vivo studies to characterize SelenoN enzymatic activity and the molecular and cellular context of this activity. Firstly, we were able to express and purify pure and soluble recombinant form of SelenoN. Analysis showed that SelenoN binds a small molecule, currently under characterization. The resolution of SelenoN 3D structure provided new insight and understanding of the catalytic site of the protein. In parallel, SelenoN cellular environment and partners were investigated using proximal labeling (BioID) in cellulo, showing a specific localization within the endoplasmic reticulum, related to protein folding and ER stress response. Finally, in vivo using SelenoN-/-mice model demonstrated a gender specific metabolic phenotype. These integrative studies provided key information about the molecular and physio-pathological basis of SELENON-related myopathies and will pave the way for therapy development
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3

Rother, Michael. "Selenoprotein-Biosynthese in Archaea." Diss., lmu, 2002. http://nbn-resolving.de/urn:nbn:de:bvb:19-680.

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4

Tobe, Ryuta. "Enzymological studies on selenoprotein biosynthesis." Kyoto University, 2009. http://hdl.handle.net/2433/126536.

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Анотація:
Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第14875号
農博第1787号
新制||農||975(附属図書館)
学位論文||H21||N4490(農学部図書室)
27297
UT51-2009-K671
京都大学大学院農学研究科応用生命科学専攻
(主査)准教授 栗原 達夫, 教授 渡邊 隆司, 教授 阪井 康能
学位規則第4条第1項該当
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5

Eussner, Ursula. "Selenoprotein P in der kolorektalen Karzinogenese." [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=967777690.

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6

Crosley, L. K. "Molecular mechanisms of selenoprotein gene expression." Thesis, University of Newcastle Upon Tyne, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.399315.

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7

Cockman, Eric Michael. "Post-Transcriptional Regulation of Selenoprotein S." Case Western Reserve University School of Graduate Studies / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=case1562593531805034.

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8

Villette, Stephane. "Molecular study of selenoprotein in gene expression." Thesis, University of Newcastle Upon Tyne, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.391327.

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9

Miller, Susan Mary. "Selenoprotein function and expression in human endothelium." Thesis, University of Edinburgh, 2000. http://hdl.handle.net/1842/23124.

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In this thesis the selenoproteins expressed by endothelial cells (isolated from various vascular beds and different species) and the modification of their expression through changes in Se supply and activation of second messenger pathways were studied. The ability of sodium selenite and selenomethionine supplementation to prevent oxidative damage in cultured endothelial cells was also examined, as well as the effect of sodium selenite in stabilising nitric oxide. The present study has confirmed the expression of cytoplasmic glutathione peroxidase (cyGPX) and phospholipid hydroperoxide glutathione peroxidase (PHGPX) in human umbilical vein endothelial cells (HUVEC), however thioredoxin reductase (TR) was found to be the predominant selenoprotein expressed accounting for approximately 43% of the total intracellular 75Se-labelled proteins. No extracellular selenoproteins were synthesised by HUVEC. The overall pattern of selenoprotein expression in endothelial cells isolated from different species and from various human tissue showed considerable variation, though differences were less pronounced when comparing the endothelial cells isolated from various human vascular beds and the human endothelial cell line EAhy926. The expression of TR, cyGPX and PHGPX and other unidentified selenoproteins in HUVEC was significantly modified in response to the phorbol ester phorbol-12-myristate 13-acetate (PMA). A 48 hr incubation with PMA led to significantly decreased expression of both TR and PHGPX (approximately half of that found in untreated cells). Whilst the expression of cyGPX was increased approximately two-fold by PMA treatment, a brief exposure to PMA (one minute) produced similar effects on the expression of these selenoproteins, after a 48 hr lag-period. These effects of PMA could be attenuated by the protein kinase C inhibitor, GF109203X. The calcium ionophore A23187 also modified selenoprotein expression, however time cells began to detach. These observations suggest that the A23187 effect may result from toxicity rather than activation of the calcium signalling pathway.
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Pagmantidis, Vasileios. "Selenoprotein gene expression and susceptibility to colon cancer." Thesis, University of Newcastle Upon Tyne, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.413956.

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Книги з теми "Selenoprote"

1

Selenoprotein Structure and Function. Elsevier, 2022. http://dx.doi.org/10.1016/s0076-6879(22)x0002-5.

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2

Weerapana, Eranthie. Selenoprotein Structure and Function. Elsevier Science & Technology, 2022.

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Weerapana, Eranthie. Selenoprotein Structure and Function. Elsevier Science & Technology Books, 2022.

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4

Yeh, Jan-ying. The influence of selenium on selenoprotein W. 1995.

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Sun, Yu. Selenoprotein W: Distribution and function in rat tissue and cultured cells. 1998.

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Krehl, Susanne. ˜Dasœ Selenoprotein Glutathionperoxidase-2: Physiologische Funktion und Einfluss auf die entzündungsassoziierte Colonkarzinogenese. 2011.

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Частини книг з теми "Selenoprote"

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Hill, Kristina E., and Raymond F. Burk. "Selenoprotein P." In Selenium, 123–35. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1609-5_11.

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Reeves, Mariclair A., and Marla J. Berry. "Selenoprotein M." In Selenium, 197–203. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4614-1025-6_15.

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Saito, Yoshiro, and Kazuhiko Takahashi. "Selenoprotein P." In Advanced Topics in Science and Technology in China, 77–88. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_5.

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Tanguy, Yannick, Sébastien Arthaud, Anthony Falluel-Morel, Destiny-Love Manecka, Abdeslam Chagraoui, Isabelle Lihrmann, and Youssef Anouar. "Selenoprotein T." In Advanced Topics in Science and Technology in China, 89–95. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_6.

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Kim, Ick Young, and Daewon Jeong. "Selenoprotein W." In Advanced Topics in Science and Technology in China, 97–105. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_7.

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Allmang, Christine, and Alain Krol. "Selenoprotein Biosynthesis." In Advanced Topics in Science and Technology in China, 107–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_8.

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Schweizer, Ulrich. "Selenoprotein P." In Encyclopedia of Metalloproteins, 1942–48. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_474.

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Moustafa, Mohamed E. "Selenoprotein K." In Encyclopedia of Metalloproteins, 1938–42. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_499.

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Tsuji, Petra A., and Bradley A. Carlson. "Selenoprotein Sep15." In Encyclopedia of Metalloproteins, 1948–52. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_500.

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Sunde, Roger A. "Regulation of selenoprotein expression." In Selenium, 81–96. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1609-5_8.

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Тези доповідей конференцій з теми "Selenoprote"

1

Galinn, Sarah E., Lindsay C. Rosenthal, Steven M. Barsotti, and Petra A. Tsuji. "Abstract 4881: Influence of polyphenols on selenoprotein expression in human colon cancer cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4881.

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Penney, Kathryn L., Haojie Li, Lorelei A. Mucci, J. Steven Morris, Howard D. Sesso, Meir J. Stampfer, and Jing Ma. "Abstract A122: Genetic variation in selenoprotein P, selenium levels, and prostate cancer risk and survival." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Dec 6–9, 2009; Houston, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-09-a122.

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Lin, Shih-Wen, Neal D. Freedman, Philip R. Taylor, You-Lin Qiao, Christian C. Abnet, Paula Hyland, Nan Hu, et al. "Abstract A59: Selenoprotein gene variants and risk of esophageal and gastric cancer in a Chinese population." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Oct 22-25, 2011; Boston, MA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1940-6207.prev-11-a59.

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4

Gopalakrishna, Rayudu, Jason E. Schiffman, Joshua Man, Lok Lei, Adela Wu, and Usha Gundimeda. "Abstract 1889: Curcumin potentiates the cancer-preventive actions of selenium by inactivating selenoprotein thioredoxin reductase in prostate cancer cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1889.

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Gopalakrishna, Rayudu, Jason Eric Schiffman, Kelley Mowatt, and Usha Gundimeda. "Abstract 3687: Curcumin both inactivates and induces selenoprotein thioredoxin reductase: dual regulation influences curcumin-induced apoptosis in prostate cancer cells." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3687.

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Ahmed, Elaf Husham, and Aseel Mokdad Hatam Abdul Wahed. "Evaluation of Fetuin A, Hepassocin, Selenoprotien P levels and number of biochemical variables in diabetes mellitus type 2 males’ patients." In FIFTH INTERNATIONAL CONFERENCE ON APPLIED SCIENCES: ICAS2023. AIP Publishing, 2024. http://dx.doi.org/10.1063/5.0211542.

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Li, Sharon, Paula L. Hyland, Neal D. Freedman, Nan Hu, Hua Su, Lemin Wang, Chaoyu Wang, et al. "Abstract 2206: Genetic variants in selenoprotein genes and risk of esophageal squamous cell carcinoma and gastric cancer in a Chinese population." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2206.

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Gopalakrishna, Rayudu, Barsegh A. Barseghian, Carleen Sarksian, Jason E. Schiffman, David V. Rayudu та Usha Gundimeda. "Abstract 3677: Prostate cancer progression decreases the cancer prevention by selenium: relation to overexpression of protein kinase Cε and selenoprotein thioredoxin reductase." У Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3677.

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Gopalakrishna, Rayudu, Venkata S. Arepalli, Albert Elhiani, Jason E. Schiffman, and Usha Gundimeda. "Abstract 1609: Oxidation products of green tea polyphenols induce inactivation of PKC isoenzymes and induce cell death via modulation of selenoprotein thioredoxin reductase and quinone reductase." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1609.

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