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Thematische Bibliographien / Selenoprote

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Zeitschriftenartikel

Auswahl der wissenschaftlichen Literatur zum Thema „Selenoprote“

Autor: Grafiati

Veröffentlicht am 18. Mai 2024

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Zeitschriftenartikel zum Thema "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 (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

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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

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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 (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

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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 (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 microgram

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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 (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 selenopr

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6

Whanger, P. D. "Selenoprotein expression and function—Selenoprotein W." Biochimica et Biophysica Acta (BBA) - General Subjects 1790, no. 11 (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 (2022): 1268. http://dx.doi.org/10.3390/biom12091268.

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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 selecti

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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 (2009): 329–38. http://dx.doi.org/10.1042/bsr20080146.

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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

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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 (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 do

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10

Urbano, Teresa, Marco Vinceti, Jessica Mandrioli, 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 (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 posi

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