ArticleThe Journal of biological chemistry2006
Aminoglycosides decrease glutathione peroxidase-1 activity by interfering with selenocysteine incorporation.
Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- Enhancing Gpx1 palmitoylation to inhibit angiogenesis by targeting PPT1.Redox biology · 2024Article
- The role of glutathione peroxidase-1 in health and disease.Free radical biology & medicine · 2022Review
- Selenium Status and Supplementation Effects in Pregnancy-A Study on Mother-Child Pairs from a Single-Center Cohort.Nutrients · 2022Observational
- Geneticin reduces mRNA stability.PloS one · 2022Article
- Natural Autoimmunity to Selenoprotein P Impairs Selenium Transport in Hashimoto's Thyroiditis.International journal of molecular sciences · 2021Article
- Copper interferes with selenoprotein synthesis and activity.Redox biology · 2020Article
- Aminoglycoside-driven biosynthesis of selenium-deficient Selenoprotein P.Scientific reports · 2017Article
- Sex-specific and inter-individual differences in biomarkers of selenium status identified by a calibrated ELISA for selenoprotein P.Redox biology · 2017Article
- Natural allelic variations in glutathione peroxidase-1 affect its subcellular localization and function.Cancer research · 2014Article
- Secisbp2 is essential for embryonic development and enhances selenoprotein expression.Antioxidants & redox signaling · 2014Article
- High error rates in selenocysteine insertion in mammalian cells treated with the antibiotic doxycycline, chloramphenicol, or geneticin.The Journal of biological chemistry · 2013Article
- Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities.Antioxidants & redox signaling · 2011Review
- Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein.Free radical biology & medicine · 2011Article
- Targeted insertion of cysteine by decoding UGA codons with mammalian selenocysteine machinery.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Antioxidant enzyme deficiencies and vascular disease.Expert review of endocrinology & metabolism · 2010Article
- Aging decreases expression and activity of glutathione peroxidase-1 in human endothelial progenitor cells.Microvascular research · 2009Article
- Functional analysis of the interplay between translation termination, selenocysteine codon context, and selenocysteine insertion sequence-binding protein 2.The Journal of biological chemistry · 2007Article
- The L7Ae RNA binding motif is a multifunctional domain required for the ribosome-dependent Sec incorporation activity of Sec insertion sequence binding protein 2.Molecular and cellular biology · 2007Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Cellular glutathione peroxidase is a key intracellular antioxidant enzyme that contains a selenocysteine residue at its active site. Selenium, a selenocysteine incorporation sequence in the 3'-untranslated region of the glutathione peroxidase mRNA, and other translational cofactors are necessary for "read-through" of a UGA stop codon that specifies selenocysteine incorporation. Aminoglycoside antibiotics facilitate read-through of premature stop codons in prokayotes and eukaryotes. We studied the effects of G418, an aminoglycoside, on cellular glutathione peroxidase expression and function in mammalian cells. Insertion of a selenocysteine incorporation element along with a UGA codon into a reporter construct allows for read-through only in the presence of selenium. G418 increased read-through in selenium-replete cells as well as in the absence of selenium. G418 treatment increased immunodetectable endogenous or recombinant glutathione peroxidase but reduced the specific activity of the enzyme. Tandem mass spectrometry experiments indicated that G418 caused a substitution of l-arginine for selenocysteine. These data show that G418 can affect the biosynthesis of this key antioxidant enzyme by promoting substitution at the UGA codon.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.