ArticleFree radical biology & medicine2011
Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein.
Article in Free radical biology & medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Antioxidant Upregulation Contributes to Improvements in Diaphragm Function Following Cervical Spinal Cord Injury and Hyperbaric Oxygen Therapy.Antioxidants (Basel, Switzerland) · 2026Article
- Loss of LanC-like proteins delays post-injury regeneration of aging skeletal muscles.bioRxiv : the preprint server for biology · 2026Article
- Metabolic alterations in the absence of a neuromuscular phenotype in humanizedBrain communications · 2026Article
- Selenium in Peptide Chemistry.Molecules (Basel, Switzerland) · 2023Review
- Review
- Organic zinc with moderate chelation strength enhances zinc absorption in the small intestine and expression of related transporters in the duodenum of broilers.Frontiers in physiology · 2022Article
- LanCLs add glutathione to dehydroamino acids generated at phosphorylated sites in the proteome.Cell · 2021Article
- Selenium and Glutathione-Depleted Rats as a Sensitive Animal Model to Predict Drug-Induced Liver Injury in Humans.International journal of molecular sciences · 2019Article
- Review
- Glutathione peroxidase's reaction intermediate selenenic acid is stabilized by the protein microenvironment.Free radical biology & medicine · 2014Article
- Superoxide dismutase 1 loss disturbs intracellular redox signaling, resulting in global age-related pathological changes.BioMed research international · 2014Review
- Redox regulation of mitochondrial function.Antioxidants & redox signaling · 2012Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Se-dependent glutathione peroxidase-1 (GPX1) and Cu,Zn-superoxide dismutase (SOD1) are two major intracellular antioxidant enzymes. The purpose of this study was to elucidate the biochemical mechanisms for the 40% loss of hepatic GPX1 activity in SOD1(-/-) mice. Compared with the wild type (WT), the SOD1(-/-) mice showed no change in the total amount of GPX1 protein. However, their total enzyme protein exhibited 31 and 38% decreases (P<0.05) in the apparent k(cat) for hydrogen peroxide and tert-butylperoxide (at 2mM GSH), respectively. Most striking, mass spectrometry revealed two chemical forms of the 47th residue of GPX1: the projected native selenocysteine (Sec) and the Se-lacking dehydroalanine (DHA). The hepatic GPX1 protein of the SOD1(-/-) mice contained 38% less Sec and 77% more DHA than that of WT and showed aggravated dissociation of the tetramer structure. In conclusion, knockout of SOD1 elevated the conversion of Sec to DHA in the active site of hepatic GPX1, leading to proportional decreases in the apparent k(cat) and activity of the enzyme protein as a whole. Our data reveal a structural and kinetic mechanism for the in vivo functional dependence of GPX1 on SOD1 in mammals and provide a novel mass spectrometric method for the assay of oxidative modification of the GPX1 protein.
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