ArticleChemico-biological interactions2011
Catalytic reduction of carbonyl groups in oxidized PAPC by Kvβ2 (AKR6).
Article in Chemico-biological interactions, 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, 16 citations in OpenAlex.
- Redox Regulation of KAntioxidants & redox signaling · 2024Review
- Non-conducting functions of potassium channels in cancer and neurological disease.Current topics in membranes · 2023Review
- Review
- Pyridine nucleotide redox potential in coronary smooth muscle couples myocardial blood flow to cardiac metabolism.Nature communications · 2022Article
- S-acylation-dependent membrane microdomain localization of the regulatory Kvβ2.1 subunit.Cellular and molecular life sciences : CMLS · 2022Article
- Article
- The Biosynthesis of Enzymatically Oxidized Lipids.Frontiers in endocrinology · 2020Review
- Modifying the Tumour Microenvironment: Challenges and Future Perspectives for Anticancer Plasma Treatments.Cancers · 2019Review
- Article
- Oxidative and reductive metabolism of lipid-peroxidation derived carbonyls.Chemico-biological interactions · 2015Article
- Tissue distribution, ontogeny, and chemical induction of aldo-keto reductases in mice.Drug metabolism and disposition: the biological fate of chemicals · 2013Article
- Regulation of ion channels by pyridine nucleotides.Circulation research · 2013Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The β-subunits of the voltage-gated potassium channel (Kvβ) belong to the aldo-keto reductase superfamily. The Kvβ-subunits dock with the pore-forming Kv α-subunits and impart or accelerate the rate of inactivation in Kv channels. Inactivation of Kv currents by Kvβ is differentially regulated by oxidized and reduced pyridine nucleotides. In mammals, AKR6 family is comprised of 3 different genes Kvβ1-3. We have shown previously that Kvβ2 catalyzes the reduction of a broad range of carbonyls including aromatic carbonyls, electrophilic aldehydes and prostaglandins. However, the endogenous substrates for Kvβ have not been identified. To determine whether products of lipid oxidation are substrates of Kvβs, we tested the enzymatic activity of Kvβ2 with oxidized phospholipids generated during the oxidation of 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine (PAPC). Electrospray ionization mass spectrometric analysis showed that Kvβ2 catalyzed the NADPH-dependent reduction of several products of oxPAPC, including 1-palmitoyl-2-(5-oxovaleroyl)-sn-glycero-3-phosphorylcholine (POVPC), 1-palmitoyl-2-(epoxycyclopentenone)-sn-glycero-3-phosphorylcholine (PECPC), 1-palmitoyl-2-(5,6)- epoxyisoprostane E2-sn-glycero-3-phosphocholine (PEIPC). These results were validated using high resolution mass spectrometric analysis. Time course analysis revealed that the reduced products reached significant levels for ions at m/z 594/596 (POVPC/PHVPC), 810/812 (PECPC/2H-PECPC) and 828/830 (PEIPC/2H-PEIPC) in the oxPAPC+Kvβ2 mixture (p<0.01). These results suggest that Kvβ could serve as a sensor of lipid oxidation via its catalytic activity and thereby alter Kv currents under conditions of oxidative stress.
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