ArticleBritish journal of pharmacology2002
Glibenclamide binding to sulphonylurea receptor subtypes: dependence on adenine nucleotides.
Article in British journal of pharmacology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 88 citations in OpenAlex.
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- Identification and functional characterisation of N-linked glycosylation of the orphan G protein-coupled receptor Gpr176.Scientific reports · 2020Article
- ATP binding without hydrolysis switches sulfonylurea receptor 1 (SUR1) to outward-facing conformations that activate KThe Journal of biological chemistry · 2019Article
- Interrogating Synaptic Architecture: Approaches for Labeling Organelles and Cytoskeleton Components.Frontiers in synaptic neuroscience · 2019Review
- Cantu syndrome-associated SUR2 (ABCC9) mutations in distinct structural domains result in KThe Journal of biological chemistry · 2018Article
- Fluorescent flavonoids for endoplasmic reticulum cell imaging.Journal of materials chemistry. B · 2016Article
- Two-Photon Enzymatic Probes Visualizing Sub-cellular/Deep-brain Caspase Activities in Neurodegenerative Models.Scientific reports · 2016Article
- KATP Channels in the Cardiovascular System.Physiological reviews · 2016Review
- Molecular action of sulphonylureas on KATP channels: a real partnership between drugs and nucleotides.Biochemical Society transactions · 2015Review
- Structurally distinct ligands rescue biogenesis defects of the KATP channel complex via a converging mechanism.The Journal of biological chemistry · 2015Article
- Neonatal Diabetes and Congenital Hyperinsulinism Caused by Mutations in ABCC8/SUR1 are Associated with Altered and Opposite Affinities for ATP and ADP.Frontiers in endocrinology · 2015Article
- Cellular compartmentalization of secondary metabolism.Frontiers in microbiology · 2015Review
- Sulfonylureas suppress the stimulatory action of Mg-nucleotides on Kir6.2/SUR1 but not Kir6.2/SUR2A KATP channels: a mechanistic study.The Journal of general physiology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1: ATP-sensitive K(+) channels are composed of pore-forming subunits Kir6.2 and of sulphonylurea receptors (SURs); the latter are the target of the hypoglycaemic sulphonylureas like glibenclamide. Here, we report on the negative allosteric modulation by MgATP and MgADP of glibenclamide binding to SUR1 and to SUR2 mutants with high glibenclamide affinity, SUR2A(Y1206S) and SUR2B(Y1206S). 2: ATP, in the presence of an ATP-regenerating system to oppose hydrolysis during incubation, inhibited glibenclamide binding to SUR1 and SUR2B(Y1206S) by approximately 60%, to SUR2A(Y1206S) by 21%). Inhibition curves for the SUR2(Y1206S) isoforms were monophasic with IC(50) values of 5-10 microM; the curve for SUR1 was biphasic (IC(50) values 4.7 and 1300 microM). 3: Glibenclamide inhibition curves for ADP, performed in the presence of an ATP-consuming system to oppose ATP formation from ADP, were generally shifted rightwards and showed positive cooperativity, in particular with the SUR2(Y1206S) isoforms. 4: In the absence of the coupled enzyme systems, inhibition curves of MgATP or MgADP were generally shifted leftwards. This indicated synergy of MgATP and MgATP in acting together. 5: Coexpression of SUR1 and SUR2B(Y1206S) with Kir6.2 reduced both potency and efficacy of ATP in inhibiting glibenclamide binding; this was particularly marked for Kir6.2/SUR1. 6: The data show (a) that the inhibitory effects of ATP and ADP on glibenclamide binding differ from one another, (b) that they depend on the SUR subtype, and (c) that they are weakened by coexpression with Kir6.2.
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