ArticleThe Journal of physiology1997
Properties of cloned ATP-sensitive K+ currents expressed in Xenopus oocytes.
Article in The Journal of physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed, 195 citations in OpenAlex.
- Characterization of four structurally diverse inhibitors of SUR2-containing KChannels (Austin, Tex.) · 2024Article
- A loss-of-function mutation in KCNJ11 causing sulfonylurea-sensitive diabetes in early adult life.Diabetologia · 2024Article
- Discovery and Characterization of VU0542270, the First Selective Inhibitor of Vascular Kir6.1/SUR2B KMolecular pharmacology · 2024Article
- Review
- Proteasome granule formation is regulated through mitochondrial respiration and kinase signaling.Journal of cell science · 2022Article
- Inward and outward currents of native and cloned K(ATP) channels (Kir6.2/SUR1) share single-channel kinetic properties.Biochemistry and biophysics reports · 2022Article
- Remnants of the Balbiani body are required for formation of RNA transport granules iniScience · 2022Article
- Lactate is an energy substrate for rodent cortical neurons and enhances their firing activity.eLife · 2021Article
- Study of Uptake Mechanisms of Halloysite Nanotubes in Different Cell Lines.International journal of nanomedicine · 2021Article
- Implication of Potassium Channels in the Pathophysiology of Pulmonary Arterial Hypertension.Biomolecules · 2020Review
- Functional modulation of sarcolemmal KAmerican journal of physiology. Cell physiology · 2020Article
- Dynamic heterogeneity and non-Gaussian statistics for ganglioside GM1s and acetylcholine receptors on live cell membrane.Molecular biology of the cell · 2020Article
- Genetic Discovery of ATP-Sensitive KCirculation. Arrhythmia and electrophysiology · 2019Review
- A novel high-affinity inhibitor against the human ATP-sensitive Kir6.2 channel.The Journal of general physiology · 2018Article
- Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating.eLife · 2017Article
- Mitochondrial uncoupler carbonyl cyanide m-chlorophenylhydrazone induces vasorelaxation without involving KBritish journal of pharmacology · 2016Article
- Neonatal diabetes caused by a homozygous KCNJ11 mutation demonstrates that tiny changes in ATP sensitivity markedly affect diabetes risk.Diabetologia · 2016Article
- Sensitivity of KATP channels to cellular metabolic disorders and the underlying structural basis.Acta pharmacologica Sinica · 2016Article
- KATP Channels in the Cardiovascular System.Physiological reviews · 2016Review
- Vascular inward rectifier K+ channels as external K+ sensors in the control of cerebral blood flow.Microcirculation (New York, N.Y. : 1994) · 2015Review
23 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
1. We have studied the electrophysiological properties of cloned ATP-sensitive K+ channels (KATP channels) heterologously expressed in Xenopus oocytes. This channel comprises a sulphonylurea receptor subunit (SUR) and an inwardly rectifying K+ channel subunit (Kir). 2. Oocytes injected with SUR1 and either Kir6.2 or Kir6.1 exhibited large inwardly rectifying K+ currents when cytosolic ATP levels were lowered by the metabolic inhibitors azide or FCCP. No currents were observed in response to azide in oocytes injected with Kir6.2, Kir6.1 or SUR1 alone, indicating that both the sulphonylurea receptor (SUR1) and an inward rectifier (Kir6.1 or Kir6.2) are needed for functional channel activity. 3. The pharmacological properties of Kir6.2-SUR1 currents resembled those of native beta-cell ATP-sensitive K+ channel currents (KATP currents): the currents were > 90% blocked by tolbutamide (500 microM), meglitinide (10 microM) or glibenclamide (100 nM), and activated 1.8-fold by diazoxide (340 microM), 1.4-fold by pinacidil (1 mM) and unaffected by cromakalim (0.5 mM). 4. Macroscopic Kir6.2-SUR1 currents in inside-out patches were inhibited by ATP with a Ki of 28 microM. Kir6.1-SUR1 currents ran down within seconds of patch excision preventing analysis of ATP sensitivity. 5. No sensitivity to tolbutamide or metabolic inhibition was observed when SUR1 was coexpressed with either Kir1.1a or Kir2.1, suggesting that these proteins do not couple in Xenopus ocytes. 6. Our data demonstrate that the Xenopus oocyte constitutes a good expression system for cloned KATP channels and that expression may be assayed by azide-induced metabolic inhibition.
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