The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Intracellular ATP directly blocks K+ channels in pancreatic B-cells
Abstract
It is known that glucose-induced depolarization of pancreatic B-cells is due to reduced membrane K+-permeability and is coupled to an increase in the rate of glycolysis, but there has been no direct evidence linking specific metabolic processes or products to the closing of membrane K+ channels. During patch-clamp studies of proton inhibition of Ca2+-activated K+ channels [GK(Ca)] in B-cells, we identified a second K+-selective channel which is rapidly and reversibly inhibited by ATP applied to the cytoplasmic surface of the membrane. This channel is spontaneously active in excised patches and frequently coexists with GK(Ca) channels yet is insensitive to membrane potential and to intracellular free Ca2+ and pH. Blocking of the channel is ATP-specific and appears not to require metabolism of the ATP. This ATP-sensitive K+ channel [GK(ATP)] may be a link between metabolism and membrane K+-permeability in pancreatic B-cells.
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“Metabolic regulation of the channel is mediated by changes in the intracellular concentrations of ATP and MgADP, which inhibit and stimulate the channel, respectively (127, 163, 328).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [127]
In the citing paper
“In excised inside-out patches, ATP inhibition is half-maximal at ≈10 μM in the absence of Mg2+ (127), but this increases to 20-30 µM in the presence of Mg2+ due to the simultaneous presence of Mg-nucleotide stimulation via SUR1 (234).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [127]
Citations
Cites
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Lowering of pHi inhibits Ca2+-activated K+ channels in pancreatic B-cells
Cook, D. L., Ikeuchi, M., & Fujimoto, W. Y. (1984) · Nature · doi:10.1038/311269a0 · Cited by 264
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Research works printed but not linked: 22
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Feng, Z., & Sun, H. (2017) · Springer series in translational stroke research · doi:10.1007/978-3-319-45345-3_7 · Cited by 3
Metadata
- Authors
- Cook, D. L., & Hales, N.
- Affiliations
- United States Department of Veterans Affairs (US)
- Venue
- Nature
- Published
- 1984-09
- Volume
- 311
- Issue
- 5983
- Pages
- 271-273
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1985770721
- Cited by
- 1,208
- References
- 24
- Citations by year
- 2026: 11 · 2025: 16 · 2024: 12 · 2023: 22 · 2022: 14 · 2021: 21 · 2020: 12 · 2019: 19 · 2018: 13 · 2017: 9 · 2016: 15 · 2015: 21 · 2014: 34 · 2013: 14 · 2012: 29
- FWCI
- 13.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Keywords
- ATP-sensitive potassium channels, pancreatic beta cells, intracellular ATP, potassium channel inhibition, glycolysis, proton inhibition, calcium-activated potassium channels
- MeSH terms
- Adenosine Triphosphate, Animals, Cell Membrane Permeability, Cells, Cultured, Cytoplasm, Electric Conductivity, Ion Channels, Islets of Langerhans, Potassium, Rats
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