Intracellular ADP activates K+ channels that are inhibited by ATP in an insulin‐secreting cell line
Open accessAbstract
the effect of ADP on ATP‐sensitive K+ channels in the insulin‐secreting RINm5F cell line has been investigated with the help of single‐channel current recording from saponin‐permeabilized cells. ADP (100–500 μM) markedly activates K+ channels when added to the bath solution in contact with the membrane inside. ADP‐β‐S cannot mimick this effect. During sustained ATP (500 μM)‐evoked inhibition of K+ channel opening, 500 μM ADP markedly and reversibly activates the channels. Conversely ATP markedly reduces the opening probability of ADP‐activated channels. It is suggested that the physiological control of K+ channel opening in the insulin‐secreting cells is mediated by changes in ATP/ADP ratio rather than being solely determined by the ATP concentration.
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Metabolic regulation of the KATP channel is mediated by changes in intracellular concentrations of ATP and MgADP, which inhibit and stimulate the channel, respectively.
“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 [163]
The Results report that ADP activated ATP-inhibited K+ channels in permeabilized RINmSF cells and that ATP closed ADP-activated channels. The Discussion proposes that changes in the ATP/ADP ratio regulate channel opening after metabolic stimulation. The paper identifies the activating substance as ADP, however, and does not establish that MgADP specifically mediates the effect. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe lower ATP sensitivity of the KATP channel in the intact cell is due to the presence of intracellular MgADP, and glucose acts by changing the relative concentrations of ATP and ADP.
“There is considerable evidence that the lower ATP sensitivity of the KATP channel in the intact cell is due to the presence of intracellular MgADP, as in this configuration KATP channel activity persists at intracellular ATP concentrations normally associated with nearly complete inhibition of channel activity (72, 163, 328, 366). This suggests that glucose acts by changing the relative Concentra”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [163]
The Introduction notes that channels remain active in intact cells despite ATP concentrations that inhibit them in excised patches. The Results show that ADP activates ATP-inhibited channels, and the Discussion proposes that glucose-related changes in the ATP/ADP ratio regulate channel opening. The paper does not specifically identify MgADP or establish that it causes the lower apparent ATP sensitivity in intact cells. (LLM, conf=0.87)
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Cites
Intracellular ATP directly blocks K+ channels in pancreatic B-cells
Cook, D. L., & Hales, N. (1984) · Nature · doi:10.1038/311271a0 · Cited by 1,208 · see citing works
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Research works printed but not linked: 1
- Dunne, M.J., Findlay, I., Petersen, O.H. and Wollheim, C.B. (1986) J. Membr. Biol., in press.
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Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men
Rorsman, P., & Ashcroft, F. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00008.2017 · Cited by 793 · see citing works
Clinical and molecular characterisation of 300 patients with congenital hyperinsulinism
Kapoor, R. R., Flanagan, S. E., Arya, V. B., Shield, J. P., Ellard, S., & Hussain, K. (2013) · European Journal of Endocrinology · doi:10.1530/eje-12-0673 · Cited by 243 · see citing works
- Authors
- Dunne, M. J., & Petersen, O. H.
- Affiliations
- University of Liverpool (GB)
- Corresponding author
- Petersen, Ole H.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1986-11-10
- Volume
- 208
- Issue
- 1
- Pages
- 59-62
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1997849672
- Cited by
- 229
- References
- 1
- Citations by year
- 2026: 1 · 2024: 2 · 2023: 3 · 2022: 5 · 2021: 5 · 2020: 1 · 2019: 1 · 2018: 3 · 2017: 5 · 2016: 3 · 2015: 2 · 2014: 2 · 2013: 6 · 2012: 3
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Université de Genève
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Adenosine and Purinergic Signaling
- Keywords
- ADP, ATP-sensitive potassium channels, ATP, insulin secretion, RINm5F cells, potassium channel activation, ATP/ADP ratio, intracellular nucleotides, single-channel recording, saponin-permeabilized cells
- MeSH terms
- Insulin Secretion, Adenine Nucleotides, Adenosine Diphosphate, Adenosine Triphosphate, Cell Line, Insulin, Ion Channels, Membrane Potentials, Potassium
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