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The regulation of ion channels and transporters by glycolytically derived ATP
Open accessAbstract
Glycolysis is an evolutionary conserved metabolic pathway that provides small amounts of energy in the form of ATP when compared to other pathways such as oxidative phosphorylation or fatty acid oxidation. The ATP levels inside metabolically active cells are not constant and the local ATP level will depend on the site of production as well as the respective rates of ATP production, diffusion and consumption. Membrane ion transporters (pumps, exchangers and channels) are located at sites distal to the major sources of ATP formation (the mitochondria). We review evidence that the glycolytic complex is associated with membranes; both at the plasmalemma and with membranes of the endo/sarcoplasmic reticular network. We examine the evidence for the concept that many of the ion transporters are regulated preferentially by the glycolytic process. These include the Na(+)/K(+)-ATPase, the H(+)-ATPase, various types of Ca(2+)-ATPases, the Na(+)/H(+) exchanger, the ATP-sensitive K(+) channel, cation channels, Na(+) channels, Ca(2+) channels and other channels involved in intracellular Ca(2+) homeostasis. Regulation of these pumps, exchangers and ion channels by the glycolytic process has important consequences in a variety of physiological and pathophysiological processes, and a better understanding of this mode of regulation may have important consequences for developing future strategies in combating disease and developing novel therapeutic approaches.
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“There is also evidence that the glycolytic enzymes may be localized right where the neuron most requires acute resupply of ATP: at the plasma membrane and on the synaptic vesicles where major ion pumping is performed by transport ATPases (Ikemoto et al., 2003; Dhar-Chowdhury et al., 2007; Hinckelmann et al., 2016).”
From Fueling thought: Management of glycolysis and oxidative phosphorylation in neuronal metabolism (2018) · cites this paper as Dhar-Chowdhury et al., 2007
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“There is also evidence that the glycolytic enzymes may be localized right where the neuron most requires acute resupply of ATP: at the plasma membrane and on the synaptic vesicles where major ion pumping is performed by transport ATPases (Ikemoto et al., 2003; Dhar-Chowdhury et al., 2007; Hinckelmann et al., 2016).”
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Metadata
- Authors
- Dhar-Chowdhury, P., Malester, B., Rajacic, P., & Coetzee, W. A.
- Affiliations
- NYU Langone Health (US)
- Corresponding author
- Coetzee, W. A.
- ORCID
- Coetzee, W. A.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2007-09-21
- Volume
- 64
- Issue
- 23
- Pages
- 3069-3083
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11135988
- OpenAlex
- W2007360886
- Cited by
- 107
- References
- 160
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 7 · 2023: 8 · 2022: 16 · 2021: 7 · 2020: 1 · 2019: 6 · 2018: 4 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 6 · 2013: 7 · 2012: 6
- FWCI
- 1.46
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- ion channel modulation, membrane transporters, Na+/K+-ATPase, H+-ATPase, Ca2+-ATPase, Na+/H+ exchanger, cation channels, sodium channels, calcium channels, sarcoplasmic reticulum, endoplasmic reticulum, ATP levels
- MeSH terms
- Insulin Secretion, Calcium-Transporting ATPases, Sodium-Potassium-Exchanging ATPase, Animals, Blood Glucose, Cell Compartmentation, Cell Membrane, Glycolysis, Homeostasis, Humans, Insulin, Ion Channels, Ion Exchange, Potassium Channels, Proton Pumps, Membrane Transport Proteins
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