ArticleFrontiers in neuroenergetics2010
General requirement for harvesting antennae at ca and h channels and transporters.
Article in Frontiers in neuroenergetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 23 citations in OpenAlex.
- Local Attraction of Substrates and Co-Substrates Enhances Weak Acid and Base Transmembrane Transport.Biomolecules · 2022Review
- Proton Transport in Cancer Cells: The Role of Carbonic Anhydrases.International journal of molecular sciences · 2021Review
- Basigin drives intracellular accumulation of l-lactate by harvesting protons and substrate anions.PloS one · 2021Article
- Fluid Brain Glycolysis: Limits, Speed, Location, Moonlighting, and the Fates of Glycogen and Lactate.Neurochemical research · 2020Review
- Carbonic anhydrase IX and acid transport in cancer.British journal of cancer · 2020Review
- Catalytically inactive carbonic anhydrase-related proteins enhance transport of lactate by MCT1.FEBS open bio · 2019Article
- Membrane-anchored carbonic anhydrase IV interacts with monocarboxylate transporters via their chaperones CD147 and GP70.The Journal of biological chemistry · 2019Article
- The proteoglycan-like domain of carbonic anhydrase IX mediates non-catalytic facilitation of lactate transport in cancer cells.Oncotarget · 2018Article
- A surface proton antenna in carbonic anhydrase II supports lactate transport in cancer cells.eLife · 2018Article
- The Astrocyte: Powerhouse and Recycling Center.Cold Spring Harbor perspectives in biology · 2015Review
- Analysis of the binding moiety mediating the interaction between monocarboxylate transporters and carbonic anhydrase II.The Journal of biological chemistry · 2015Article
- Intracellular and extracellular carbonic anhydrases cooperate non-enzymatically to enhance activity of monocarboxylate transporters.The Journal of biological chemistry · 2014Article
- Small is fast: astrocytic glucose and lactate metabolism at cellular resolution.Frontiers in cellular neuroscience · 2013Article
- Lactate flux in astrocytes is enhanced by a non-catalytic action of carbonic anhydrase II.The Journal of physiology · 2012Article
- Aspects of astrocyte energy metabolism, amino acid neurotransmitter homoeostasis and metabolic compartmentation.ASN neuro · 2012Review
- Intramolecular proton shuttle supports not only catalytic but also noncatalytic function of carbonic anhydrase II.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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
The production and dissipation of energy in cells is intimately linked to the movement of small molecules in and out of enzymes, channels, and transporters. An analytical model of diffusion was described previously, which was used to estimate local effects of these proteins acting as molecular sources. The present article describes a simple but more general model, which can be used to estimate the local impact of proteins acting as molecular sinks. The results show that the enzymes, transporters, and channels, whose substrates are present at relatively high concentrations like ATP, Na(+), glucose, lactate, and pyruvate, do not operate fast enough to deplete their vicinity to a meaningful extent, supporting the notion that for these molecules the cytosol is a well-mixed compartment. One specific consequence of this analysis is that the well-documented cross-talk existing between the Na(+)/K(+) ATPase and the glycolytic machinery should not be explained by putative changes in local ATP concentration. In contrast, Ca2(+) and H(+) transporters like the Na(+)/Ca2(+) exchanger NCX and the Na(+)/H(+) exchanger NHE, show experimental rates of transport that are two to three orders of magnitude faster than the rates at which the aqueous phase may possibly feed their binding sites. This paradoxical result implies that Ca2(+) and H(+) transporters do not extract their substrates directly from the bulk cytosol, but from an intermediate "harvesting" compartment located between the aqueous phase and the transport site.
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