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Cited by 125Ion Transport and Channel RegulationMetabolism, Diabetes, and CancerATP Synthase and ATPases Research

The mechanism of insulin stimulation of (Na+,K+)-ATPase transport activity in muscle

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Rosić, N K, Standaert, M L, Pollet, R J·1985·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)88958-x
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Abstract

Since the mechanism underlying the insulin stimulation of (Na+,K+)-ATPase transport activity observed in multiple tissues has remained undetermined, we have examined (Na+,K+)-ATPase transport activity (ouabain-sensitive 86Rb+ uptake) and Na+/H+ exchange transport (amiloride-sensitive 22Na+ influx) in differentiated BC3H-1 cultured myocytes as a model of insulin action in muscle. The active uptake of 86Rb+ was sensitive to physiological insulin concentrations (1 nM), yielding a maximum increase of 60% without any change in 86Rb+ permeability. In order to determine the mechanism of insulin stimulation of (Na+,K+)-ATPase activity, we demonstrated that insulin also stimulates passive 22Na+ influx by Na+/H+ exchange transport (maximal 200% increase) and an 80% increase in intracellular Na+ concentration with an identical time course and dose-response curve as insulin-stimulated (Na+,K+)-ATPase transport activity. Incubation of the cells with high [Na+] (195 mM) significantly potentiated insulin stimulation of ouabain-inhibitable 86Rb+ uptake. The ionophore monensin, which also promotes passive Na+ entry into BC3H-1 cells, mimics the insulin stimulation of ouabain-inhibitable 86Rb+ uptake. In contrast, incubation with amiloride or low [Na+] (10 mM), both of which inhibit Na+/H+ exchange transport, abolished the insulin stimulation of (Na+,K+)-ATPase transport activity. Furthermore, each of these insulin-stimulated transport activities displayed a similar sensitivity to amiloride. These results indicate that insulin stimulates a large increase in Na+/H+ exchange transport and that the resulting Na+ influx increases the intracellular Na+ concentration, thus activating the internal Na+ transport sites of the (Na+,K+)-ATPase. This Na+ influx is, therefore, the mediator of the insulin-induced stimulation of membrane (Na+,K+)-ATPase transport activity classically observed in muscle.

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Authors
Rosić, N. K., Standaert, M. L., & Pollet, R. J.
Affiliations
University of South Florida (US)
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1985-05
Volume
260
Issue
10
Pages
6206-6212
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(18)88958-x
OpenAlex
W1604267989
Cited by
125
References
72
Citations by year
2026: 2 · 2024: 1 · 2022: 4 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 4 · 2016: 1 · 2015: 1 · 2014: 1
FWCI
4.54
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
National Institutes of Health (5r01am018608-10)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
insulin, Na+/K+-ATPase, Na+/H+ exchange, muscle, intracellular sodium, 86Rb uptake, amiloride, monensin, insulin signaling
MeSH terms
Sodium-Potassium-Exchanging ATPase, Animals, Biological Transport, Active, Carrier Proteins, Cell Line, Insulin, Muscles, Rubidium, Sodium, Sodium-Hydrogen Exchangers, Mice

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