Acute Hyperglycemia Provides an Insulin-Independent Inducer for GLUT4 Translocation in C2C12 Myotubes and Rat Skeletal Muscle
Abstract
GLUT4 translocation and activation of glucose uptake in skeletal muscle can be induced by both physiological (i.e., insulin, nerve stimulation, or exercise) and pharmacological (i.e., phorbol ester) means. Recently, we demonstrated that high glucose levels may mimic the effects of phorbol esters on protein kinase C (PKC) and insulin receptor function (J Biol Chem 269:3381–3386, 1994). In this study, we tested whether the previously described effects of phorbol esters on translocation of GLUT4 in myotubes in culture and also in rat skeletal muscle might be mimicked by glucose. We found that stimulation of C2C12 myotubes with both insulin (10–7) mol/l, 5 min) and glucose (25 mmol/l, 10 min) induces a comparable increase of the GLUT4 content in the plasma membrane. To test whether this effect occurs in intact rat skeletal muscle as well, two different model systems were used. As an in vitro model, isolated rat hindlimbs were perfused for 80 min with medium containing 6 mmol/l glucose ± insulin (1.6 × 10–9 mmol/l, 40 min) or 25 mmol/l glucose. As an in vivo model, acute hyperglycemia (> 11 mmol/l glucose, 20 min) was induced in Wistar rats by intraperitoneal injection of glucose under simultaneous suppression of the endogenous insulin release by injection of somatostatin. In both models, subcellular fractions were prepared from hindlimb skeletal muscle, and plasma membranes were characterized by the enrichment of the marker enzyme α1 Na+ -K+ -ATPase. Acute hyperglaycemia in vivo (n = 5) and in vitro (n = 6) induced an increases of GLUT4 content in the α1 Na+ -K+ -ATPase–enriched fraction (in vivo, 2.45 ± 0.47-fold increase to basal [mean ±SE]; in vitro, 1.71 ± 0.14-fold increase to basal), which was Quantitatively similar to that obtained after insulin treatment (in vivi, 2.35 ± 0.62-fold increase to basal; in vitro, 1.91 ± 0.21-fold increase to basal). Glucose-in-duced GLUT4 translocation in myotubes was prevented by prior addition of the PKC inhibitor 1-(5-isoquinolinyl-by prior addition of the PKC inhibitor 1-(5-isoquinolinyl-sulfonyl)-2-methylpiperazine; in rat skeletal muscle,GLUT4 translocation was paralleled by a translocation of PKC β, while no effect on PKC α, δ, ∊, and ζ was observed. These results suggest that glucose-induced GLUT4 translocation might represenet an insulin-independent autoregulatory mechanism of the skeletal muscle to rapidly increase glucose uptake in acute hyperglycemia. Activation of PKC β might be involved in this mechanisum in skeletal muscle. GLUT4 translocation was paralleled by a translocation of PKC β, while no effect on PKC α, δ, μ, and ¶ was observed. These results suggest that glucose-induced GLUT4 translocation might represent an insulin-independent autoregulatory mechanism of the skeletal muscle to rapidly increase glucose uptake in acute hyperglycemia. Activation of PKC P might be involved in this mechanism in skeletal muscle.
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Hyperglycemia induces translocation of GLUT4 transporters to the plasma membrane in muscle.
“Furthermore, hyperglycemia has been demonstrated to induce translocation of GLUT4 transporters to the plasma membrane in muscle (17).”
From Impaired basal glucose effectiveness but unaltered fasting glucose release and gluconeogenesis during short-term hypercortisolemia in healthy subjects (2004) · cites this paper as [17]
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The Effects of Interleukin-10 on Skeletal Muscle Insulin Resistance and Myogenesis
Dağdeviren, S. (2016) · eScholarship@UMassChan · doi:10.13028/m2qp42 · Cited by 1 · see citing works
“On the other hand, researchers stated that during hyperglycemia, half of the total glucose uptake in the skeletal muscle is non-insulin dependent [98] and hyperglycemia can increase GLUT4 translocation to the membrane [102].”
BackgroundIn vivo Glut4 translocation in lean and fatty Zucker rat hearts: effect of insulin dose and time
Li, W.-M. (1996) · doi:10.14288/1.0087192
“In addition to cardiac tissue, it has been shown in skeletal muscle that acute hyperglycemia could induce Glut4 translocation both under in vitro and in vivo conditions with the effect comparable to that of insulin (Galante et al., 1995).”
Background
- Authors
- Galante, P., Mosthaf, L., Kellerer, M., Berti, L., Tippmer, S., Bossenmaier, B., Fujiwara, T., Okuno, A., Horikoshi, H., & Ulrich Häring, H.
- Affiliations
- Institute of Diabetes Research (DE)
- Sankyo Company Limited Pharmacology and Molecular Biology Laboratories Tokyo, Japan
- Institut für Diabetesforschung Munich, Germany
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 1995-06-01
- Volume
- 44
- Issue
- 6
- Pages
- 646-651
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2107184306
- Cited by
- 77
- References
- 0
- Citations by year
- 2025: 1 · 2023: 3 · 2022: 3 · 2020: 2 · 2019: 1 · 2018: 2 · 2016: 5 · 2015: 2 · 2014: 1 · 2013: 2 · 2012: 3
- FWCI
- 1.49
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes, Cardiovascular Risks, and Lipoproteins
- Keywords
- GLUT4 translocation, acute hyperglycemia, glucose uptake, skeletal muscle, C2C12 myotubes, insulin-independent glucose transport, phorbol ester, protein kinase C, insulin receptor, somatostatin, hindlimb perfusion, plasma membrane, Na+/K+-ATPase, glucose transporter 4, insulin signaling, neurostimulation
- MeSH terms
- Animals, Biological Transport, Cell Membrane, Glucose, Hyperglycemia, Monosaccharide Transport Proteins, Muscle Proteins, Protein Kinase C, Rats, Wistar, Muscle, Skeletal, Glucose Transporter Type 4, Rats
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