Cited by 107Metabolism, Diabetes, and CancerLipid metabolism and biosynthesisAdipose Tissue and Metabolism

Effects of individual fatty acids on glucose uptake and glycogen synthesis in soleus muscle in vitro

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Thompson, Alison L., Lim-Fraser, Megan Y.-C., Kraegen, Edward W., Cooney, Gregory J.·2000·American Journal of Physiology-Endocrinology and Metabolism

Abstract

Soleus muscle strips from Wistar rats were preincubated with palmitate in vitro before the determination of insulin-mediated glucose metabolism in fatty acid-free medium. Palmitate decreased insulin-stimulated glycogen synthesis to 51% of control in a time- (0–6 h) and concentration-dependent (0–2 mM) manner. Basal and insulin-stimulated glucose transport/phosphorylation also decreased with time, but the decrease occurred after the effect on glycogen synthesis. Preincubation with 1 mM palmitate, oleate, linoleate, or linolenate for 4 h impaired glycogen synthesis stimulated with a submaximal physiological insulin concentration (300 μU/ml) to 50–60% of the control response, and this reduction was associated with impaired insulin-stimulated phosphorylation of protein kinase B (PKB). Preincubation with different fatty acids (all 1 mM for 4 h) had varying effects on insulin-stimulated glucose transport/phosphorylation, which was decreased by oleate and linoleate, whereas palmitate and linolenate had little effect. Across groups, the rates of glucose transport/phosphorylation correlated with the intramuscular long-chain acyl-CoA content. The similar effects of individual fatty acids on glycogen synthesis but different effects on insulin-stimulated glucose transport/phosphorylation provide evidence that lipids may interact with these two pathways via different mechanisms.

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Crossref · 10.1152/ajpendo.2000.279.3.e577

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  • Exposure to NEFA in vitro decreased insulin-mediated glucose uptake and glycogen synthesis and reduced beta-cell function, including reduced insulin release and impaired proinsulin to insulin processing.

    “Exposure to NEFA in vitro decreased insulin-mediated glucose uptake and glycogen synthesis [146] as well as reduced beta-cell function [147, 148], encompassing both reduced insulin release and impaired proinsulin to insulin processing.”

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References 44 · Cited by 107

Authors
Thompson, A. L., Lim-Fraser, M. Y.-C., Kraegen, E. W., & Cooney, G. J.
Affiliations
Garvan Institute of Medical Research (AU)
Venue
American Journal of Physiology-Endocrinology and Metabolism
Published
2000-09-01
Volume
279
Issue
3
Pages
E577-E584
ISSN
  • 0193-1849 (ISSN-L)
  • 1522-1555
OpenAlex
W1778141833
Cited by
107
References
44
Citations by year
2025: 2 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 1 · 2015: 3 · 2014: 7 · 2013: 5 · 2012: 4
FWCI
2.53
Type
journal article
Language
en
Open access
Locations
  • American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Royal Society
  • University of New South Wales
  • Medical Research Council
  • National Health and Medical Research Council
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
Keywords
fatty acids, palmitate, oleate, linoleate, linolenic acid, insulin-stimulated glucose uptake, glucose transport, glucose phosphorylation, glycogen synthesis, Akt, soleus muscle, long-chain acyl-CoA, skeletal muscle glucose metabolism
MeSH terms
Acyl Coenzyme A, Adenosine Triphosphate, Animals, Dietary Fats, Fatty Acids, Glucose, Glycogen, Insulin, Insulin Resistance, Male, Monosaccharide Transport Proteins, Proto-Oncogene Proteins, Rats, Wistar, Protein Serine-Threonine Kinases, Muscle, Skeletal, Glucose-6-Phosphate, Proto-Oncogene Proteins c-akt, Rats, In Vitro Techniques

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