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Cited by 146Lipid metabolism and biosynthesisAdipose Tissue and MetabolismMetabolism, Diabetes, and Cancer

Malonyl-CoA and the regulation of fatty acid oxidation in soleus muscle

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ALAM, Nasreen, SAGGERSON, E. David·1998·Biochemical Journal
DOI 10.1042/bj3340233PMC PMC1219684
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Abstract

1. Rat soleus strips were incubated with 5 mM glucose, after which tissue metabolites were measured. Alternatively, muscle strips were incubated with 5 mM glucose and 0.2 mM palmitate, and the formation of 14CO2 from exogenous palmitate or from fatty acids released from prelabelled glycerolipids was measured. 2. Etomoxir, which inhibits the mitochondrial overt form of carnitine palmitoyltransferase (CPT1), increased the tissue content of long-chain fatty acyl-CoA esters and decreased the ratio of fatty acylcarnitine to fatty acyl-CoA, suggesting that such changes could be a diagnostic for the inhibition of CPT1 3. Over a range of incubation conditions there was a positive correlation between the tissue contents of malonyl-CoA and long-chain fatty acyl-CoA esters. Under conditions in which these two metabolites increased in content (i.e. with insulin or with 3 mM dichloroacetate) there was a corresponding decrease in the ratio of fatty acylcarnitine to fatty acyl-CoA and a decrease in beta-oxidation. Isoprenaline or palmitate (0.5 mM) opposed the effect of insulin, decreasing the contents of malonyl-CoA and long-chain fatty acyl-CoA, increasing the ratio of fatty acylcarnitine to fatty acyl-CoA and increasing beta-oxidation. These findings are consistent with the notion that all of these agents can cause the acute regulation of CPT1 in Type I skeletal muscle. 4. The addition of 5-amino-4-imidazolecarboxamide ribonucleoside (AICAriboside) to cause activation of the AMP-activated protein kinase decreased the tissue content of malonyl-CoA. AICAriboside also had an antilipolytic effect in the muscle strips. 5. Measurements were made of the activities of ATP-citrate lyase, acetyl-CoA carboxylase, fatty acid synthase and malonyl-CoA decarboxylase in soleus muscle and in representative Type IIa and Type IIb muscles. A cytosolic activity of malonyl-CoA decarboxylase would seem to offer a feasible route for the disposal of malonyl-CoA in skeletal muscle.

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  • Inhibition of ACC by AMPK leads to a reduction in malonyl CoA, which allows activation of the mitochondrial fatty acid transporter CPT1 and greater flux of fatty acids into mitochondria for oxidation.

    “The inhibition of ACC by AMPK leads to a reduction in the levels of manonyl CoA, which allows for the activation of the mitochondrial fatty acid transporter Carnitine palmitoyltransferase I (CPT1) allowing for a greater flux of fatty acids into the mitochondria for oxidation [15].”

    From New strategies in sport nutrition to increase exercise performance (2016) · cites this paper as [15]

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  1. Ha, J., Lee, J.-K., Kim, K.-S., Witters, L. A. and Kim, K.-H. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 11466-11470

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Authors
ALAM, N., & SAGGERSON, E. D.
Affiliations
University College London (GB)
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
1998-08-15
Volume
334
Issue
1
Pages
233-241
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
DOI
10.1042/bj3340233
PMC
PMC1219684
OpenAlex
W131343593
Cited by
141
References
66
Citations by year
2026: 1 · 2024: 1 · 2023: 5 · 2021: 1 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 3 · 2016: 4 · 2015: 6 · 2014: 4 · 2013: 4 · 2012: 2
FWCI
4.46
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords
malonyl-CoA, fatty acid oxidation, fatty acid beta-oxidation, carnitine palmitoyltransferase 1, soleus muscle, insulin, dichloroacetate, isoproterenol, palmitate, AMPK, malonyl-CoA decarboxylase, ATP citrate lyase, acetyl-CoA carboxylase, fatty acid synthase, skeletal muscle metabolism
MeSH terms
Acyl Coenzyme A, Animals, ATP Citrate (pro-S)-Lyase, Carboxy-Lyases, Carnitine O-Palmitoyltransferase, Enzyme Inhibitors, Epoxy Compounds, Glucose, Kinetics, Malate Dehydrogenase, Male, Malonyl Coenzyme A, Models, Biological, Oxidation-Reduction, Regression Analysis, Rats, Sprague-Dawley, Muscle, Skeletal, Palmitic Acid, Rats, Fatty Acid Synthases, In Vitro Techniques

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