gAd-globular Head Domain of Adiponectin Increases Fatty Acid Oxidation in Newborn Rabbit Hearts
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Adiponectin is an adipocyte-derived hormone that has a number of metabolic effects in the body, including the control of both glucose and fatty acid metabolism. The globular head domain of adiponectin, gAd, has also been shown to increase fatty acid oxidation in skeletal muscle. Within days after birth, a rapid increase in fatty acid oxidation occurs in the heart. We examined whether adiponectin or gAd plays a role in this maturation of cardiac fatty acid oxidation. Plasma adiponectin increased in newborn rabbits following birth: 1.2 +/- 0.3 microg/ml in 1-day-old, 6.8 +/- 1.8 microg/ml in 7-day-old, and 45 +/- 5 microg/ml in 6-week-old rabbits. Because plasma insulin levels decrease and remain low throughout the suckling period, and because this decrease may contribute to the maturation of fatty acid oxidation, we examined the effects of adiponectin and gAd on fatty acid oxidation in isolated perfused 1-day-old rabbit hearts in the presence or absence of 100 microunits/ml insulin. Adiponectin (10 microg/ml) did not alter fatty acid oxidation in the presence of insulin. In the absence of insulin, the addition of recombinant gAd (1.5 microg/ml) increased fatty acid oxidation compared with control (129 +/- 18 versus 66 +/- 11 nmol.g dry weight(-1).min(-1), respectively (p < 0.05). In 7-day-old hearts, where fatty acid oxidation rates were 5-fold higher than 1-day-old hearts, gAd did not alter fatty acid oxidation rates. The increase in fatty acid oxidation in 1-day-old hearts occurred independently of changes in 5'-AMP-activated protein kinase, acetyl-CoA carboxylase, or malonyl-CoA. The effect of gAd on fatty acid oxidation was reversed in the presence of 100 microunits/ml insulin. These results suggest that a decrease in plasma insulin and increase in gAd are involved in the increase of cardiac fatty acid oxidation in the immediate newborn period.
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The COOH-terminal globular fragment of adiponectin regulates cardiac fatty acid oxidation in rabbit hearts in the immediate newborn period.
“Another study demonstrated a role for the COOH-terminal globular fragment of adiponectin in regulating cardiac fatty acid oxidation in rabbit hearts in the immediate newborn period (265).”
From Cardiac remodeling in obesity (2008) · cites this paper as [265]
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- Authors
- Onay-Besikci, A., Altarejos, J. Y., & Lopaschuk, G. D.
- Affiliations
- University of Alberta (CA)
- Corresponding author
- Lopaschuk, Gary D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-10
- Volume
- 279
- Issue
- 43
- Pages
- 44320-44326
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1993722516
- Cited by
- 53
- References
- 28
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 1 · 2022: 4 · 2021: 2 · 2019: 2 · 2018: 1 · 2016: 2 · 2015: 1 · 2014: 2 · 2013: 3 · 2012: 2
- FWCI
- 3.09
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- adiponectin, cardiac fatty acid oxidation, insulin, plasma adiponectin levels, AMPK, acetyl-CoA carboxylase, malonyl-CoA, newborn rabbits
- MeSH terms
- Acetyl-CoA Carboxylase, Acyl Coenzyme A, Animals, Animals, Newborn, Centrifugation, Density Gradient, Fatty Acids, Glucose, Heart, Insulin, Malonyl Coenzyme A, Models, Biological, Multienzyme Complexes, Myocardium, Oxygen, Phosphorylation, Rabbits, Recombinant Proteins, Serine, Sucrose, Time Factors, Blotting, Western, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, Muscle, Skeletal, Palmitic Acid, Intercellular Signaling Peptides and Proteins, Adiponectin, AMP-Activated Protein Kinases
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