Skeletal muscle mitochondrial FAT/CD36 content and palmitate oxidation are not decreased in obese women. 2007

Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
Department of Human Health & Nutritional Sciences, University of Guelph, 50 Stone Rd., Guelph, Ontario, Canada N1G2W1. ghollowa@uoguelph.ca

A reduction in fatty acid oxidation has been associated with lipid accumulation and insulin resistance in the skeletal muscle of obese individuals. We examined whether this decrease in fatty acid oxidation was attributable to a reduction in muscle mitochondrial content and/or a dysfunction in fatty acid oxidation within mitochondria obtained from skeletal muscle of age-matched, lean [body mass index (BMI) = 23.3 +/- 0.7 kg/m2] and obese women (BMI = 37.6 +/- 2.2 kg/m2). The mitochondrial marker enzymes citrate synthase (-34%), beta-hydroxyacyl-CoA dehydrogenase (-17%), and cytochrome c oxidase (-32%) were reduced (P < 0.05) in obese participants, indicating that mitochondrial content was diminished. Obesity did not alter the ability of isolated mitochondria to oxidize palmitate; however, fatty acid oxidation was reduced at the whole muscle level by 28% (P < 0.05) in the obese. Mitochondrial fatty acid translocase (FAT/CD36) did not differ in lean and obese individuals, but mitochondrial FAT/CD36 was correlated with mitochondrial fatty acid oxidation (r = 0.67, P < 0.05). We conclude that the reduction in fatty acid oxidation in obese individuals is attributable to a decrease in mitochondrial content, not to an intrinsic defect in the mitochondria obtained from skeletal muscle of obese individuals. In addition, it appears that mitochondrial FAT/CD36 may be involved in regulating fatty acid oxidation in human skeletal muscle.

UI MeSH Term Description Entries
D008875 Middle Aged An adult aged 45 - 64 years. Middle Age
D008931 Mitochondria, Muscle Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available. Sarcosomes,Mitochondrion, Muscle,Muscle Mitochondria,Muscle Mitochondrion,Sarcosome
D009765 Obesity A status with BODY WEIGHT that is grossly above the recommended standards, usually due to accumulation of excess FATS in the body. The standards may vary with age, sex, genetic or cultural background. In the BODY MASS INDEX, a BMI greater than 30.0 kg/m2 is considered obese, and a BMI greater than 40.0 kg/m2 is considered morbidly obese (MORBID OBESITY).
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010168 Palmitates Salts and esters of the 16-carbon saturated monocarboxylic acid--palmitic acid. Hexadecanoates,Palmitate
D002787 Sterol Esterase An enzyme that catalyzes the hydrolysis of CHOLESTEROL ESTERS and some other sterol esters, to liberate cholesterol plus a fatty acid anion. Cholesterol Esterase,15-Ketosteryl Oleate Hydrolase,Acylcholesterol Lipase,Cholesterol Ester Hydrolase,Cholesteryl Oleate Hydrolase,Cholesterylester Hydrolase,Hormone-Sensitive Lipase,Lipase A (Lysosomal Acid Cholesterol Esterase),Lipoidal Steroid Esterase,Lysosomal Acid Cholesterol Esterase,Lysosomal Acid Lipase,Steroid Hormone Esterase,Sterol Ester Acylhydrolase,15 Ketosteryl Oleate Hydrolase,Acid Lipase, Lysosomal,Acylhydrolase, Sterol Ester,Esterase, Cholesterol,Esterase, Lipoidal Steroid,Esterase, Steroid Hormone,Esterase, Sterol,Hormone Sensitive Lipase,Hydrolase, 15-Ketosteryl Oleate,Hydrolase, Cholesterol Ester,Hydrolase, Cholesteryl Oleate,Hydrolase, Cholesterylester,Lipase, Acylcholesterol,Lipase, Hormone-Sensitive,Steroid Esterase, Lipoidal
D002950 Citrate (si)-Synthase Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7. Citrate Synthase,Synthase, Citrate
D003576 Electron Transport Complex IV A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane. Cytochrome Oxidase,Cytochrome aa3,Cytochrome-c Oxidase,Cytochrome Oxidase Subunit III,Cytochrome a,a3,Cytochrome c Oxidase Subunit VIa,Cytochrome-c Oxidase (Complex IV),Cytochrome-c Oxidase Subunit III,Cytochrome-c Oxidase Subunit IV,Ferrocytochrome c Oxygen Oxidoreductase,Heme aa3 Cytochrome Oxidase,Pre-CTOX p25,Signal Peptide p25-Subunit IV Cytochrome Oxidase,Subunit III, Cytochrome Oxidase,p25 Presequence Peptide-Cytochrome Oxidase,Cytochrome c Oxidase,Cytochrome c Oxidase Subunit III,Cytochrome c Oxidase Subunit IV,Oxidase, Cytochrome,Oxidase, Cytochrome-c,Signal Peptide p25 Subunit IV Cytochrome Oxidase,p25 Presequence Peptide Cytochrome Oxidase
D005227 Fatty Acids Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed) Aliphatic Acid,Esterified Fatty Acid,Fatty Acid,Fatty Acids, Esterified,Fatty Acids, Saturated,Saturated Fatty Acid,Aliphatic Acids,Acid, Aliphatic,Acid, Esterified Fatty,Acid, Saturated Fatty,Esterified Fatty Acids,Fatty Acid, Esterified,Fatty Acid, Saturated,Saturated Fatty Acids
D005260 Female Females

Related Publications

Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
October 2009, American journal of physiology. Regulatory, integrative and comparative physiology,
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
April 1995, Journal of applied physiology (Bethesda, Md. : 1985),
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
June 1981, Biochemical and biophysical research communications,
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
December 2016, Journal of exercise nutrition & biochemistry,
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
July 2005, The Journal of clinical investigation,
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
May 1982, Biochimica et biophysica acta,
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
September 2006, American journal of physiology. Endocrinology and metabolism,
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
January 1995, Obesity research,
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
November 1982, Biochimica et biophysica acta,
Graham P Holloway, and A Brianne Thrush, and George J F Heigenhauser, and Narendra N Tandon, and David J Dyck, and Arend Bonen, and Lawrence L Spriet
August 2006, American journal of physiology. Endocrinology and metabolism,
Copied contents to your clipboard!