Effect of carnitine on branched-chain amino acid oxidation by liver and skeletal muscle. 1978

H S Paul, and S A Adibi

The effect of L-carnitine (0.5-2.0 mM) on the rates of alpha-decarboxylation of 1-14C-labeled branched-chain amino acids by gastrocnemius muscle and liver homogenates of fed rats was investigated. Carnitine increased the rate of alpha-decarboxylation of leucine (125%) and valine (28%) by muscle, but it was without effect on the oxidation of these amino acids by liver. Carnitine increased the rate of alpha-decarboxylation of alpha-ketoisocaproate by both tissues. This effect was more pronounced in muscle (130% increase) than in liver (41% increase). The activity of carnitine acyltransferase, with isovaleryl-CoA as a substrate, was 18 times higher in muscle mitochondria than in liver mitochondria. Both starvation and diabetes increased the rate of alpha-decarboxylation of leucine by muscle without having a remarkable effect on the concentration of carnitine or the activity of carnitine acyltransferase. We conclude that: a) carnitine stimulates decarboxylation of branched-chain amino acids by increasing the conversion of their ketoanalogues into carnitine esters, b) a greater carnitine acyltransferase activity in muscle than in liver may be responsible for the greater carnitine effect in muscle, c) carnitine does not appear responsible for the enhancement of leucine oxidation by muscle of starved and diabetic rats.

UI MeSH Term Description Entries
D007930 Leucine An essential branched-chain amino acid important for hemoglobin formation. L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
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
D002208 Caproates Derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated six carbon aliphatic structure. Hexanoates,Caproic Acid Derivatives,Caproic Acids,Hexanoic Acid Derivatives,Hexanoic Acids,Acid Derivatives, Caproic,Acid Derivatives, Hexanoic,Acids, Caproic,Acids, Hexanoic,Derivatives, Caproic Acid,Derivatives, Hexanoic Acid
D002331 Carnitine A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism. Bicarnesine,L-Carnitine,Levocarnitine,Vitamin BT,L Carnitine
D002333 Carnitine Acyltransferases Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. EC 2.3.1. Acylcarnitine Translocase,Carnitine Translocase,Carnitine-Acetylcarnitine Translocase,Carnitine-Acylcarnitine Translocase,Acyltransferases, Carnitine,Carnitine Acetylcarnitine Translocase,Carnitine Acylcarnitine Translocase,Translocase, Acylcarnitine,Translocase, Carnitine,Translocase, Carnitine-Acetylcarnitine,Translocase, Carnitine-Acylcarnitine
D003921 Diabetes Mellitus, Experimental Diabetes mellitus induced experimentally by administration of various diabetogenic agents or by PANCREATECTOMY. Alloxan Diabetes,Streptozocin Diabetes,Streptozotocin Diabetes,Experimental Diabetes Mellitus,Diabete, Streptozocin,Diabetes, Alloxan,Diabetes, Streptozocin,Diabetes, Streptozotocin,Streptozocin Diabete
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino

Related Publications

H S Paul, and S A Adibi
January 1986, JPEN. Journal of parenteral and enteral nutrition,
H S Paul, and S A Adibi
February 2006, The Journal of nutrition,
H S Paul, and S A Adibi
December 2017, European journal of gastroenterology & hepatology,
H S Paul, and S A Adibi
August 1959, The American journal of physiology,
H S Paul, and S A Adibi
September 1980, The Journal of biological chemistry,
H S Paul, and S A Adibi
July 1976, Biochimica et biophysica acta,
Copied contents to your clipboard!