Linked Life Data

11811466

Source:http://linkedlifedata.com/resource/pubmed/id/11811466

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2002-1-28
pubmed:abstractText
A trial was conducted to biochemically explain the decreased lipid deposition and increased protein accretion observed in pigs fed carnitine. Our hypothesis was that an increase in the ratio of acetyl CoA:CoA-SH produced by stimulation of fatty acid oxidation by supplemental L-carnitine may decrease branched-chain alpha-keto acid dehydrogenase activity and increase pyruvate carboxylase activity. Such changes could reduce oxidative loss of branched-chain amino acids and provide more carbons for amino acid biosynthesis. Yorkshire gilts (n = 36; 12 per treatment) were fed a control diet or diets containing either 50 or 125 ppm of added L-carnitine during growth from 56 to 120 kg. After slaughter, the semitendinosus muscle and liver were collected for isolation of mitochondria and hepatocytes. Increasing dietary L-carnitine did not influence growth performance (P > 0.10) but linearly decreased (P < 0.05) 10th rib backfat thickness and increased (linear, P < 0.05) percentages of lean and muscle. The rates of [1-(14)G]palmitate oxidation in isolated hepatocytes and isolated mitochondria, and incorporation of [35S]methionine into the acid insoluble fraction of isolated hepatocytes were increased (linear, P < 0.01) in pigs fed L-carnitine. Flux through branched-chain alpha-keto acid dehydrogenase linearly decreased (P < 0.01) in isolated liver and muscle mitochondria with increasing dietary carnitine. Flux through pyruvate carboxylase was increased (linear, P < 0.01) in isolated mitochondria from liver of pigs fed carnitine, and assays with particle-free extracts indicated that the amount of mitochondrial pyruvate carboxylase was tripled by feeding carnitine (linear, P < 0.01). The association of increased protein accretion and reduced backfat thickness with greater rates of palmitate oxidation, more rapid flux through pyruvate carboxylase, and reduced flux through branched-chain alpha-keto acid dehydrogenase suggests pigs fed carnitine are more able to use fat for energy, divert carbon toward synthesis of amino acids, and spare branched-chain amino acids for protein synthesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-8812
pubmed:author
pubmed:issnType
Print
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3104-12
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11811466-3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide), pubmed-meshheading:11811466-Adipose Tissue, pubmed-meshheading:11811466-Amino Acids, Branched-Chain, pubmed-meshheading:11811466-Animals, pubmed-meshheading:11811466-Body Composition, pubmed-meshheading:11811466-Carnitine, pubmed-meshheading:11811466-Female, pubmed-meshheading:11811466-Hepatocytes, pubmed-meshheading:11811466-Ketone Oxidoreductases, pubmed-meshheading:11811466-Mitochondria, Liver, pubmed-meshheading:11811466-Mitochondria, Muscle, pubmed-meshheading:11811466-Multienzyme Complexes, pubmed-meshheading:11811466-Muscle, Skeletal, pubmed-meshheading:11811466-Palmitates, pubmed-meshheading:11811466-Protein Biosynthesis, pubmed-meshheading:11811466-Pyruvate Carboxylase, pubmed-meshheading:11811466-Swine
pubmed:year
2001
pubmed:articleTitle
Dietary L-carnitine suppresses mitochondrial branched-chain keto acid dehydrogenase activity and enhances protein accretion and carcass characteristics of swine.
pubmed:affiliation
Department of Animal Sciences and Industry, Kansas State University, Manhattan 66506-0201, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't