Document Detail


Peroxisome proliferator-activated receptor alpha and enzymes of carnitine biosynthesis in the liver are down-regulated during lactation in rats.
MedLine Citation:
PMID:  19154956     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
This study investigated the hypothesis that lactation lowers gene expression of peroxisome proliferator-activated receptor (PPAR) alpha in the liver and that this leads to a down-regulation of hepatic enzymes involved in carnitine synthesis and novel organic cation transporters (OCTNs). Thirty-two pregnant female rats were divided into 4 groups. In the first group, all pups were removed, whereas in the other groups, litters were adjusted to sizes of 4, 10, or 18 pups per dam. Dams suckling their litters, irrespective of litter size, had lower relative messenger RNA concentrations of PPARalpha, various classic PPARalpha target genes involved in fatty acid catabolism, as well as enzymes involved in carnitine synthesis (trimethyllysine dioxygenase, 4-N-trimethylaminobutyraldehyde dehydrogenase, gamma-butyrobetaine dioxygenase) and OCTN1 in the liver than dams whose litters were removed (P < .05). Moreover, dams suckling their litters had a reduced activity of gamma-butyrobetaine dioxygenase in the liver and reduced concentrations of carnitine in plasma, liver, and muscle compared with dams without litters (P < .05). In conclusion, the present study demonstrates for the first time that lactation leads to a down-regulation of PPARalpha and genes involved in hepatic carnitine synthesis and uptake of carnitine (OCTN1) in the liver, irrespective of litter size. It is moreover suggested that down-regulation of PPARalpha in the liver may be a means to conserve energy and metabolic substrates for milk production in the mammary gland.
Authors:
Anke Gutgesell; Robert Ringseis; Corinna Brandsch; Gabriele I Stangl; Frank Hirche; Klaus Eder
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Metabolism: clinical and experimental     Volume:  58     ISSN:  1532-8600     ISO Abbreviation:  Metab. Clin. Exp.     Publication Date:  2009 Feb 
Date Detail:
Created Date:  2009-01-21     Completed Date:  2009-02-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0375267     Medline TA:  Metabolism     Country:  United States    
Other Details:
Languages:  eng     Pagination:  226-32     Citation Subset:  IM    
Affiliation:
Institute of Agricultural and Nutritional Sciences, Martin-Luther-University of Halle-Wittenberg, D-06108 Halle, Saale, Germany.
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MeSH Terms
Descriptor/Qualifier:
Aldehyde Oxidoreductases / genetics,  metabolism
Animals
Carnitine / biosynthesis*
Carrier Proteins / genetics,  metabolism
Down-Regulation / physiology
Eating / physiology
Energy Metabolism / physiology
Fatty Acid Transport Proteins / genetics,  metabolism
Fatty Acids, Nonesterified / blood
Female
Gene Expression Regulation, Enzymologic / physiology
Lactation / physiology*
Litter Size
Liver / physiology*
Male
Mammary Glands, Animal / physiology
Membrane Proteins / genetics,  metabolism
Mixed Function Oxygenases / genetics,  metabolism
PPAR alpha / genetics*,  metabolism
Pregnancy
RNA, Messenger / metabolism
Rats
gamma-Butyrobetaine Dioxygenase / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Fatty Acid Transport Proteins; 0/Fatty Acids, Nonesterified; 0/Membrane Proteins; 0/Octn1 protein, rat; 0/PPAR alpha; 0/RNA, Messenger; 541-15-1/Carnitine; EC 1.-/Mixed Function Oxygenases; EC 1.14.11.-/trimethyl-lysine hydroxylase; EC 1.14.11.1/gamma-Butyrobetaine Dioxygenase; EC 1.2.-/4-N-trimethylaminobutyraldehyde dehydrogenase; EC 1.2.-/Aldehyde Oxidoreductases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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