期刊
BIOCHEMICAL JOURNAL
卷 354, 期 -, 页码 189-197出版社
PORTLAND PRESS
DOI: 10.1042/0264-6021:3540189
关键词
cultured hepatocyte; long-chain fatty acyl-CoA; PPAR alpha-null mice; transient transfection
Liver carnitine palmitoyltransferase I (L-CPT I) catalyses the transfer of long-chain fatty acid (LCFA) for translocation across the mitochondrial membrane. Expression of the L-CPT I gene is induced by LCFAs as well as by lipid-lowering compounds such as clofibrate, Previous studies have suggested that the peroxisome-proliferator-activated receptor alpha (PPAR alpha) is a common mediator of the transcriptional effects of LCFA and clofibrate, We found that free LCFAs rather than acyl-CoA eaters are the signal metabolites responsible for the stimulation of L-CPT I gene expression. Using primary culture of hepatocytes we found that LCFAs failed to stimulate L-CPT I gene expression both in wild-type and PPAR alpha -null mice. These results suggest that the PPAR alpha -knockout mouse does not represent a suitable model for the regulation of L-CPT I gene expression by LCFAs in the liver. Finally, we determined that clofibrate stimulates L-CPT I through a classical direct repeat 1 (DR1) motif in the promoter of the L-CPT I gene while LCFAs induce L-CPT I via elements in the first intron of the gene, Our results demonstrate that LCFAs can regulate gene expression through PPAR alpha -independent pathways and suggest that the regulation of gene expression by dietary lipids is more complex than previously proposed.
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