Cyclic AMP and Fatty Acids Increase Carnitine Palmitoyltransferase I Gene Transcription in Cultured Fetal Rat Hepatocytes

1996 ◽  
Vol 235 (3) ◽  
pp. 789-798 ◽  
Author(s):  
Florence Chatelain ◽  
Claude Kohl ◽  
Victoria Esser ◽  
J. Denis Mcgarry ◽  
Jean Girard ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Cyclic Amp ◽  
Gene Transcription ◽  
Rat Hepatocytes ◽  
Carnitine Palmitoyltransferase ◽  
Fetal Rat ◽  
Carnitine Palmitoyltransferase I ◽  
I Gene

Regulation of liver carnitine palmitoyltransferase I gene expression by hormones and fatty acids

2001 ◽  
Vol 29 (2) ◽  
pp. 310-316 ◽  
Author(s):  
J.-F. Louet ◽  
C. Le May ◽  
J.-P. Pégorier ◽  
J.-F. Decaux ◽  
J. Girard
Keyword(s):  
Fatty Acids ◽  
Gene Transcription ◽  
Peroxisome Proliferator ◽  
Gene Encoding ◽  
First Intron ◽  
Transcriptional Effect ◽  
Carnitine Palmitoyltransferase I ◽  
Responsive Element ◽  
Cpt I ◽  
I Gene

This brief review focuses on the transcriptional regulation of liver carnitine palmitoyltransferase I (L-CPT I) by pancreatic and thyroid hormones and by long-chain fatty acids (LCFA). Both glucagon and 3,3′,5-tri-iodothyronine (T3) enhanced the transcription of the gene encoding L-CPT I, whereas insulin had the opposite effect. Interestingly, the transcriptional effect of T3 required, in addition to the thyroid-responsive element, the co-operation of a sequence located in the first intron of L-CPT I gene. Non-esterified fatty acids rather than acyl-CoA ester or intramitochondrial metabolite were responsible for the transcriptional effect on the gene encoding LCPT I. It was shown that LCFA and peroxisome proliferators stimulated L-CPT I gene transcription by distinct mechanisms. Peroxisome proliferator stimulated L-CPT I gene transcription through a peroxisome-proliferator-responsive element (PPRE) located at -2846 bp, whereas LCFA induced L-CPT I gene transcription through a peroxisome-proliferator-activated receptor α (PPARα)-independent mechanism owing to a sequence located in the first intron of the gene.

scholarly journals Fatty Acids Rapidly Induce the Carnitine Palmitoyltransferase I Gene in the Pancreatic β-Cell Line INS-1

1997 ◽  
Vol 272 (3) ◽  
pp. 1659-1664 ◽  
Author(s):  
Fran¸oise Assimacopoulos-Jeannet ◽  
Stéphane Thumelin ◽  
Enrique Roche ◽  
Victoria Esser ◽  
J. Denis McGarry ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Cell Line ◽  
Carnitine Palmitoyltransferase ◽  
Pancreatic Β Cell ◽  
Β Cell ◽  
Carnitine Palmitoyltransferase I ◽  
I Gene

scholarly journals Effect of starvation and diabetes on the sensitivity of carnitine palmitoyltransferase I to inhibition by 4-hydroxyphenylglyoxylate

1987 ◽  
Vol 243 (2) ◽  
pp. 405-412 ◽  
Author(s):  
T W Stephens ◽  
R A Harris
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Rat Hepatocytes ◽  
Isolated Hepatocytes ◽  
Carnitine Palmitoyltransferase ◽  
Time Dependent ◽  
Acid Oxidation ◽  
Moderate Increase ◽  
Dependent Manner ◽  
Carnitine Palmitoyltransferase I

The sensitivity of carnitine palmitoyltransferase I to inhibition by 4-hydroxyphenylglyoxylate was decreased markedly in liver mitochondria isolated from either 48 h-starved or streptozotocin-diabetic rats. These treatments of the rat also decreased the sensitivity of fatty acid oxidation by isolated hepatocytes to inhibition by this compound. Furthermore, incubation of hepatocytes prepared from fed rats with N6O2′-dibutyryl cyclic AMP also decreased the sensitivity, whereas incubation of hepatocytes prepared from starved rats with lactate plus pyruvate had the opposite effect on 4-hydroxyphenylglyoxylate inhibition of fatty acid oxidation. The sensitivity of carnitine palmitoyltransferase I of mitochondria to 4-hydroxyphenylglyoxylate increased in a time-dependent manner, as previously reported for malonyl-CoA. Likewise, oleoyl-CoA activated carnitine palmitoyltransferase I in a time-dependent manner and prevented the sensitization by 4-hydroxyphenylglyoxylate. Increased exogenous carnitine caused a moderate increase in fatty acid oxidation by hepatocytes under some conditions and a decreased 4-hydroxyphenylglyoxylate inhibition of fatty acid oxidation at low oleate concentration, without decreasing the difference in 4-hydroxyphenylglyoxylate inhibition between fed- and starved-rat hepatocytes. Time-dependent changes in the conformation of carnitine palmitoyltransferase I or the membrane environment may be involved in differences among nutritional states in 4-hydroxyphenylglyoxylate-sensitivity of carnitine palmitoyltransferase I.

scholarly journals Fatty acids reverse the cyclic AMP inhibition of triacylglycerol and phosphatidylcholine synthesis in rat hepatocytes

1983 ◽  
Vol 216 (1) ◽  
pp. 129-136 ◽  
Author(s):  
S L Pelech ◽  
P H Pritchard ◽  
D N Brindley ◽  
D E Vance
Keyword(s):  
Fatty Acids ◽  
Cyclic Amp ◽  
Rat Hepatocytes ◽  
Phosphocholine Cytidylyltransferase ◽  
Triacylglycerol Synthesis ◽  
Monolayer Cultures ◽  
Membrane Bound ◽  
Amp Inhibition ◽  
Phosphatidylcholine Synthesis

The influence of cyclic AMP analogues and fatty acids on glycerolipid biosynthesis in monolayer cultures of rat hepatocytes was investigated. Chlorophenylthio-cyclic AMP and adenosine 3′:5′-cyclic phosphorothioate inhibited the rate of triacylglycerol synthesis from [1(3)-3H]glycerol, and phosphatidylcholine synthesis from [Me-3H]-choline. Supplementation of the hepatocytes with palmitate (1 mM) reversed chlorophenylthio-cyclic AMP inhibition of triacylglycerol synthesis. Similarly, cyclic AMP analogue-inhibition of phosphatidylcholine synthesis was abolished when the cells were simultaneously incubated with oleate (3 mM). Reactivation of phosphatidylcholine synthesis in chlorophenylthio-cyclic AMP-supplemented cells with oleate was accompanied by conversion of CTP: phosphocholine cytidylyltransferase into the membrane-bound form, since these cells released the enzyme more slowly after treatment with digitonin. The opposing actions of cyclic AMP and fatty acids are discussed in relation to the regulation of glycerolipid biosynthesis during starvation, diabetes and stress.

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