Nutritional Control of Rat Liver Fatty Acid Synthase and S14 mRNA Abundance

Clarke, Steven D.; Armstrong, Michael K.; Jump, Donald Β.

doi:10.1093/jn/120.2.218

Cited by 97 publications

(54 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This cytosolic enzyme catalyzes the formation of long chain fatty acids from acetylCoA, malonyl-CoA, and NADPH. Other authors also found that high carbohydrate (60) and cafeteria diets (high fat and high sucrose diet) (59) induced FASN expression at the mRNA level in rats. Patients suffering from non-alcoholic fatty liver disease also show an increase of expression of FASN (61) consistent with the increased FASN expression and fatty liver found in HFD-fed rats.…”

Section: Discussionmentioning

confidence: 85%

Lipogenesis Is Decreased by Grape Seed Proanthocyanidins According to Liver Proteomics of Rats Fed a High Fat Diet

Baiges

Palmfeldt

Bladé

et al. 2010

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Bioactive proanthocyanidins have been reported to have several beneficial effects on health in relation to metabolic syndrome, type 2 diabetes, and cardiovascular disease. We studied the effect of grape seed proanthocyanidin extract (GSPE) in rats fed a high fat diet (HFD). This is the first study of the effects of flavonoids on the liver proteome of rats suffering from metabolic syndrome. Three groups of rats were fed over a period of 13 weeks either a chow diet (control), an HFD, or a high fat diet supplemented for the last 10 days with GSPE (HFD ؉ GSPE). The liver proteome was fractionated, using a Triton X-114-based two-phase separation, into soluble and membrane protein fractions so that total proteome coverage was considerably improved. The data from isobaric tag for relative and absolute quantitation (

show abstract

Section: Discussionmentioning

confidence: 85%

Lipogenesis Is Decreased by Grape Seed Proanthocyanidins According to Liver Proteomics of Rats Fed a High Fat Diet

Baiges

Palmfeldt

Bladé

et al. 2010

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

show abstract

“…FAS, acetyl-CoA carboxylase, and ATP-citrate lyase (24,25)). Nuclear spot 14 protein, the expression of which matches that of lipid synthesis (26), is also induced by premature weaning and disappears in catabolic circumstances such as fasting (27). Hence, leptin, the encoded protein of the ob gene, which is secreted by the adipocyte as part of the sensing program of adipose stores, also behaves as nutritionally regulated (28).…”

Section: Discussionmentioning

confidence: 99%

Adiponutrin, a Transmembrane Protein Corresponding to a Novel Dietary- and Obesity-linked mRNA Specifically Expressed in the Adipose Lineage

Baulande

Lasnier

Lucas

et al. 2001

Journal of Biological Chemistry

219

273

View full text Add to dashboard Cite

We have used a mRNA differential display technique to identify new genes involved in the reprogramming of gene expression during the adipose conversion of mouse 3T3 preadipocyte cell lines. We report here on the identification and cloning of a novel adipose-specific cDNA encoding a predicted membrane protein of 413 amino acids. The level of the corresponding 3.2-kilobase mRNA is tremendously increased during 3T3-L1 and 3T3-F442A differentiation into adipocytes. A single, very abundant 3.2-kilobase transcript is also found in inguinal and epididymal white adipose tissues and in interscapular brown adipose tissue but not in any other tissues examined. Its expression in adipose tissue is under tight nutritional regulation. The level of this novel 3.2-kilobase transcript becomes virtually nondetectable during fasting but is dramatically increased when fasted mice are refed a high carbohydrate diet. Based on its adipose specificity and dietary regulation, the novel gene product has been designated adiponutrin. The expression of adiponutrin mRNA is also 50-fold elevated in genetically obese fa/fa rats, indicating a link between adiponutrin and obesity. Western blot and confocal imagery analyses with epitope-tagged protein transiently expressed in 3T3-L1 adipocytes, and COS cells show that adiponutrin strictly localizes to membranes and is absent from the cytosol. Sequence analysis reveals homologies with several other members of related eukaryotic proteins, including a human paralog, which has been recently described in vesicular transport mechanisms. This leads us to suggest that adiponutrin could be involved in vesicular targeting and protein transport restricted to the adipocyte function.

show abstract

“…A group of rats was also fasted for 48 h, which both increases fatty acid oxidation and decreases fatty acid biosynthesis [18][19][20]. Table 2 shows the changes seen in plasma glucose and fatty acid levels in the various rat models.…”

Section: Figure 5 Rat Liver MCD Activity and Protein Levels In 6-weekmentioning

confidence: 99%

“…Another well established protocol for altering fatty acid biosynthesis and oxidation in the liver is to starve and then refeed rats [18][19][20]. Table 2 demonstrates the significant decrease in serum glucose and increase in serum fatty acids caused by fasting.…”

Section: Figure 5 Rat Liver MCD Activity and Protein Levels In 6-weekmentioning

confidence: 99%

Characterization of rat liver malonyl-CoA decarboxylase and the study of its role in regulating fatty acid metabolism

Dyck

Berthiaume

Thomas

et al. 2000

Biochemical Journal

View full text Add to dashboard Cite

In the liver, malonyl-CoA is central to many cellular processes, including both fatty acid biosynthesis and oxidation. MalonylCoA decarboxylase (MCD) is involved in the control of cellular malonyl-CoA levels, and functions to decarboxylate malonylCoA to acetyl-CoA. MCD may play an essential role in regulating energy utilization in the liver by regulating malonyl-CoA levels in response to various nutritional or pathological states. The purpose of the present study was to investigate the role of liver MCD in the regulation of fatty acid oxidation in situations where lipid metabolism is altered. A single MCD enzyme of molecular mass 50.7 kDa was purified from rat liver using a sequential column chromatography procedure and the cDNA was subsequently cloned and sequenced. The liver MCD cDNA was identical to rat pancreatic β-cell MCD cDNA, and contained two potential translational start sites, producing proteins of 50.7 kDa and 54.7 kDa. Western blot analysis using polyclonal antibodies generated against rat liver MCD showed that the 50.7 kDa isoform of MCD is most abundant in heart and liver, and of relatively low abundance in skeletal muscle (despite elevated MCD transcript levels in skeletal muscle). Tissue distribution experiments demonstrated that the pancreas is the only rat tissue so far identified that contains both the 50.7 kDa and 54.7 kDa isoforms of MCD. In addition, transfection of the full-length rat liver MCD cDNA into COS cells produced two isoforms of MCD. This indicated either that both initiating methionines are functionally active, generating two proteins, or that the 54.7 kDa isoform is the only MCD protein translated and removal of the putative mitochondrial targeting pre-sequence generates a protein of approx. 50.7 kDa in size. To address this,

show abstract

Nutritional Control of Rat Liver Fatty Acid Synthase and S14 mRNA Abundance

Cited by 97 publications

References 24 publications

Lipogenesis Is Decreased by Grape Seed Proanthocyanidins According to Liver Proteomics of Rats Fed a High Fat Diet

Lipogenesis Is Decreased by Grape Seed Proanthocyanidins According to Liver Proteomics of Rats Fed a High Fat Diet

Adiponutrin, a Transmembrane Protein Corresponding to a Novel Dietary- and Obesity-linked mRNA Specifically Expressed in the Adipose Lineage

Characterization of rat liver malonyl-CoA decarboxylase and the study of its role in regulating fatty acid metabolism

Contact Info

Product

Resources

About