THE INTRACELLULAR FREE FATTY ACID POOL IN ADIPOSE TISSUE

2009 ◽  
Vol 20 (5) ◽  
pp. 154-157 ◽  
Keyword(s):  
Adipose Tissue ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Acid Pool ◽  
Fatty Acid Pool

scholarly journals Lipolysis and the Free Fatty Acid Pool in Seedlings

1964 ◽  
Vol 39 (6) ◽  
pp. 880-883 ◽  
Author(s):  
Allen J. St. Angelo ◽  
Aaron M. Altschul
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Acid Pool ◽  
Fatty Acid Pool

The subcellular distribution of free fatty acids released during post-decapitative ischemia in rat cerebral cortex

1985 ◽  
Vol 63 (11) ◽  
pp. 1183-1188 ◽  
Author(s):  
R. Roy Baker ◽  
Zou Dao Loh
Keyword(s):  
Fatty Acids ◽  
Cerebral Cortex ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Free Fatty Acids ◽  
Subcellular Distribution ◽  
Phospholipase A ◽  
C Cells ◽  
Acid Pool ◽  
Fatty Acid Pool

After periods of 5 and 30 min following decapitation, rat cerebral cortices were removed and subcellular fractions were prepared. Fractions P1A (large myelin), P1B (nuclei), P1C (cells and debris), P2A (small myelin), P2B (synaptosomes), P2C (mitochondria), and P3 (microsomes) were isolated. Free fatty acid levels of 1.0 and 1.4 μmol/g tissue were found in the homogenates at the early and late times of ischemia. In the 30-min samples, P1A, P1C, and P2A had relatively high specific contents of total free fatty acids in comparison with other subfractions. At this time P2C was relatively enriched in arachidonate, P1A and P2A were enriched in palmitate, and P2B and P3 were enriched in stearate in comparison with the homogenate. P2C had the highest ratio of polyunsaturates/saturates in its free fatty acid pool. Comparing the 5- and 30-min samples, a large increase in the quantity of free fatty acids was found in fractions P1A and P2A, so that at the later time P1A + P2A contained 60 mol% of the free fatty acid in the total subfractions derived from cerebral cortex. In comparison with the homogenate, the lack of accumulation of free fatty acids in certain membranes known to possess phospholipase activities (e.g., phospholipase A2 in P2C) and the buildup of free fatty acids in P1A and P2A led to the hypothesis that free fatty acids may be migrating outwards from intracellular sites of production and accumulating in the multilamellar structure of myelin.

Chylomicron triglyceride metabolism in resting and exercising fed dogs

1982 ◽  
Vol 52 (4) ◽  
pp. 815-820 ◽  
Author(s):  
R. L. Terjung ◽  
L. Budohoski ◽  
K. Nazar ◽  
A. Kobryn ◽  
H. Kaciuba-Uscilko
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Corn Oil ◽  
Removal Rate ◽  
Moderate Intensity ◽  
Beta Oxidation ◽  
Fed State ◽  
Acid Pool ◽  
Fatty Acid Pool

The turnover of circulating triglycerides (TG) was determined in dogs during rest, following ingestion of food that included corn oil, and in the final period of a 1-h treadmill exercise of moderate intensity (72–84 m/min). In all cases the loss of [14C]TG from the plasma followed a first-order process. The fractional removal rate constant at rest was 26.5 +/- 1.9% (SE) n = 10) of the circulating pool size per minute, and it was increased slightly to 33.8 +/- 3.6% (n = 7) per minute during exercise. The uptake of plasma TG-derived fatty acids (5 min postinjection) was increased (P less than 0.05) in working muscle, whereas the TG uptake in fat tended to decrease. Further, the percent of TG-derived fatty acids found in the muscle's acylglyceride pool was less (90.0 +/- 3.6 vs. 53.5 +/- 1.8%), while that in the muscle's free fatty acid pool was greater (12.3 +/- 36.1 +/- 4.7%) in working compared with resting muscle. Thus the fourfold greater quantity of plasma TG-derived fatty acids found in the working muscle's free fatty acid pool could account for the entire increased TG uptake caused by exercise. This suggests that, in the fed state, circulating TG could represent a potential source of fatty acids for beta-oxidation in working muscle. However, the importance of plasma TG-derived fatty acids as an energy substrate during muscle use in a postprandial state has yet to be determined quantitatively.

scholarly journals Flavour development via lipolysis of milkfats: changes in free fatty acid pool

2007 ◽  
Vol 42 (8) ◽  
pp. 961-968 ◽  
Author(s):  
Mafalda A. Regado ◽  
Betina M. Cristóvão ◽  
Carla G. Moutinho ◽  
Victor M. Balcão ◽  
Raquel Aires-Barros ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Acid Pool ◽  
Fatty Acid Pool

scholarly journals The Fatty Acid Pool in Adipose Tissue

1961 ◽  
Vol 236 (12) ◽  
pp. 3121-3124 ◽  
Author(s):  
Vincent P. Dole
Keyword(s):  
Adipose Tissue ◽  
Fatty Acid ◽  
Acid Pool ◽  
Fatty Acid Pool

scholarly journals Clearing-factor lipase in adipose tissue. A possible role of adenosine 3′,5′-(cyclic)-monophosphate in the regulation of its activity

1968 ◽  
Vol 109 (5) ◽  
pp. 841-849 ◽  
Author(s):  
D. R. Wing ◽  
D S Robinson
Keyword(s):  
Adipose Tissue ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Cyclic Amp ◽  
Lipase Activity ◽  
Glucose Concentration ◽  
Free Fatty Acid Concentration ◽  
Epididymal Fat ◽  
Fat Bodies

1. The rise in clearing-factor lipase activity that occurs when epididymal fat bodies from starved rats are incubated in appropriate media in vitro is inhibited in the presence of 6-N-2′-O-dibutyryl-3′,5′-(cyclic)-AMP (1mm). 2. Inhibition occurs at a concentration of glucose in the incubation medium of 1·3mg./ml. or less, but not at a glucose concentration of 2·4mg./ml., unless caffeine (1mm), an inhibitor of 3′,5′-(cyclic)-nucleotide phosphodiesterase, is also present. Caffeine (5mm) alone inhibits the rise in clearing-factor lipase activity at a glucose concentration of 2·4mg./ml. of medium. 3. The concentration of free fatty acids in the epididymal fat bodies normally falls during incubations in vitro as the rise in clearing-factor lipase activity occurs. In the presence of 1mm-6-N-2′-O-dibutyryl-3′,5′-(cyclic)-AMP, however, either the tissue free fatty acid concentration is increased or it does not fall to the same extent. The concentration of glucose in the incubation medium is important in determining the direction and extent of the changes in tissue free fatty acid concentration that occur in the presence of 6-N-2′-O-dibutyryl-3′,5′-(cyclic)-AMP. 4. Free fatty acid concentrations in epididymal fat bodies in vivo rise as the clearing-factor lipase activity of the tissue falls during starvation. 5. The possibility that the concentration of 3′,5′-(cyclic)-AMP in adipose tissue may regulate clearing-factor lipase activity, and that the regulation may occur through effects of the nucleotide on tissue free fatty acid concentrations, is discussed.

scholarly journals Cellular retinol-binding protein type III is a PPARγ target gene and plays a role in lipid metabolism

2008 ◽  
Vol 295 (6) ◽  
pp. E1358-E1368 ◽  
Author(s):  
Cynthia F. Zizola ◽  
Gary J. Schwartz ◽  
Silke Vogel
Keyword(s):  
Adipose Tissue ◽  
Fatty Acid ◽  
Lipid Metabolism ◽  
Free Fatty Acid ◽  
Target Gene ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Wild Type ◽  
Type Iii ◽  
Cellular Retinol Binding Protein

Cellular retinol-binding protein (CRBP) type III (CRBP-III) belongs to the family of intracellular lipid-binding proteins, which includes the adipocyte-binding protein aP2. In the cytosol, CRBP-III binds retinol, the precursor of retinyl ester and the active metabolite retinoic acid. The goal of the present work is to understand the regulation of CRBP-III expression and its role in lipid metabolism. Using EMSAs, luciferase reporter assays, and chromatin immunoprecipitation assays, we found that CRBP-III is a direct target of peroxisome proliferator-activated receptor-γ (PPARγ). Moreover, CRBP-III expression was induced in adipose tissue of mice after treatment with the PPARγ agonist rosiglitazone. To examine a potential role of CRBP-III in regulating lipid metabolism in vivo, CRBP-III-deficient (C-III-KO) mice were maintained on a high-fat diet (HFD). Hepatic steatosis was decreased in HFD-fed C-III-KO compared with HFD-fed wild-type mice. These differences were partly explained by decreased serum free fatty acid levels and decreased free fatty acid efflux from adipose tissue of C-III-KO mice. In addition, the lack of CRBP-III was associated with reduced food intake, increased respiratory energy ratio, and altered body composition, with decreased adiposity and increased lean body mass. Furthermore, expression of genes involved in mitochondrial fatty acid oxidation in brown adipose tissue was increased in C-III-KO mice, and C-III-KO mice were more cold tolerant than wild-type mice fed an HFD. In summary, we demonstrate that CRBP-III is a PPARγ target gene and plays a role in lipid and whole body energy metabolism.

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