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PubMed2005

Palmitate induces tumor necrosis factor-alpha expression in C2C12 skeletal muscle cells by a mechanism involving protein kinase C and nuclear factor-kappaB activation.

The mechanisms responsible for increased expression of TNF-alpha in skeletal muscle cells in diabetic states are not well understood. We examined the effects of the saturated acid palmitate on TNF-alpha expression. Exposure of C2C12 skeletal muscle cells to 0.75 mm palmitate enhanced mRNA (25-fold induction, P < 0.001) and protein (2.5-fold induction) expression of the proinflammatory cytokine TNF-alpha. This induction was inversely correlated with a fall in GLUT4 mRNA levels (57% reduction, P < 0.001) and glucose uptake (34% reduction, P < 0.001). PD98059 and U0126, inhibitors of the ERK-MAPK cascade, partially prevented the palmitate-induced TNF-alpha expression. Palmitate increased nuclear factor (NF)-kappaB activation and incubation of the cells with the NF-kappaB inhibitors pyrrolidine dithiocarbamate and parthenolide partially prevented TNF-alpha expression. Incubation of palmitate-treated cells with calphostin C, a strong and specific inhibitor of protein kinase C (PKC), abolished palmitate-induced TNF-alpha expression, and restored GLUT4 mRNA levels. Palmitate treatment enhanced the expression of phospho-PKCtheta, suggesting that this PKC isoform was involved in the changes reported, and coincubation of palmitate-treated cells with the PKC inhibitor chelerythrine prevented the palmitate-induced reduction in the expression of IkappaBalpha and insulin-stimulated Akt activation. These findings suggest that enhanced TNF-alpha expression and GLUT4 down-regulation caused by palmitate are mediated through the PKC activation, confirming that this enzyme may be a target for either the prevention or the treatment of fatty acid-induced insulin resistance.

Alkaloids↗
PubMed1991

Regulation of in vitro palmitate oxidation in liver from dairy cows during early lactation.

Regulatory effects of carnitine, glucose, some glucogenic compounds (propionate, pyruvate, alanine, lactate, glycerol, and fructose), ketone bodies (acetate, acetoacetate, and beta-hydroxybutyrate), and insulin on oxidation of palmitate were studied in slices of liver obtained from high producing dairy cows during early lactation. A total of 77 biopsies of liver from 21 multiparous Holstein cows (36 +/- 16 d postpartum) was used. L-Carnitine increased oxidation of palmitate to CO2 by more than twofold and oxidation to acid-soluble products by about fourfold. Propionate decreased oxidation of palmitate in liver slices incubated without added carnitine, but the decrease was lessened by carnitine. Pyruvate, lactate, and alanine increased palmitate oxidation, especially in the presence of carnitine. Glycerol, glucose, and insulin tended to decrease palmitate oxidation in the absence of carnitine. Fructose tended to decrease oxidation to CO2 but did not affect oxidation to acid-soluble products. Acetate and acetoacetate decreased oxidation of palmitate, whereas beta-hydroxybutyrate decreased palmitate oxidation in the absence of carnitine but increased palmitate oxidation in its presence. In general, carnitine decreased the inhibitory effects of compounds that decreased palmitate oxidation but increased the stimulatory effects of compounds that increased palmitate oxidation.

Alanine↗
PubMed2002

Insulin secretion induced by palmitate--a process fully dependent on glucose concentration.

The effect of 0.1 mM palmitate on insulin secretion by 1 hr incubated pancreatic islets was examined in the presence of different glucose concentrations (5.6 and 16.7 mM). The oxidation of both glucose and palmitate and the incorporation of [U-14C]-palmitate into lipid fractions and phospholipid species were determined. In the presence of 5.6 mM glucose, palmitate reduced insulin release by 80%. In contrast, in the presence of 16.7 mM glucose, palmitate raised the amount of insulin released by 49%. Palmitate (0.1 mM) caused a significant reduction (52%) of [U-14C]-glucose decarboxylation at 5.6 mM but it did not have any effect at 16.7 mM glucose. The decarboxylation of [U-14C]-palmitate was markedly lower (94%) in the presence of 16.7 mM, as compared to 5.6 mM glucose. [U-14C]-Palmitate was significantly incorporated into total lipid fractions in the presence of both glucose concentrations. The increase in glucose concentration from 5.6 to 16.7 mM raised by 138% the incorporation of [U-14C]-palmitate into phospholipids: phosphatidylcholine (PC), phosphatidylserine (PS), phosphatidylethanolamine (PE), phosphatidic acid (PA) and phosphatidylinositol (PI). PC and PA at 0.1 mM raised by three and four-fold, respectively, insulin release by incubated pancreatic islets. We postulated that palmitate (at 0.1 mM) promotes a deviation of glycerol-phosphate to lipid synthesis, decreasing glucose oxidation (at 5.6 mM) and possibly ATP/ADP ratio in the cytosol, leading to a reduction in insulin secretion. At 16.7 mM glucose concentration, the high glycolytic flux is now enough to provide glycerol-phosphate for lipid synthesis and carbons for the Krebs cycle. So, under this condition, ATP production might be not reduced. The increase in the production of PA and PC may explain the increase in insulin secretion observed at 16.7 mM glucose.

Animals↗
PubMed2003

The effect of retinyl palmitate added to iron-fortified maize porridge on erythrocyte incorporation of iron in African children with vitamin A deficiency.

Retinyl palmitate added to Fe-fortified maize bread has been reported to enhance Fe absorption in adult Venezuelan subjects but not in Western Europeans. It is not known to what extent these results were influenced by differences in vitamin A status of the study subjects. The objective of the present study was to evaluate the influence of retinyl palmitate added to Fe-fortified maize porridge on erythrocyte incorporation of Fe in children with vitamin A deficiency, before and after vitamin A supplementation. Erythrocyte incorporation of Fe-stable isotopes was measured 14 d after intake of maize porridge (2.0 mg Fe added as ferrous sulfate) with and without added retinyl palmitate (3.5 micromol; 3300 IU). The study was repeated 3 weeks after vitamin A supplementation (intake of a single dose of 210 micromol retinyl palmitate; 'vitamin A capsule'). Vitamin A status was evaluated by the modified relative dose-response (MRDR) technique. Retinyl palmitate added to the test meal reduced the geometric mean erythrocyte incorporation of Fe at baseline from 4.0 to 2.6 % (P=0.008, n 13; paired t test). At 3 weeks after vitamin A supplementation, geometric mean erythrocyte incorporation was 1.9 and 2.3 % respectively from the test meal with and without added retinyl palmitate (P=0.283). Mean dehydroretinol:retinol molar ratios were 0.156 and 0.125 before and after intake of the single dose of 210 micromol retinyl palmitate; 'vitamin A capsule' (P=0.15). In conclusion, retinyl palmitate added to the labelled test meals significantly decreased erythrocyte incorporation of Fe in children with vitamin A deficiency at baseline but had no statistically significant effect 3 weeks after vitamin A supplementation. The difference in response to retinyl palmitate added to Fe-fortified maize porridge on erythrocyte incorporation of Fe before and after intake of the vitamin A capsule indicates, indirectly, changes in vitamin A status not measurable by the MRDR technique. The lack of conclusive data on the effect of retinyl palmitate on Fe absorption indicates the complexity of the interactions between vitamin A status, dietary vitamin A and Fe metabolism.

Adolescent↗
PubMed1987

Hydrolysis of 11-cis- and all-trans-retinyl palmitate by homogenates of human retinal epithelial cells.

The retinal epithelium plays an important role in the storage and metabolism of retinoids in the eye. Studies were conducted to examine the enzymatic hydrolysis of retinyl esters by human retinal epithelial cells. Homogenates prepared from these cells were found to hydrolyze both the 11-cis- and all-trans-isomers of retinyl palmitate. Retinyl ester hydrolysis was time-, protein-, and pH-dependent. The 11-cis isomer was hydrolyzed at a rate which was approximately 20 times greater than that of the all-trans isomer. The 11-cis-retinyl palmitate hydrolase activity did not require detergents, unlike the all-trans-retinyl palmitate hydrolase activity, which required detergents for activity. The 11-cis-retinyl palmitate hydrolase activity was maximally active with the addition of 1.0% sodium taurocholate at about pH 8.5, was abolished by incubation at 50 degrees C for 10 min, and was quantitatively recovered in the pellet after centrifugation at 100,000 X g for 1 h. The rate of hydrolysis of 11-cis-retinyl palmitate became saturated with increasing concentrations of 11-cis-retinyl palmitate; under the assay conditions employed, the hydrolase activity had an apparent Km of 19 microM toward 11-cis-retinyl palmitate. All-trans-retinol and 11-cis-retinyl did not affect the rate of hydrolysis of 11-cis-retinyl palmitate, and addition of all-trans-retinyl palmitate only weakly inhibited the 11-cis-retinyl palmitate hydrolytic activities. These data indicate that the human retinal epithelium possesses distinct activities for the hydrolysis of 11-cis- and all-trans-retinyl esters and raise the possibility that these activities may provide a means of distinguishing the stereoisomers of retinol in this tissue.

Adult↗
PubMedDate not supplied

Modeling of palmitate transport in the heart.

Transport of palmitate from the albumin-palmitate complex in the plasma to inside mitochondria where it undergoes beta-oxidation is a multistep process. Albumin's large size prevents permeation via interendothelial clefts. Palmitate dissociation from albumin in solution is too slow to provide an adequate supply of the unbound palmitate. The discovery that the dissociation occurs upon albumin binding to an endothelial surface receptor resolves the conundrum. Palmitate transport across the luminal surface membrane may be either carrier-mediated or passive. Fatty-acid binding protein inside endothelial and cardiac muscle cells facilitates diffusion through cytosol while maintaining the unbound palmitate concentration at a very low level. Within the interstitium, albumin is again the palmitate carrier. Still controversial is whether or not there is a saturable sarcolemmal transporter or simply passive exchange. Inside the myocyte palmitate is again bound to the fatty acid binding protein which buffers the free palmitate concentration, facilitates diffusion, and may facilitate further intracellular reactions.

Animals↗
PubMed1989

Study of amino acid formation during palmitate oxidation in rat brain mitochondria.

The interrelation of palmitate oxidation with amino acid formation in rat brain mitochondria has been investigated in purified mitochondria of nonsynaptic origin by measuring the formation of aspartate, alpha-ketoglutarate, and glutamate during palmitate oxidation, and also by assaying 14C-products of [1-14C]palmitate oxidation. Oxidation of palmitate (or [1-14C]palmitate) resulted in the formation of aspartate (or 14C-aspartate), and the oxidation was inhibited by aminooxyacetate (an inhibitor of transaminase). Palmitate oxidation also resulted in alpha-ketoglutarate formation, which was sensitive to the effect of aminooxyacetate. Addition of NH4Cl was found to increase 14C-products and formation of alpha-ketoglutarate, whereas glutamate formation was not increased unless the rate of palmitate oxidation was reduced by 50% by aminooxyacetate or alpha-ketoglutarate was added exogenously. Exogenous alpha-ketoglutarate was found to decrease 14C-products, but not aspartate formation. These results indicated that palmitate oxidation was closely related to aspartate formation via aspartate aminotransferase. During palmitate oxidation without aminooxyacetate or added alpha-ketoglutarate, however, alpha-ketoglutarate was not available for glutamate formation via glutamate dehydrogenase. We discuss the possibility that this was because (a) oxidative decarboxylation of alpha-ketoglutarate to form succinyl-CoA was favored over glutamate formation for the competition for alpha-ketoglutarate in the same pool, and (b) the pool of alpha-ketoglutarate produced in the aspartate aminotransferase reaction did not serve as substrate for glutamate formation.

Aminooxyacetic Acid↗
PubMed1985

Reciprocal effects of energy utilization on palmitate oxidation and esterification in hepatocytes of fed rats.

The effects of the energy-dependent process of urea synthesis from NH4Cl on the partition of [1-14C]palmitate between oxidation and esterification were examined in hepatocytes of fed rats. A high rate of urea formation from NH4Cl resulted in stimulation of total palmitate oxidation by 25 and 15% at 0.2 and 1 mM fatty acid, respectively. The stimulation of palmitate oxidation was reciprocally correlated with diminished palmitate incorporation into lipids, mainly triacylglycerols. This relationship was almost stoichiometric. NH4Cl increased the palmitate oxidation/esterification ratio from 0.72 to 1.13 and from 0.94 to 1.36 in the presence of 0.2 mM and 1 mM palmitate, respectively. The transaminase inhibitor, aminooxyacetate, strongly inhibited urea synthesis from NH4Cl, had little effect on the low beta-hydroxybutyrate/acetoacetate ratio in the presence of NH4Cl, completely reversed the changes in palmitate metabolism caused by NH4Cl and did not affect palmitate metabolism in the absence of NH4Cl. Therefore, the increased utilization of energy for urea synthesis was the causative factor by which NH4Cl stimulated total palmitate oxidation and led in consequence to its decreased esterification into lipids. Accordingly, these observations indicate that in liver cells the rate of ATP utilization is one of the determinants of triacylglycerol synthesis.

Aminooxyacetic Acid↗
PubMed1988

Precipitation of calcium palmitate from bile salt-containing dispersions.

Addition of calcium chloride to mixed micellar systems composed of sodium salts of palmitic acid and high concentrations of different bile acids results in precipitation of Ca(palmitate)2 only when the palmitate concentration exceeds a critical value, which is dependent on the concentrations of Ca2+, Na+ and bile salt, and on the type of bile salt used. All these dependencies, as well as the complex and interrelated effects of the various parameters on the kinetics of Ca(palmitate)2 precipitation are consistent with the following mechanism: (i) calcium binds to palmitate-bile salt mixed micelles and promotes their aggregation, at a rate governed by the concentration ratio between bound calcium and micelles (here denoted "binding ratio"). (ii) Ca(palmitate)2 precipitation occurs within the aggregate of micelles only if those micelles include sufficient amounts of Ca2+ and palmitate to allow for the formation of large enough crystal units of Ca(palmitate)2 which can serve as nucleation "seeds". Both the concentrations of micelles and Na+ have dual effects on the rate of precipitation. Increasing micelle concentration, by itself, accelerates aggregation but at the same time leads to a decrease of the binding ratio, thus reducing the rate of precipitation. Na+ which reduces the binding ratio through competitive binding also reduces the surface charge, thus assisting micelle aggregation. Our model also explains the facilitation of precipitation observed when phosphatidylcholine is contained in the palmitate-bile salt mixed micelles and the inhibitory effect of the water soluble bovine serum albumin.

Bile Acids and Salts↗
PubMed1994

Measurement of palmitate availability in serum samples: method and utility.

Palmitic acid shows a very low and unknown solubility at neutral pH. Binding equilibria of palmitate to human serum albumin accordingly cannot be investigated by measuring free and bound ligand concentrations as in conventional binding studies. It is feasible, on the other hand, to describe the binding equilibria in relative terms, by measuring the concentration, p, of reserve albumin, previously defined as the concentration of a purified standard albumin preparation which in buffered solution binds a trace amount of palmitate as tight as it is bound in the sample. Palmitate availability is calculated as C/p, when C is the concentration of bound palmitate. The general binding equation is modified to contain the availability beside relative binding constants, Li = Ki/K1,St, where K1,St is the first stoichiometric binding constant for palmitate to the standard albumin preparation. Availabilities and relative binding constants can replace free concentrations and usual binding constants in considerations of biochemical transport and enzymatic mechanisms. A method is described for measuring the concentration of reserve albumin for binding of palmitate, based upon determination of dialytic exchange rates for palmitate among identical equilibrium samples. A technique for reproducibly adding radiolabelled palmitate to the samples is given.

Adult↗
PubMed1987

Palmitate uptake in calcium tolerant, adult rat myocardial single cells--evidence for an albumin mediated transport across sarcolemma.

The dependence of (1-14C)-palmitate uptake in adult rat heart single cells on albumin was investigated. The apparent initial rate of palmitate uptake vs total palmitate concentration exhibited saturation kinetics, provided the concentration ratio of palmitate vs albumin was kept constant. However, if total palmitate was increased at constant albumin concentrations, the dependence of the initial rate on palmitate concentration was linear. Within the concentration range of total palmitate investigated in this study, the concentration of free palmitate remained almost constant. These results favour the hypothesis, that palmitate uptake in rat myocardium may be mediated by an albumin dependent sarcolemmal transport system.

Albumins↗
PubMed1977

Influence of acetate on the metabolism of palmitate in the perfused hind-quarter of the rat.

The metabolism of 1-14C-palmitate and its metabolic interaction with U-14C-acetate were studied in the perfused hind-quarter of the rat. 9% of 1-14C-palmitate taken up was oxidized to 14CO2 accounting for 7% of total oxygen consumption by the perfused tissue. Most label from 1-14C-palmitate was found in the lipid fraction of the muscle tissue. In spite of a 40% inhibition of palmitate oxidation, acetate only caused minor changes in the overall metabolism of palmitate. U-14C-acetate was mainly oxidized to 14CO2 and the oxygen consumption due to oxidation of acetate accounted for 20-30% of the total oxygen uptake. Minor amounts of 14C-acetate were found in muscle lipids. The addition of palmitate did not alter the metabolism of acetate. It is concluded that the presence of palmitate did not affect 14C-acetate metabolism, while the presence of acetate inhibited 14C-palmitate oxidation. The possible sites of interaction are discussed. The found interaction will probably not contribute to any major extent to the disturbed lipid metabolism found in animals and man during ethanol intake. No major changes in the tissue content of high-energy phosphate compounds were found in the presence of palmitate or acetate or both.

Acetates↗
PubMed1990

Uptake of palmitic acid by rabbit alveolar type II cells.

Alveolar type II cells require a source of palmitic acid for synthesis of dipalmitoyl phosphatidylcholine (DPPC), a major constituent of pulmonary surfactant. Previous studies indicated that maximal rates of DPPC synthesis are achieved only if exogenous palmitate is available to the type II cell. Little is known of the mechanisms by which fatty acids enter type II cells. To determine if uptake is mediated by a membrane carrier system, as described in other cell types, we examined the kinetics of palmitate uptake. Using freshly isolated rabbit type II cells, we demonstrated that radiolabeled palmitate uptake was maximal and linear for 45 s; after 1 min the apparent rate of uptake declined. The initial uptake phase was taken as a measure of cellular fatty acid influx because intracellular radiolabeled palmitate remained 80% nonesterified at this time but was 55% esterified by 2 min. Cellular influx of palmitate showed saturation kinetics with increasing concentration of nonalbumin bound palmitate. Michaelis constant was 52.6 nM, and maximum velocity was 152 pmol.10(6) cells-1.min-1. The hypothesis that saturable cellular influx of palmitate is likely linked to the previously identified membrane fatty acid binding protein (MFABP) was supported by Western-blot analysis of rat lung tissue with an antibody to MFABP that demonstrated the presence of this carrier protein in lung tissue. These data suggest that palmitate uptake by type II cells is saturable and may be mediated by a membrane-associated carrier as described in other cell types.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1989

Effects of inhibition of fatty acid oxidation on myocardial kinetics of 11C-labeled palmitate.

The effects of glucose and lactate infusion on palmitate oxidation were compared with the effect of 2-tetradecylglycidic acid (TDGA), an irreversible inhibitor of the carnitine acyltransferase I, in normoxic canine myocardium. The initial capillary transit retention fraction of [1-11C]palmitate and its fractional distribution between oxidation and esterification in myocardium were measured by the residue detection method after intracoronary tracer injection, as well as by effluent measurements of 11CO2, the end product of palmitate oxidation. TDGA reduced the initial capillary transit retention fraction (from 56 +/- 13% to 37 +/- 6%; p less than 0.001) and oxidation of palmitate (n = 19), as also evidenced by the decrease in the fraction of tracer released as 11CO2 from 28 +/- 5% to 6 +/- 3% (p less than 0.001). Infusion of carbohydrate (glucose or lactate; n = 6) reduced 11CO2 production from 30 +/- 7% to 7 +/- 4% (p less than 0.05) but did not alter the initial capillary transit retention fraction of tracer (59 +/- 5% vs. 56 +/- 10%; NS). The latter was due to increased esterification into neutral lipids (41 +/- 11% of injected palmitate after carbohydrate infusion versus 21 +/- 12% in control conditions), as measured from multiexponential curve fittings. When carbohydrates were given after inhibition of palmitate oxidation by TDGA (n = 7), the 11C tissue clearance kinetics were strikingly similar to those observed after carbohydrate infusion alone. Thus, enhanced metabolic trapping of [1-11C]palmitate in myocardium resulted in initial capillary transit retention fractions that were not different from control conditions (41 +/- 5% vs. 48 +/- 12%; NS) despite inhibition of oxidation. The results show that the intracellular metabolism of palmitate contributes to the control of its uptake by myocardium. The findings are consistent with inhibition of palmitate oxidation by carbohydrates occurring at the same site as TDGA.

Animals↗
PubMed1990

Glucose and palmitate oxidation in isolated working rat hearts reperfused after a period of transient global ischemia.

Alterations in energy substrate utilization during reperfusion of ischemic hearts can influence the functional recovery of the myocardium. Energy substrate preference by the reperfused myocardium, however, has received limited attention. Therefore, we measured oxidation rates of glucose and palmitate during reperfusion of ischemic hearts. Isolated working rat hearts were perfused with 1.2 mM palmitate and 11 mM [14C]glucose, 1.2 mM [14C]palmitate and 11 mM glucose, or 11 mM [14C]glucose alone, at an 11.5 mm Hg preload and 80 mm Hg afterload. Hearts were subjected to 60-minute aerobic perfusion or 25-minute global ischemia followed by 60-minute aerobic reperfusion. Steady-state oxidative rates of glucose or palmitate were determined by measuring 14CO2 production. In hearts perfused with glucose alone, oxidative rates during reperfusion were not significantly different than nonischemic hearts (1,008 +/- 335 vs. 1,372 +/- 117 nmol [14C]glucose oxidized/min/g dry wt, respectively). In the presence of palmitate, glucose oxidation was markedly reduced in reperfused and nonischemic hearts (81 +/- 11 and 101 +/- 15 nmol [14C]glucose oxidized/min/g dry wt, respectively). Palmitate oxidation rates were not significantly different in reperfused compared with nonischemic hearts (369 +/- 55 and 455 +/- 50 nmol [14C]palmitate oxidized/min/g dry wt, respectively). [14C]Palmitate was incorporated into myocardial triglycerides to a greater extent in reperfused ischemic hearts than in nonischemic hearts (26.0 and 13.8 mumol/g dry wt, respectively). Under the perfusion conditions used, palmitate provided over 90% of the ATP produced from exogenous substrates. Addition of the carnitine palmitoyltransferase I inhibitor, ethyl 2-[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylate (Etomoxir, 10(-6) M), during reperfusion stimulated glucose oxidation and improved mechanical recovery of ischemic hearts.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMedDate not supplied

Influence of sodium palmitate on the cellular action of potentials of the left ventricle of isolated, perfused guinea-pig heart.

Influence of sodium palmitate on the cellular action potentials of the left ventricle of isolated, perfused guinea-pig heart. Acta Physiol. Pol. 1975, 26 (1): 1-11. Transmembrane action potentials (APs) were recorded from the left ventricle and glucose uptake was estimated in the isolated guinea-pig hearts perfused with Langendorff method. After the control period the perfusion fluid was changed for the solution of altered composition containing: 1) 0.5 mM of palmitate complexed with 4% albumin and no glucose; 2) 0.1 mM or 0.5 mM of palmitate added to solution containing 11 mM of glucose; 3) substrate-free solution; 4) solution equilibrated with 5% CO-2 + 95% N-2. In all experimental groups marked shortening of AP duration was observed accompanied by the shortening of the functional refractory period and by the desynchronization of repolarization. The effect of perfusion with the substrate-free solution was similar to that evoked by substituting palmitate for glucose. In all the groups except for anoxia, fibrillation either occurred spontaneously or it was evoked by early extra stimuli. Fibrillation was reversible in all groups except for substitution 0.5 mM palmitate for glucose. Under anoxic conditions loss of excitability was observed, and shortening of AP was smaller than under palmitate. Glucose uptake was inhibited by 30% in the presence of 0.5 mM of palmitate, but not by 0.1 mM of palmitate. Thus changes in the shape of AP are not related to the glucose uptake. The possible effect of palmitate on inhibition of cellular respiration and glycolysis is discussed.

Action Potentials↗
PubMed2005

Anaerobic biodegradation of oleic and palmitic acids: evidence of mass transfer limitations caused by long chain fatty acid accumulation onto the anaerobic sludge.

Palmitic acid was the main long chain fatty acids (LCFA) that accumulated onto the anaerobic sludge when oleic acid was fed to an EGSB reactor. The conversion between oleic and palmitic acid was linked to the biological activity. When palmitic acid was fed to an EGSB reactor it represented also the main LCFA that accumulated onto the sludge. The way of palmitic acid accumulation was different in the oleic and in the palmitic acid fed reactors. When oleic acid was fed, the biomass-associated LCFA (83% as palmitic acid) were mainly adsorbed and entrapped in the sludge that became "encapsulated" by an LCFA layer. However, when palmitic acid was fed, the biomass-associated LCFA (the totality as palmitic acid) was mainly precipitated in white spots like precipitates in between the sludge, which remained "non-encapsulated." The two sludges were compared in terms of the specific methanogenic activity (SMA) in the presence of acetate, propionate, butyrate, and H(2)CO(2), before and after the mineralization of similar amounts of biomass-associated LCFA (4.6 and 5.2 g COD-LCFA/g of volatile suspended solids (VSS), for the oleic and palmitic acid fed sludge, respectively). The "non-encapsulated," sludge exhibited a considerable initial methanogenic activity on all the tested substrates, with the single exception of butyrate. However, with the "encapsulated" sludge only methane production from ethanol and H(2)/CO(2) was detected, after a lag phase of about 50 h. After mineralization of the biomass-associated LCFA, both sludges exhibited activities of similar order of magnitude in the presence of the same individual substrates and significantly higher than before. The results evidenced that LCFA accumulation onto the sludge can create a physical barrier and hinder the transfer of substrates and products, inducing a delay on the initial methane production. Whatever the mechanism, metabolic or physical, that is behind this inhibition, it is reversible, being eliminated after the depletion of the biomass-associated LCFA.

Acetates↗
PubMed2003

Palmitate acutely raises glycogen synthesis in rat soleus muscle by a mechanism that requires its metabolization (Randle cycle).

The acute effect of palmitate on glucose metabolism in rat skeletal muscle was examined. Soleus muscles from Wistar male rats were incubated in Krebs-Ringer bicarbonate buffer, for 1 h, in the absence or presence of 10 mU/ml insulin and 0, 50 or 100 microM palmitate. Palmitate increased the insulin-stimulated [(14)C]glycogen synthesis, decreased lactate production, and did not alter D-[U-(14)C]glucose decarboxylation and 2-deoxy-D-[2,6-(3)H]glucose uptake. This fatty acid decreased the conversion of pyruvate to lactate and [1-(14)C]pyruvate decarboxylation and increased (14)CO(2) produced from [2-(14)C]pyruvate. Palmitate reduced insulin-stimulated phosphorylation of insulin receptor substrate-1/2, Akt, and p44/42 mitogen-activated protein kinases. Bromopalmitate, a non-metabolizable analogue of palmitate, reduced [(14)C]glycogen synthesis. A strong correlation was found between [U-(14)C]palmitate decarboxylation and [(14)C]glycogen synthesis (r=0.99). Also, palmitate increased intracellular content of glucose 6-phosphate in the presence of insulin. These results led us to postulate that palmitate acutely potentiates insulin-stimulated glycogen synthesis by a mechanism that requires its metabolization (Randle cycle). The inhibitory effect of palmitate on insulin-stimulated protein phosphorylation might play an important role for the development of insulin resistance in conditions of chronic exposure to high levels of fatty acids.

Animals↗