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PubMed1996

Stearic acid unlike shorter-chain saturated fatty acids is poorly utilized for triacylglycerol synthesis and beta-oxidation in cultured rat hepatocytes.

Utilization of stearate as compared to various saturated fatty acids for cholesterol and lipid synthesis and beta-oxidation was determined in primary culture of rat hepatocytes. At 0.5 mmol/L in the medium, stearate (18:0) adequately solubilized by albumin was less inhibitory to cholesterol synthesis from [2-14C] acetate than myristate (14:0) and palmitate (16:0) (68% vs. 91 and 88% inhibition, respectively). The rate of incorporation into cholesterol from [1-14C] stearate (3.0 +/- 0.6 nmol/mg protein/4 h) was 37-, 1.8-, and 7.8-fold of that from myristate, palmitate, and oleate, respectively. Conversely, the rate of [1-14C] stearate incorporation into total glycerolipids was 88-90% lower than that of labeled palmitate, myristate, and oleate. The rate of [1-14C] stearate incorporation into triacylglycerol (3.6 +/- 0.4 nmol/mg protein/4 h) was 6-8% of that from myristate, palmitate, oleate, and linoleate. The rate of stearate incorporation into phospholipids was the lowest among tested fatty acids, whereas the rate of mono- and diacylglycerol synthesis was the highest with stearate treatment. The rate of beta-oxidation as measured by CO2 and acid soluble metabolite production was also the lowest with [1-14C] stearate treatment at 22.7 nmol/mg protein/4 h, which was 35-40% of those from other [1-14C] labeled fatty acids. A greater proportion of stearate than other fatty acids taken up by the hepatocytes remained free and was not metabolized. Clearly, stearate as compared to shorter-chain saturated fatty acids was less efficiently oxidized and esterified to triacylglycerol in cultured rat hepatocytes.

Animals↗
PubMed1998

Stearic acid oxidation in the Alaskan red-backed vole: effects of cold and norepinephrine.

Saturated fatty acids constitute a considerable energy reserve that could convey survival value under chronic cold exposure. It was investigated whether acclimation to cold was associated with a change in the ability of a small microtine rodent, the red-backed vole (Clethrionomys rutilis), to increase the use of saturated fatty acids during thermogenesis. The C-14 labeled stearic acid, a typical saturated fatty acid (FA), was used to determine the rate of utilization through oxidation. In warm acclimated (WA, 20 degrees C) and cold acclimated (CA, 5 degrees C) voles, acute cold exposure (WA at 5 degrees C, -2 degrees; CA at -5 degrees C) and norepinephrine (NE) injection increased metabolic rate (VO2, VCO2) and mobilization of lipid reserves. Acute cold exposure increased percent blood stearate oxidized in a linear fashion with both metabolic rate and stearate concentration in both WA and CA voles. The CA voles at 5 degrees C had increased stearate irreversible loss (1.5x) and oxidation rate (2x) compared to WA voles at 20 degrees C. The CA voles at -5 degrees C increased stearate irreversible loss and oxidation linearly with metabolic rate and blood stearate concentration. In CA voles the contribution made by stearate oxidation to VCO2, increased with the level of cold exposure and NE injection. In contrast, for WA voles stearate irreversible loss and the contribution made by stearate oxidation to VCO2 were unaffected by acute cold exposure. Thus, cold acclimation involves: (1) a modest increase (1.5x) in the use of stearate as a fuel substrate; and (2) a greater stearate oxidation and contribution to overall metabolism during acute cold exposure (-5 degrees C).

Acclimatization↗
PubMed1996

Inhibition of binding to fatty acid binding protein reduces the intracellular transport of fatty acids.

Male livers, containing lesser amounts of fatty acid binding protein (FABP), utilize fatty acids more slowly than female livers. Conventional wisdom dictates that FABP stimulates fatty acid use by increasing cytoplasmic transport rates. Previously, we showed that the cytoplasmic diffusion of a fatty acid analogue [12-N-methyl-7-nitrobenzo-2-oxa-1,3-diazol-amino stearate (NBD-stearate)] is faster in female hepatocytes, paralleling the larger amounts of FABP. Sex differences in other cytoplasmic factors could also lead to faster diffusion, independent of FABP levels. The aim of this study was to determine the effect of inhibition of fatty acid binding to FABP on the directly measured intracellular transport rate of NBD-stearate. The binding of NBD-stearate to FABP was reduced by incubating hepatocytes isolated from male and female rats with alpha-bromo-palmitate (0-1,500 microM), a modified long-chain fatty acid that binds to FABP. The inhibition by alpha-bromo-palmitate on NBD-stearate binding to FABP was measured with the use of centrifugation to separate cytosol from cytoplasmic membranes. Laser photobleaching (fluorescence recovery after photobleaching) was used to measure the cytoplasmic diffusion of NBD-stearate in hepatocytes. Alpha-Bromo-palmitate incubation reduced NBD-stearate binding to FABP in a dose-dependent manner. The measured diffusion rate was also reduced in proportion to the degree of binding inhibition. We conclude that cytoplasmic transport of NBD-stearate is modulated by binding to soluble proteins like FABP. FABP enhances diffusive transport by reducing binding to immobile cytosolic membranes.

4-Chloro-7-nitrobenzofurazan↗
PubMed2000

Possible explanation for the white band artifact seen in clinically retrieved polyethylene tibial components.

Studies have focused attention on the appearance of a subsurface white band in clinically retrieved polyethylene components and the possible contribution of this phenomenon to early polyethylene delamination. Unconsolidated polyethylene particles and oxidation have been suggested as possible reasons for the appearance of the white band. Calcium stearate and other additives used in processing ultra-high molecular weight polyethylene may also contribute to formation of the white band. A quantitative investigation was conducted on 11 retrieved tibial components that exhibited a subsurface white band to determine whether the amount of calcium stearate particles and additives were greater in the white band region when compared with the mid-portion of the same section of polyethylene. Calcium stearate particles and other additives were quantified using backscattered electron imaging with correlated elemental analysis. The particles were identified based on morphology and elemental patterns similar to reference calcium stearate particles and known additives. Significantly more (p < 0. 0001) calcium stearate particles and additives were present in the white band region (4578 +/- 418 particles/mm(2); mean +/- standard error) than the mid-portion region (1250 +/- 147 particles/mm(2)) of the sectioned tibial inserts. The percent area occupied by calcium stearate particles and additives was five times higher (p < 0.0001) within the white band region (0.81 +/- 0.10%) than the mid-portion region (0.16 +/- 0.03%). The increased presence of calcium stearate and other additives in the white band region suggests that they may play a role in the formation of the white band. In future investigations it may be important to consider how calcium stearate and other additives in polyethylene resins affect white band formation and the possible contribution to crazing, early delamination, and osteolysis in total joint replacement.

Adult↗
PubMed1993

Sex differences in intracellular fatty acid transport: role of cytoplasmic binding proteins.

Female liver clears long-chain fatty acids from plasma more rapidly than male liver, and yet the basis for this sex difference is poorly understood. We tested the hypothesis that cytosolic fatty acid binding protein (FABP), which is more concentrated in female liver, may enhance fatty acid utilization by increasing the rate of transport through the cytoplasm. We modified the technique of fluorescence recovery after laser photobleaching to measure the cytoplasmic diffusion rate of the fluorescent long-chain fatty acid 12-N-methyl-(7-nitrobenz-2-oxa-1,3-diazol)aminostearate (NBD-stearate) in cultured hepatocytes from female and male rats. NBD-stearate was used because its hepatic handling is similar to natural fatty acids. After uptake, NBD-stearate distributed uniformly in the cytoplasm but was excluded from the nucleus. Intracellular transport occurred by diffusion with no detectable convective flux. The cytoplasmic diffusion rate at 37 degrees C was 65% greater in female cells than in male cells (mean +/- SE, 5.03 +/- 0.37 vs. 3.05 +/- 0.21 x 10(-9) cm2/s respectively; P < 0.001) and was two to three orders of magnitude slower than for either unbound NBD-stearate or FABP in water. A correspondingly greater fraction of cellular NBD-stearate was found in the aqueous cytosol in females (35.1 +/- 7.0 vs. 18.2 +/- 2.7%), suggesting that FABP reduces binding of NBD-stearate to immobile cytoplasmic membranes. These data indicate that intracellular transport of NBD-stearate, a typical amphipathic molecule, is slowed by binding to cytoplasmic membranes. The primary function of soluble binding proteins such as FABP may be to enhance the diffusive fluxes of their ligands by reducing membrane binding. If cytoplasmic transport of rapidly metabolized fatty acids such as palmitate is similarly slow, substantial concentration gradients could develop within the cytoplasm of hepatocytes at steady state. By catalyzing these diffusive fluxes, FABP may regulate fatty acid metabolism.

4-Chloro-7-nitrobenzofurazan↗
PubMed1995

Confocal analysis of hepatocellular long-chain fatty acid uptake.

Transmembrane transport and cytosolic accumulation of fatty acids were investigated using confocal laser scanning microscopy (cLSM). A Zeiss LSM 310 system was used to determine the uptake of the fluorescent fatty acid derivative 12-(N-methyl)-N-[(7-nitrobenz-2-oxa-1,3- diazol-4-yl)amino]octadecanoic acid (12-NBD stearate) (C18) in single rat hepatocytes. Uptake was a saturable process with a Michaelis-Menten constant value of 68 nM. Initial uptake velocity was dependent on extracellular presence of albumin and beta-lactoglobulin. Absence of albumin reduced uptake to 32 +/- 16% (P < 0.01) of control values. In the presence of unlabeled stearate, uptake of 12-NBD stearate was lowered to 49 +/- 12% (P < 0.01). Ion substitution experiments showed no sodium dependency of uptake. Increase in membrane potential led to a pronounced accumulation of the fatty acid derivative within the plasma membrane and in the adjacent cytoplasmic compartment, whereas membrane depolarization had no effect on uptake rates. In separate experiments line scans through representative hepatocytes were analyzed to generate "x-t" plots. 12-NBD stearate showed a fluorescence pattern with prominent staining of the area of the plasma membrane and the adjacent cytoplasm, dependent on the presence of extracellular albumin. For the hepatocellular cytosolic accumulation process of 12-NBD stearate a diffusion constant of 22.2 +/- 6.2 x 10(-9) cm2/s was calculated. In contrast to the long-chain fatty acid derivative 12-NBD stearate, short (C5)- and medium (C11)-chain fatty acids revealed no membrane interaction with hepatocytes. Erythrocytes also lacked a membrane interaction process for 12-NBD stearate. In conclusion, it was demonstrated that cLSM is capable of directly evaluating the cellular fatty acid uptake process at a subcellular level.

4-Chloro-7-nitrobenzofurazan↗
PubMed1975

Variations of lipid-protein interactions in erythrocyte ghosts as a function of temperature and pH in physiological and non-physiological ranges. A study using a paramagnetic quenching of protein fluorescence by nitroxide lipid analogues.

1. Incorporation of stearic acid nitroxides into erythrocyte ghosts markedly depresses the fluorescence of membrane protein tryptophan residues. 5-Nitroxide stearate quenches fluorescence more efficiently than 16-nitroxide stearate. Both compounds exhibit dynamic (diffusion-limited) quenching above 0.28 mumol/mg protein and static quenching at lower nitroxide protein ratios. Static quenching can be attributed to high affinity binding of nitroxide stearates by membrane protein. The dynamic phase represents distribution of the stearate analogues into a fluid lipid system. 2. Protein fluorophores accessible to quenching by a cholesterol analogue, androstane nitroxide, are saturated at low nitroxide/protein ratios (less than 0.14 mumol/mg protein), without resolution of a static quenching phase. This suggests that sterols are segregated away from protein, probably in CLusters". 3. Paramagnetic quenching by stearate nitroxides increases abruptly between 35 and 50 degrees C. This discontinuous enhancement of quenching by temperature is reversible up to 41 degrees C but irreversible at higher temperatures. The discontinuity is also diminished by lowering pH from 7.3 through 6.5 to 6.0. Quenching by androstane nitroxide increases linearly with temperature up to approx. 41 degrees C and then rises exponentially. We attribute the reversible quenching thermotropism detected by stearate derivatives to reversible, thermotropic unfolding and/or depolymerisation of membrane proteins. The irreversible phase, detected also by the sterol derivative can be attributed to non-reversible protein denaturation. 4. Paramagnetic quenching of membrane tryptophan fluorescence by stearate derivatives is minimal at approx. pH 7.1 (35 degrees C) and increases sharply at lower and higher pH values, suggesting that two categories of protein residues, titrating between pH 6 and 8, profoundly influence the association of fatty acyl chains and penetrating protein segments. Quenching by androstane nitroxide exhibits no significant variation between pH 6 and 8, consistent with other data indicating that erythrocyte membrane sterols are segregated from membrane proteins, probably in clusters. 5. Our new approach confirms previous suggestions of a boundary layer of lipid in close association with some proteins in erythrocyte membranes, as well as experiments indicating that the lipid status in this boundary layer depends on that state of membrane proteins. However, sterols appear to be largely excluded from this boundary domain. Our data further show that lipid-protein interactions in erythrocyte membranes can vary significantly with fluctuations of temperature and pH in the physiological range.

Binding Sites↗
PubMed1987

The effects of cholesterol on lateral diffusion and vertical fluctuations in lipid bilayers. An electron-electron double resonance (ELDOR) study.

Electron-electron double resonance (ELDOR) and saturation-recovery spectroscopy employing 14N:15N stearic acid spin-label pairs have been used to study the effects of cholesterol on lateral diffusion and vertical fluctuations in lipid bilayers. The 14N:15N continuous wave electron-electron double resonance (CW ELDOR) theory has been developed using rate equations based on the relaxation model. The collision frequency between 14N-16 doxyl stearate and 15N-16 doxyl stearate, WHex (16:16), is indicative of lateral diffusion of the spin probes, while the collision frequency between 14N-16 doxyl stearate and 15N-5 doxyl stearate, WHex (16:5), provides information on vertical fluctuations of the 14N-16 doxyl stearate spin probe toward the membrane surface. Our results show that: (a) cholesterol decreases the electron spin-lattice relaxation time Tle of 14N-16 doxyl stearate spin label in dimyristoylphosphatidylcholine (DMPC) and egg yolk phosphatidylcholine (egg PC). (b) Cholesterol increases the biomolecular collision frequency WHex (16:16) and decreases WHex (16:5), suggesting that incorporation of cholesterol significantly orders the part of the bilayer that it occupies and disorders the interior region of the bilayer. (c) Alkyl chain unsaturation of the host lipid moderates the effect of cholesterol on both vertical fluctuations and lateral diffusion of 14N-16 doxyl stearate. And (d), there are marked differences in the effects of cholesterol on lateral diffusion and vertical fluctuations between 0-30 mol% and 30-50 mol% of cholesterol that suggest an inhomogeneous distribution of cholesterol in the membrane.

Cholesterol↗
PubMed2004

Coordination of peroxisomal beta-oxidation and fatty acid elongation in HepG2 cells.

A major product of mitochondrial and peroxisomal beta-oxidation is acetyl-CoA, which is essential for multiple cellular processes. The relative role of peroxisomal beta-oxidation of long chain fatty acids and the fate of its oxidation products are poorly understood and are the subjects of our research. In this report we describe a study of beta-oxidation of palmitate and stearate using HepG2 cells cultured in the presence of multiple concentrations of [U-(13)C(18)]stearate or [U-(13)C(16)] palmitate. Using mass isotopomer analysis we determined the enrichments of acetyl-CoA used in de novo lipogenesis (cytosolic pool), in the tricarboxylic acid cycle (glutamate pool), and in chain elongation of stearate (peroxisomal pool). Cells treated with 0.1 mm [U-(13)C(18)]stearate had markedly disparate acetyl-CoA enrichments (1.1% cytosolic, 1.1% glutamate, 10.7% peroxisomal) with increased absolute levels of C20:0, C22:0, and C24:0. However, cells treated with 0.1 mm [U-(13)C(16)]palmitate had a lower peroxisomal enrichment (1.8% cytosolic, 1.6% glutamate, and 1.1% peroxisomal). At higher fatty acid concentrations, acetyl-CoA enrichments in these compartments were proportionally increased. Chain shortening and elongation was determined using spectral analysis. Chain shortening of stearate in peroxisomes generates acetyl-CoA, which is subsequently used in the chain elongation of a second stearate molecule to form very long chain fatty acids. Chain elongation of palmitate to stearate appeared to occur in a different compartment. Our results suggest that 1) chain elongation activity is a useful and novel probe for peroxisomal beta-oxidation and 2) chain shortening contributes a substantial fraction of the acetyl-CoA used for fatty acid elongation in HepG2 cells.

Acetyl Coenzyme A↗
PubMed1990

The coating and the encapsulation of an interactive powder mixture and its application to sustained release preparations.

Fine cohesive isoprenaline HCl particles adhered to the surface of coarser potato starch particles to form interactive mixtures. These were coated with magnesium stearate by dry mixing. To check if there was a lowering of homogeneity in the latter stage, the degree of mixing was investigated before and after adding magnesium stearate. The surface appearance of magnesium stearate-coated interactive mixtures became smoother as mixing time increased or the temperature of the powder bed during mixing was raised. Ultimately, the magnesium stearate encapsulated the particles of interactive mixture. The coated interactive mixtures improved sustained release of isoprenaline HCl over the starch mixtures alone, the effect depending on the density of the magnesium stearate. Only in encapsulated mixtures was the release rate of drug decreased as the amount of magnesium stearate increased. The release of isoprenaline HCl from the interactive mixtures followed first-order kinetics. A linear relationship existed between the first-order rate constant and the reciprocal thickness of the magnesium stearate film, indicating a diffusion-controlled system with the film having some pores.

Chemistry, Pharmaceutical↗