SEARCH · PubMed Health

Results for “Acetates”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 631 records · Page 35Linked to original sources

PubMed1996

Comparison of acetate turnover in methanogenic and sulfate-reducing sediments by radiolabeling and stable isotope labeling and by use of specific inhibitors: evidence for isotopic exchange.

Acetate turnover in the methanogenic freshwater anoxic sediments of Lake Vechten, The Netherlands, and in anoxic sediments from the Tamar Estuary, United Kingdom, and the Grosser Jasmunder Bodden, Germany, the latter two dominated by sulfate reduction, was determined. Stable isotopes and radioisotopes, inhibitors (chloroform and fluoroacetate), and methane flux were used to provide independent estimates of acetate turnover. Pore water acetate pool sizes were determined by gas chromatography with a flame ionization detector, and stable isotope-labeled acetate was determined by gas chromatography-mass spectrometry. The appearance of acetates with a different isotope labeling pattern from that initially added demonstrated that isotopic exchange occurred during methanogenic acetate metabolism. The predominant exchange processes were (i) D-H exchange in the methyl group and (ii) (sup13)C-(sup12)C exchange at the carboxyl carbon. These exchanges are most probably caused by the activity of the enzyme complex carbon monoxide dehydrogenase and subsequent methyl group dehydrogenation by tetrahydromethanopterine or a related enzyme. The methyl carbon was not subject to exchange during transformation to methane, and hence acetate with the methyl carbon labeled will provide the most reliable estimate of acetate turnover to methane. Acetate turnover rate estimates with these labels were consistent with independent estimates of acetate turnover (acetate accumulation after inhibition and methane flux). Turnover rates from either radioisotope- or stable isotope-labeled methyl carbon isotopes are, however, dependent on accurate determination of the acetate pool size. The additions of large amounts of stable isotope-labeled acetate elevate the acetate pool size, stimulating acetate consumption and causing deviation from steady-state kinetics. This can, however, be overcome by the application of a non-steady-state model. Isotopic exchange in sediments dominated by sulfate reduction was minimal.

Journal Article↗

PubMed1997

Formation of DNA adducts by cyproterone acetate and some structural analogues in primary cultures of human hepatocytes.

Recently, we have shown that the therapeutically-used progestin and antiandrogen cyproterone acetate (CPA) causes the formation of high levels of DNA adducts in rat hepatocytes and rat liver [J. Topinka, U. Andrae, L.R. Schwarz, T. Wolff, Cyproterone acetate generates DNA adducts in rat liver and in primary rat hepatocyte cultures, Carcinogenesis 14 (1993) 423-427: J. Topinka, B. Binkova, L.R. Schwarz, T. Wolff, Cyproterone acetate is an integral part of hepatic DNA adducts induced by this steroidal drug, Carcinogenesis 17 (1996) 167-169; S. Werner, J. Topinka, T. Wolff, L.R. Schwarz, Accumulation and persistence of DNA adducts of the synthetic steroid cyproterone acetate in rat liver, Carcinogenesis 16 (1995) 2369-2372; J. Topinka, B. Binkova, H.K. Zhu, U. Andrae, I. Neumann, L.R. Schwarz, S. Werner, T. Wolff, DNA damaging activity of the cyproterone acetate analogues chlormadinone acetate and megestrol acetate in rat liver, Carcinogenesis 16 (1995) 1483-1487]. Its structural analogues, chlormadinone acetate (CMA) and megestrol acetate (MGA) were much less active in this respect [J. Topinka, B. Binkova, H.K. Zhu, U. Andrae, I. Neumann, L.R. Schwarz, S. Werner, T. Wolff, DNA damaging activity of the cyproterone acetate analogues chlormadinone acetate and megestrol acetate in rat liver, Carcinogenesis 16 (1995) 1483-1487]. In the present study we addressed the question whether these compounds and two further analogues, medroxyprogesterone acetate (MPA) and progesterone, induce the formation of DNA adducts in primary cultures of human hepatocytes. Incubation of CPA with human hepatocytes from two male and four female donors induced the formation of significant levels of CPA-DNA adducts detectable by 32P-postlabeling. The by far most prevalent DNA adduct is most likely identical with adduct A formed in CPA-treated rats. DNA binding was found even at 0.03 microM CPA, the lowest concentration used. The maximum effect occurred at about 10 microM in 5 of the 6 cell preparations. At this concentration 480 and 2690 adducts x 10(-9) nucleotides were detected in hepatocytes of the two male donors and 1072, 816, 613 and 659 adducts x 10(-9) nucleotides in the hepatocytes of the four female donors after an exposure of 6 h with CPA. Extending the incubation time to 20 h resulted in a roughly three-fold higher binding. CMA and MGA were assayed in two of the liver cell preparations from the female donors. At a concentration of 20 microM and an incubation time of 6 h, DNA adduct levels for CMA were 21 and 43% and for MGA 31 and 65% of the levels observed with 20 microM CPA. In contrast, DNA binding of MPA amounted to less than 1% of that observed with CPA and DNA binding of the natural occurring progestin progesterone was below the level of detection. The results point to a genotoxic risk associated with the therapeutic use of CPA and possibly of CMA and MGA. Furthermore, the findings suggest that the significant genotoxicity observed with CPA, MGA and CMA is associated with the presence of the double bond in position 6-7 of the steroid, which is absent in MPA and progesterone.

Adult↗

PubMed2004

Fatal workplace accident involving ethyl acetate: a distribution study.

The tissue distribution of ethyl acetate and ethanol in a case of acute intoxication by ethyl acetate is presented. The victim was a 39-year-old man who was found dead lying on his abdomen in the interior of a tank containing ethyl acetate. Confirmation of ethyl acetate was obtained with static headspace gas chromatography with mass spectrometry. In blood, rapid biotransformation of ethyl acetate occurs by plasma esterases resulting in acetic acid and ethanol. Quantitation of ethyl acetate and ethanol in the postmortem samples was performed using static headspace gas chromatography with flame ionization detector. N-butanol was used as internal standard. Separation of the compounds was obtained on a Supelcowaxtrade mark-10 Fused Silica capillary column. The method was linear over the specific ranges investigated and showed a within-run accuracy of 99.8 and 101.0% and a precision of 0.5 and 2.0% for ethanol and ethyl acetate, respectively. The postmortem samples were analyzed in duplicate or triplicate. Coefficients of variation were < or =4.51% for ethyl acetate and < or =0.52% for ethanol. The low ratios of the ethyl acetate concentration to the ethanol concentration found in the postmortem tissue samples confirmed the rapid in vivo biotransformation of ethyl acetate. The highest concentration of ethyl acetate was found in the testis indicating that postmortem percutane absorption may have occurred. To our knowledge, this is the first reported tissue distribution study of ethyl acetate and ethanol in a case of acute intoxication by ethyl acetate.

Accidents, Occupational↗

PubMed2006

Lipopolysaccharide plus 12-o-tetradecanoylphorbol 13-acetate induction of migration and invasion of glioma cells in vitro and in vivo: Differential inhibitory effects of flavonoids.

In an earlier study, we reported that nitric oxide is involved in lipopolysaccharide plus 12-o-tetradecanoylphorbol 13-acetate-induced malignant transformation via increases in metalloproteinase 9 enzyme activity and inducible nitric oxide synthase gene expression in rat glioma C6 cells, however the mechanism has remained undefined. Lipopolysaccharide plus 12-o-tetradecanoylphorbol 13-acetate, but not lipopolysaccharide or 12-o-tetradecanoylphorbol 13-acetate alone, induced transformation in glioma C6 cells (but not in human glioblastoma cells GBM-8401 cells) without affecting their viability. An increase in inducible nitric oxide synthase protein expression, nitric oxide production, and metalloproteinase 9 enzyme activity is identified lipopolysaccharide/12-o-tetradecanoylphorbol 13-acetate-treated C6 cells, however lipopolysaccharide/12-o-tetradecanoylphorbol 13-acetate and 12-o-tetradecanoylphorbol 13-acetate (but not lipopolysaccharide) addition shows the similar inductive pattern on metalloproteinase 9 enzyme activity without affecting inducible nitric oxide synthase protein expression and nitric oxide production in GBM-8401 cells. Treatment of C6 cells with lipopolysaccharide/12-o-tetradecanoylphorbol 13-acetate increases the expression of phosphorylated extracellular regulated protein kinases and Jun N-terminal kinases, but not p38, proteins, and an addition of the extracellular regulated protein kinases inhibitor PD98059 or Jun N-terminal kinases inhibitors SP600125, but not the p38 inhibitor SB203580, significantly blocked lipopolysaccharide/12-o-tetradecanoylphorbol 13-acetate-induced inducible nitric oxide synthase protein expression and metalloproteinase 9 enzyme activity accompanied by blocking morphological transformation in C6 cells. Among 19 structurally related flavonoids, kaempferol and wogonin exhibit significant inhibitory effects on lipopolysaccharide/12-o-tetradecanoylphorbol 13-acetate-induced morphological transformation and colony formation, and attenuation of inducible nitric oxide synthase, phosphorylated extracellular regulated protein kinases protein expression, and metalloproteinase 9 enzyme activity was observed. 2'-OH flavone at a dose of 100 microM inhibition of lipopolysaccharide/12-o-tetradecanoylphorbol 13-acetate-induced events via apoptosis induction is identified. Furthermore, lipopolysaccharide/12-o-tetradecanoylphorbol 13-acetate, but not lipopolysaccharide or 12-o-tetradecanoylphorbol 13-acetate, induces tumoral invasion and migration in vitro and in vivo, and those are blocked by kaempferol and wogonin addition. These data suggest that combination of lipopolysaccharide and 12-o-tetradecanoylphorbol 13-acetate promotes tumoral progression via activating metalloproteinase 9 enzyme activity and inducible nitric oxide synthase gene expression, which is located downstream of mitogen-activated protein kinases activation, in rat glioma cells C6. Kaempferol and wogonin exhibit effective inhibitory effects on lipopolysaccharide/12-o-tetradecanoylphorbol 13-acetate-induced events, and thus possess the potential for further development.

Animals↗

PubMed2001

Influence of acetate and CO2 on the TMAO-reduction reaction by Shewanella baltica.

In this work, the TMAO-reduction by Shewanella baltica, one of the representative spoilage organisms in modified atmosphere packaged marine fish fillets, and the effect of acetate and CO2 on this reduction were studied in vitro. The growth of S. baltica and the corresponding evolution of some compounds (acetate, lactate, pyruvate, glucose and trimethylamine (TMA)) were followed during storage at 4 degrees C in two types of broths. The first medium was a defined medium (pH = 6.8) to which lactate or pyruvate was added as hydrogen donor. Pyruvate showed to be more efficient as H-donor for S. baltica than lactate, as growth was much faster when equimolar amounts of pyruvate instead of lactate were present. Although the growth of S. baltica, when pyruvate is used as H-donor and no acetate is added, was not much inhibited by the CO2-atmosphere, CO2 had a pronounced effect on the studied reactions as it partly inhibited the reduction of pyruvate to acetate. The effect of acetate on this reaction was, on the other hand, not significant. To simulate the reactions occurring in situ, a buffered fish extract (pH = 6.8) was used. In spite of the neutral pH, the growth of S. baltica in this medium was highly inhibited by relatively small concentrations of acetate (< 0.3%). When 0.1% of acetate was added to the fish extract, less acetate was formed and lactate was more slowly consumed in comparison to the experiments without the addition of acetate. The consumption of lactate and the production of acetate were almost completely inhibited when the fish extract contained 0.25% of acetate. Apparently, the addition of acetate inhibited the use of lactate as H-donor. After extended storage times (17 days at 4 degrees C) TMA production started. Most probably, alternative H-donors were used by S. baltica, from which the pathway seems to be less energy efficient. This can be deduced from the exceptional growth inhibition of S. baltica by small amounts of acetate. However, when practical storage times for fish (e.g. 6 days at 4 degrees C after packaging) are considered, growth and TMAO-reduction by S. baltica was completely inhibited during this period by 0.25% of acetate.

Acetates↗

PubMed1978

Growth and methanogenesis by Methanosarcina strain 227 on acetate and methanol.

Methanosarcina strain 227 exhibited exponential growth on sodium acetate in the absence of added H(2). Under these conditions, rates of methanogenesis were limited by concentrations of acetate below 0.05 M. One mole of methane was formed per mole of acetate consumed. Additional evidence from radioactive labeling studies indicated that sufficient energy for growth was obtained by the decarboxylation of acetate. Diauxic growth and sequential methanogenesis from methanol followed by acetate occurred in the presence of mixtures of methanol and acetate. Detailed studies showed that methanol-grown cells did not metabolize acetate in the presence of methanol, although acetate-grown cells did metabolize methanol and acetate simultaneously before shifting to methanol. Acetate catabolism appeared to be regulated in response to the presence of better metabolizable substrates such as methanol or H(2)-CO(2) by a mechanism resembling catabolite repression. Inhibition of methanogenesis from acetate by 2-bromoethanesulfonate, an analog of coenzyme M, was reversed by addition of coenzyme M. Labeling studies also showed that methanol may lie on the acetate pathway. These results suggested that methanogenesis from acetate, methanol, and H(2)-CO(2) may have some steps in common, as originally proposed by Barker. Studies with various inhibitors, together with molar growth yield data, suggest a role for electron transport mechanisms in energy metabolism during methanogenesis from methanol, acetate, and H(2)-CO(2).

Acetates↗

PubMed1997

Acetate intolerance is mediated by enhanced synthesis of nitric oxide by endothelial cells.

The clinical picture of acetate intolerance strictly mimics the nitric oxide (NO) effect, including smooth muscle relaxation and extreme vasodilation. Because acetate induces production of cAMP, which is a powerful stimulus of NO synthase (NOS), we evaluated the effect of different dialysate solutions with and without acetate on NOS activity in endothelial cells (EC). NOS activity of EC, evaluated as H3-citrulline produced from H3-arginine, was modulated by the dialysate composition (e.g., 38 mmol/L acetate produced an increase of 3.2 +/- 0.39-fold compared with basal values (P < 0.0005), and the small amount of acetate (4 mmol/L) in 35 mmol/L bicarbonate solution increased the NOS activity by 2 +/- 0.49-fold (P < 0.05). Conversely, the acetate-free solution produced no effect on NOS activity. The mRNA encoding for inducible NOS was highly expressed in EC incubated with acetate buffer and also with acetate in bicarbonate dialysis buffer. The EC proliferative index was depressed by acetate (P < 0.0005), and tumor necrosis factor synthesis was increased (P < 0.0005) compared with acetate-free buffer. This study suggests that dialytic "acetate intolerance" can be induced by the activation, through cAMP and tumor necrosis factor release, of NOS. The small amount of acetate in bicarbonate dialysate, although capable of inducing in vitro NOS activation, is likely to be rapidly metabolized, whereas the large amounts of this anion in acetate fluids overwhelm metabolism by the liver. Acetate-free dialysate is the only solution that provides an acceptable level of biocompatibility both in vivo and in vitro.

Acetates↗

PubMed1983

Linalyl Acetate Is Metabolized by Pseudomonas incognita with the Acetoxy Group Intact.

Metabolism of linalyl acetate by Pseudomonas incognita isolated by enrichment culture on the acyclic monoterpene alcohol linalool was studied. Biodegradation of linalyl acetate by this strain resulted in the formation of linalool, linalool-8-carboxylic acid, oleuropeic acid, and Delta-4-acetoxy-4-methyl hexenoic acid. Cells adapted to linalyl acetate metabolized linalyl acetate-8-aldehyde to linalool-8-carboxylic acid, linalyl acetate-8-carboxylic acid, Delta-4-acetoxy-4-methyl hexenoic acid, and geraniol-8-carboxylic acid. Resting cell suspensions previously grown with linalyl acetate oxidized linalyl acetate-8-aldehyde to linalyl acetate-8-carboxylic acid, Delta-4-acetoxy-4-methyl hexenoic acid, and pyruvic acid. The crude cell-free extract (10,000 g of supernatant), obtained from the sonicate of linalyl acetate-grown cells, was shown to contain enzyme systems responsible for the formation of linalyl acetate-8-carboxylic acid and linalool-8-carboxylic acid from linalyl acetate. The same supernatant contained NAD-linked alcohol and aldehyde dehydrogenases involved in the formation of linalyl acetate-8-aldehyde and linalyl acetate-8-carboxylic acid, respectively. On the basis of various metabolites isolated from the culture medium, resting cell experiments, growth and manometric studies carried out with the isolated metabolites as well as related synthetic analogs, and the preliminary enzymatic studies performed with the cell-free extract, a probable pathway for the microbial degradation of linalyl acetate with the acetoxy group intact is suggested.

Journal Article↗

PubMed1997

Evidence to suggest that extracellular acetate is accumulated by rat hippocampal cholinergic nerve terminals for acetylcholine formation and release.

It is well established that extracellular choline is transported into central cholinergic nerve terminals by 'high' and 'low' affinity processes to form the neurotransmitter acetylcholine (ACh). The intent of the present investigation was to ascertain whether extracellular acetate might also be transported into central cholinergic nerve terminals to form ACh. To test this possibility, rat hippocampal tissue was incubated with varying concentrations of extracellular [1-(14)C]acetate (0.1-100 microM) and the uptake of [1-(14)C]acetate and the amount of [14C]ACh formed by the tissue determined. The results indicated that the uptake of extracellular [1-(14)C]acetate was temperature-dependent and saturable having an apparent Michaelis constant (Km) of 22 microM. The formation of [14C]ACh in the tissue as a function of extracellular [1-(14)C]acetate appeared to occur by both 'high' and 'low' affinity processes with apparent Km values of 0.5 and 19.6 microM, respectively. In other experiments, three inhibitors (lithium, allicin and sodium) of acetyl CoA synthetase (EC 6.2.1.1 acetate: CoA ligase), the enzyme which converts acetate to acetyl CoA when ATP and CoA are present, inhibited [1-(14)C]acetate uptake and the amount of [14C]ACh formed from that [1-(14)C]acetate. Additionally, vesamicol, an inhibitor of ACh transport into synaptic vesicles, blocked the filling of a synaptic vesicle-enriched fraction of hippocampal tissue with newly synthesized [14C]ACh formed from extracellular [1-(14)C]acetate. High K+ depolarization of hippocampal tissue loaded with extracellular [1-(14)C]acetate not only increased the synthesis but also the release of [14C]ACh. These results suggest that extracellular acetate is recycled by rat hippocampal cholinergic nerve terminals for the formation and release of ACh. They also suggest that the enzyme acetyl CoA synthetase mediates extracellular acetate uptake into hippocampal cholinergic nerve terminals by metabolizing it to acetyl CoA and thereby creating a diffusion gradient for it to follow.

Acetate-CoA Ligase↗

PubMed2006

Transport of acetate and sodium in sheep omasum: mutual, but asymmetric interactions.

We have studied the transport of acetate across the isolated epithelium of sheep omasum; no net transport was observed (J(ms) approximately = J(sm)) under Ussing chamber conditions. Low mucosal pH (pH 6.4) significantly enhanced J(ms) acetate and the transport rates of acetate increased linearly and significantly (r2=0.99) with the luminal acetate concentration. The presence of another short chain fatty acid (propionate) did not affect J(ms) acetate significantly. Neither addition of 1 mmol l(-1) DIDS to the mucosal side nor HCO3 replacement caused changes of J(ms) acetate; this does not support the assumption of acetate transport via anion exchange. Addition of 1 mmol l(-1) amiloride to the mucosal side significantly decreased acetate fluxes at high mucosal acetate concentration (100 mmol l(-1)) and low pH (6.4) indicating interaction between acetate uptake in the undissociated form, intracellular release of protons and activation of Na+/H+ exchange (NHE). However, the mutual interaction between Na transport via NHE and acetate transport is asymmetric. Stimulation or inhibition of Na transport via NHE is much more pronounced than the corresponding changes of acetate fluxes. Thus, the obtained results support the conclusion that acetate is transported via simple diffusion and probably predominantly in the protonated form, thereby explaining the positive and mutual interaction between Na transport and short chain fatty acids.

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid↗

PubMed1966

Transport and metabolism of acetate in rat brain cortex in vitro.

1. [1-(14)C]Acetate undergoes metabolism when incubated aerobically at 37 degrees in the presence of rat brain-cortex slices, forming (14)CO(2) and (14)C-labelled amino acids (glutamate, glutamine, aspartate and relatively small quantities of gamma-aminobutyrate). In the absence of glucose the yield of (14)C-labelled aspartate exceeds that of (14)C-labelled glutamate and glutamine. The addition of glucose brings about a doubling of the rate of formation of (14)CO(2) and a greatly increased yield of (14)C-labelled glutamate or glutamine, whereas that of (14)C-labelled aspartate is diminished. 2. The addition of potassium chloride (100mm) to the incubation medium causes an increased rate of (14)CO(2) formation in the presence or absence of glucose and an increased rate of utilization of acetate. 3. The addition of 2,4-dinitrophenol (0.1mm) suppresses the rate of utilization of [1-(14)C]acetate. 4. The presence of ouabain (10mum) suppresses the rate of formation of (14)CO(2) from [1-(14)C]acetate and the rate of acetate utilization. Acetate conversion into carbon dioxide in the rat brain cortex is both Na(+)- and K(+)-dependent and controlled by operation of the active sodium-transport process. Only the Na(+)-stimulated rate is suppressed by ouabain. 5. Sodium fluoroacetate (1mm) decreases the rate of (14)CO(2) evolution from [1-(14)C]acetate in the presence of rat brain cortex without affecting the respiratory rate. The results are consistent with the conclusion that fluoroacetate competes with, or blocks, a transport carrier for acetate, so that in its presence only the passive diffusion rate of acetate takes place. 6. The presence of sodium propionate or sodium butyrate suppresses the utilization of [1-(14)C]acetate in rat brain cortex and leads to a concentration ratio (tissue/medium) of [1-(14)C]-acetate greater than unity. 7. The presence of NH(4) (+) diminishes acetate utilization, this being attributed to a diminished ATP concentration. Glycine is also inhibitory. It is concluded that acetate transport into the brain is carrier-mediated and dependent on the operation of the sodium pump.

Acetates↗

PubMed1974

Production and utilization of acetate in mammals.

1. In an attempt to define the importance of acetate as a metabolic precursor, the activities of acetyl-CoA synthetase (EC 6.2.1.1) and acetyl-CoA hydrolase (Ec 3.1.2.1) were assayed in tissues from rats and sheep. In addition, the concentrations of acetate in blood and liver were measured, as well as the rates of acetate production by tissue slices and mitochondrial fractions of these tissues. 2. Acetyl-CoA synthetase occurs at high activities in heart and kidney cortex of both species as well as in rat liver and the sheep masseter muscle. The enzyme is mostly in the cytosol fraction of liver, whereas it is associated with the mitochondrial fraction in heart tissue. Both mitochondrial and cytosol activities have a K(m) for acetate of 0.3mm. Acetyl-CoA synthetase activity in liver was not altered by changes in diet, age or alloxan-diabetes. 3. Acetyl-CoA hydrolase is widely distributed in rat and sheep tissues, the highest activity being found in liver. Essentially all of the activity in liver and heart is localized in the mitochondrial fraction. Hepatic acetyl-CoA hydrolase activity is increased by starvation in rats and sheep and during the suckling period in young rats. 4. The concentrations of acetate in blood are decreased by starvation and increased by alloxan-diabetes in both species. The uptake of acetate by the sheep hind limb is proportional to the arterial concentration of acetate, except in alloxan-treated animals, where uptake is impaired. 5. Acetate is produced by liver and heart slices and also by heart mitochondrial fractions that are incubated with either pyruvate or palmitoyl-(-)-carnitine. Liver mitochondrial fractions do not form acetate from either substrate but instead convert acetate into acetoacetate. 6. We propose that acetate in the blood of rats or starved sheep is derived from the hydrolysis of acetyl-CoA. Release of acetate from tissues would occur under conditions when the function of the tricarboxylic acid cycle is restricted, so that the circulating acetate serves to redistribute oxidizable substrate throughout the body. This function is analogous to that served by ketone bodies.

Acetates↗

PubMed1981

Acetate supply and utilization by the tissues of sheep in vivo.

1. The supply and utilisation of acetate has been estimated simultaneously in the whole animal and tissues of sheep using a combination is isotope-dilution and arteriovenous-difference techniques. Animals were made alloxani-diabetic and acetate metabolism was compared when stabilized to normal metabolite levels with insulin (ITA sheep) and when food and insulin had been withdrawn for 36 h (fasted, diabetic sheep). 2. Acetate was simultaneously produced and utilized by all tissues. The exogenous (or gut) supply of acetate was the most important determinant of circulating acetate level. Endogenous acetate was produced mainly in the liver; 77 and 94% in fasted, diabetic and ITA sheep respectively. The production of endogenous acetate remained fairly constant and was not related to ketogenesis, which supports the idea that circulating acetate is largely a produce of fermentation. The liver, gut and muscle utilized 17, 25 and 54% respectively (96% total) of the acetate entry rate in ITA sheep; a similar percentage utilization was found in fasted, diabetic sheep. 3. Acetate is largely oxidized to carbon dioxide in the gut and muscles of sheep and may account for 30-40% of their oxidative metabolism. This figure is similar to that for the whole animal. The total acetate taken up by the liver could account for 30% of the oxygen consumption; however, the liver may not directly oxidize all the utilized acetate. 4. The over-all conclusion from this study is that acetate is largely of dietary origin and the major factor determining its rate of utilization is the arterial concentration.

Acetates↗

PubMed1988

Depressant effect of acetate in isolated cardiac tissue.

Because acetate may have cardiodepressant properties in vitro, but previous studies have not separated out effects of acetate from possible effects of osmolality, sodium concentration, or calcium complexing, the effects of isosmotic acetate substitution (at a constant calcium concentration) on contractility were studied in isolated rat atrial tissue and in an isolated perfused non-working whole heart preparation. In spontaneously contracting right atrial tissue acetate induced dose dependent inhibition of isometric tension in the clinically important dose range of 4 to 16 mmol.litre-1. Bath acetate concentrations of 4, 16, or 64 mmol.litre-1 reduced peak tension (mean(SEM] to 78(2.7)%, 56(2.5)%, or 61(4.6)% respectively of control values. Because the calcium concentrations of the acetate baths were set equal to that of the control bath, calcium complexing by acetate could not have accounted for acetate's cardiodepressant effect. The inhibitory action was demonstrable with both isosmotic and hyperosmotic acetate solutions. Acetate had no effect on the spontaneous rate of atrial contraction. Inhibition of contractility (+dP/dt) by acetate in the whole heart preparation was also demonstrable at bath acetate concentrations of 8 and 16 mmol.litre-1. The results suggest that acetate has a myocardial depressant effect in vitro at concentrations achievable in the plasma during haemodialysis. The myocardial depressant action is not dependent on calcium complexing or on changes in bath osmolality or sodium concentration.

Acetates↗

PubMed2006

On-line haemodiafiltration with and without acetate.

BACKGROUND: In patients on on-line convective treatments, given the considerable quantity of dialysis fluid re-infused, the small amount of acetate present in bicarbonate dialysis fluid as a pH stabilizing factor may allow a significant transfer of that anion to the patient, possibly inducing cytokine activation. METHODS: To verify this hypothesis, we performed on-line haemodiafiltration (OL-HDF) with (3 mmol/l) and without acetate in dialysis fluid in a cross-over randomized order on 12 prevalent patients. RESULTS: In comparison with the pre-treatment values, plasma acetate levels were unchanged during and after acetate-free OL-HDF, while they were 5-6 times higher in the course of OL-HDF containing acetate in dialysis fluid; plasma acetate levels returned to basal values 2 h after the end of the procedure. The total increase of bases in the patient attributable to acetate was 36%. Plasma bicarbonate values at the end of treatment were significantly lower in treatments without acetate, as compared to those with acetate. Interleukin-6 plasma levels were super-imposable at the beginning and in the course of the two methods compared, but there was a tendency towards a greater increase at an interval of 2 h following OL-HDF with acetate. CONCLUSIONS: Our preliminary results confirm the assumption that body gain of acetate is particularly high in convective treatments, while acetate-free OL-HDF slows down acetate burden. Clinical advantages due to these effects should be evaluated in properly designed prospective studies.

Acetates↗

PubMed1968

Acetate assimilation by Nitrobacter agilis in relation to its "obligate autotrophy".

Acetate (1 to 10 mm) had no effect on the rate of nitrite oxidation or exponential growth by Nitrobacter agilis. However, acetate-1-(14)C and -2-(14)C were both assimilated by growing cultures, and acetate carbon contributed 33 to 39% of newly synthesized cell carbon. Carbon from acetate was incorporated into all of the major cell constituents, including most of the amino acids of cell protein and poly-beta-hydroxybutyrate (PHB). Cultures grown in the presence of acetate showed a significant increase in turbidity, attributable in part to protein synthesis and the accumulation of PHB in the "post-exponential phase," when the supply of nitrite was completely exhausted. Cell suspensons of N. agilis assimilated acetate in the absence of bicarbonate and even in the absence of nitrite. However, the addition of nitrite increased the rate of acetate assimilation by cell suspensions. The distribution of (14)C-acetate incorporated by cell suspensions was qualitatively similar to that found with growing cultures. Cell suspensions of N. agilis slowly oxidized acetate to CO(2). Addition of nitrite suppressed CO(2) production from acetate but increased the assimilation of acetate carbon into cell material. N. agilis contained all the enzymes of the tricarboxylic acid cycle. Growth of N. agilis in the presence of acetate did not significantly affect the levels of the enzymes of the tricarboxylic acid cycle, but did result in a 100-fold increase in the specific activity of isocitratase. In contrast, carboxydismutase was partially repressed. N. agilis was grown heterotrophically through seven transfers on a medium containing acetate and casein hydrolysate. The addition of nitrite increased the rate of heterotrophic growth. Heterotrophically grown organisms still retained their ability to grow autotrophically with nitrite. However, these organisms oxidized nitrite at a slower rate. Organisms from autotrophic and heterotrophic cultures were analyzed to determine the mean guanine plus cytosine content of their deoxyribonucleic acid; in both cases this mean was 61.2 +/- 1%. We concluded that N. agilis is not an obligate autotroph; it appears to be a facultative autotroph which resembles the novel facultative autotroph, Thiobacillus intermedius, very closely.

Acetates↗

PubMed1996

Anastrozole, a potent and selective aromatase inhibitor, versus megestrol acetate in postmenopausal women with advanced breast cancer: results of overview analysis of two phase III trials. Arimidex Study Group.

PURPOSE: To compare the efficacy and tolerability of anastrozole (1 and 10 mg once daily), a selective, oral, nonsteroidal aromatase inhibitor, and megestrol acetate (40 mg four times daily), in postmenopausal women who progressed following tamoxifen treatment. PATIENTS AND METHODS: Two randomized, double-blind for anastrozole, open-label for megestrol acetate, parallel-group, multicenter trials were conducted in 764 patients. Because both trials were identical in design, an analysis of the combined results was performed to strengthen interpretation of results from each trial. RESULTS: The median follow-up duration was approximately 6 months. The estimated progression hazards ratios were 0.97 (97.5% confidence interval [CI], 0.75 to 1.24) for anastrozole 1 mg versus megestrol acetate and 0.92 (97.5% CI, 0.71 to 1.19) for anastrozole 10 mg versus megestrol acetate. The overall median time to progression was approximately 21 weeks. Approximately one third of patients in each group benefited from treatment. Twenty-seven patients (10.3%) in the anastrozole 1-mg group, 22 (8.9%) in the anastrozole 10-mg group, and 20 (7.9%) in the megestrol acetate group had a complete or partial response, and 66 (25.1%), 56 (22.6%), and 66 (26.1%) patients, respectively, had stable disease for > or = 24 weeks. For all end points, individual trial results were similar to the results of the combined analysis. Anastrozole and megestrol acetate were well tolerated. Gastrointestinal disturbance was more common among patients in the anastrozole groups than the megestrol acetate group; the difference between the anastrozole 10 mg and megestrol acetate groups was significant (P = .005). Significantly fewer patients in the anastrozole 1-mg (P < .0001) and 10-mg (P < .002) groups had weight gain than in the megestrol acetate group. More than 30% of megestrol acetate-treated patients had weight gain > or = 5%, and 10% of patients had weight gain > or = 10%. Patients who received megestrol acetate continued to gain weight over time. CONCLUSION: Anastrozole, 1 and 10 mg once daily, is well tolerated and as effective as megestrol acetate in the treatment of postmenopausal women with advanced breast cancer who progressed following tamoxifen treatment. Moreover, anastrozole therapy avoids the weight gain associated with megestrol acetate treatment.

Adult↗

PubMed2001

Rumen microbial sequestration of [2-(13)C]acetate in cattle.

To investigate the impact of rumen microbial sequestration of VFA carbon on estimates of acetate availability based on intraruminal infusion of [2-(13)C] acetate, three nonlactating or low-yielding dairy cows were continuously intraruminally infused with [2-(13)C]acetate for 26 h. The 13C content of ruminal VFA, duodenal carbon, and fatty acids (FA) and AA isolated from liquid-associated ruminal microbes and duodenal DM was measured by an isotope ratio mass spectrometer interfaced to an elemental analyzer or a gas-liquid chromatograph. The ruminal gross production of acetate was 38 +/- 4 mol/d and could account for about 38% of the DE intake. Of the intraruminally infused 13C in [2-(13)C]acetate, 7.6 +/- 0.9% was recovered at the duodenum. The 13C content of ruminal propionate, butyrate, and valerate increased (P < 0.05) with intraruminal infusion of [2-(13)C]acetate. It was estimated that about 28% of the 13C intraruminally infused in [2-(13)C]acetate could be accounted for by duodenal 13C flow and absorption of non-acetate VFA. A number of FA isolated from liquid-associated ruminal microbes (C6, C12, C14, anteiso C15, and iso C15) were enriched with 13C (P < 0.05) at a level comparable to the enrichment of ruminal butyrate. Any absorption of these FA from the rumen would further contribute to non-acetate 13C uptake. A maximum of 72% of the ruminal gross production of acetate represented acetate absorption from the rumen in the present study. Consequently, previously used models using intraruminal isotope dilution techniques seem not to be appropriate for measuring acetate availability in ruminants. The number of metabolites exchanging carbon with acetate was found to be so high that assessments of the entire range of inter conversions seem to be practically impossible. Portal absorption studies are discussed as an alternative method of estimating VFA availability to the metabolism in ruminants.

Acetates↗