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At least 937 records · Page 52Linked to original sources
PubMed2002

[The effects of butyrates and non-steroidal anti-inflammatory agents on HT-29 colonic carcinoma cells].

OBJECTIVE: Adenocarcinoma cells HT-29 were used to investigate whether butyrates and non-steroidal anti-inflammatory agents (NSAIDs, aspirin and NS-398) would be effective adjuvants for inducing apoptosis and to probe its possible mechanisms. METHODS: Prostaglandin E(2) (PGE(2)) isolated from HT-29 cell culture supernants was investigated with ELISA. Flow cytometry was used for estimating apoptosis. The morphology of apoptotic cells was investigated by means of electron microscopy. RESULTS: Butyrates could stimulate the secretion of PGE(2). In contrast, NSAIDs inhibited it to a level below 30 ng/L. Both butyrates and NSAIDs could induce apoptosis. The effects showed the obvious tendency of time- and concentration-dependency (P < 0.05). Combination with two drugs could enhance the above effects. CONCLUSIONS: Butyrates and NSAIDs could induce apoptosis individually. Combination with the two drugs could enhance the above effects by down-regulating cyclooxygenase-2 expression.

Adenocarcinoma↗
PubMed2002

Response of HT29 cells to butyrate depends on time of exposure and glucose deprivation.

The high level of alkaline phosphatase activity in HT29 cells induced after 2 or 5 days of butyrate treatment was decreased during their prolonged exposure (about 30 days) to this agent together with a decrease of sensitivity to apoptosis. However, an enormous additive effect on alkaline phosphatase activity was found after butyrate treatment of glucose-starved cells. In concert with this finding, the substructural analysis revealed a dense brush border, tendency to polarization and morphologically normal mitochondria. It can be concluded that prolonged butyrate treatment of HT29 cells attenuated their response to this agent. On the other hand, glucose deprivation, as another inductor of differentiation, was found to increase the sensitivity of HT29 cells to butyrate.

Butyrates↗
PubMedDate not supplied

[Comparative assessment of the diagnostic capacities of PET with 18FDG and 1-[11C] sodium butyrate in the examination of patients with tumors of the brain and cerebral circulatory disorders: results of semiquantitative assessment].

The purpose of the present study was to determine the capacities of differential diagnosis of the bulky masses of the brain by positron emission tomography (PET) with 11C-butyrate by the direct indication--the tumor RFP level measured by means of the semiquantitative indicator--the differential accumulation coefficient (DAC). For comparison, 18FDG PET widely used to detect malignant tumors was preliminarily made. Brain PET was performed in 86 patients (45 males and 41 females whose age ranged from 18 to 69 years to identify bulky masses or to rule out continuous tumor growth. In all cases, the data were histologically and morphologically verified. Of the 86 patients, 21 were found to have malignant tumors, 41 had benign tumors, arteriovenous malformations, cerebral circulatory disorders, and cysts were detected in 3, 7, and 14 cases, respectively. The level of 18FDG accumulation was ascertained to be directly related to the grade of malignancy. In 20 of the 21 patients with malignant tumors, DAC for 18FDG was greater than 1. However, it was impossible to differentiate benign tumors and non-tumoral masses by using only 18FDG. Comparing the data obtained by means of 18FDG and 11C-butyrate revealed their comparability in detecting neoplasms. Patients with vascular tumors (benign meningioma and adenoma of the pituitary were an exception. Their DAC for 11C-butyrate was greater than 1. In follow-up CT scanning, just a single injection of 11C-butyrate may allow one to estimate the vascular and tissue components of masses, which facilitates the identification of vascular non-tumoral processes and tumors. The additional criterion that allows a neoplasm to be differentiated from nontumoral processes permits a rapid tumor release of a radioactive label.

Adolescent↗
PubMed2003

Butyrates, as a single drug, induce histone acetylation and granulocytic maturation: possible selectivity on core binding factor-acute myeloid leukemia blasts.

Acute myeloid leukemia (AML) is a disease characterized by a block of maturation. Genes coding for core binding factors are rearranged in a considerable subset of AML cases and result in an altered interaction of core binding factor (CBF) subunits with transcriptional coregulators (NCoR/SMRT). Recruitment of histone deacetylase is also altered in AML, and a subsequent transcriptional repression of target genes involved in myeloid maturation is determined. We determined here the effects of two histone deacetylase inhibitors, sodium butyrate and the stable prodrug xylitol butyrate derivative (D1), on a t(8;21)-positive cell line (Kasumi-1) as well as primary AML blasts. Exposure (24-96 h) to butyrates (1 mM) of Kasumi-1 cells induced histone H4 acetylation, whereas H3 acetylation was unchanged. Induction of morphological and immunophenotypic granulocytic maturation (96 h), also confirmed by an increased expression of CAAT/enhancer binding protein alpha, was observed. Inhibition of proliferation and apoptosis via activation of caspase-9 was also observed. In primary AML blasts, butyrates (0.5 mM) increased histone H4 acetylation of 18 of 19 cases tested. Terminal granulocytic maturation was observed in all cases (5 of 5) characterized by chromosomal translocations involving CBF, whereas in non-CBF cases, maturation was incomplete (4 of 8) or absent (4 of 8). Our data indicate the possibility to effectively remove, in CBF AML cases, the maturation block generated by histone deacetylase stable recruitment, contributing to a possible development of molecularly targeted therapies of AML.

Acetylation↗
PubMed2004

Potentiated antitumor effects of a combination therapy with a farnesyltransferase inhibitor L-744,832 and butyrate in vitro.

Farnesyltransferase inhibitors, butyrate and butyric acid derivatives have previously been reported to exert anti-tumor activity in experimental models in vitro and in vivo and have recently gained acceptance as potential anticancer agents. In our study, we examined antitumor effects of a combination of a farnesyltransferase inhibitor L-744,832 and butyrate in vitro against MDA-MB-231 and MIA PaCa-2 human cancer cells. This combination therapy showed synergistic antitumor activity against MDA-MB-231 cells, which was at least in part due to induction of p27KIP1 expression. Both drugs increased intracellular levels of p53 as well but there was no significant difference between the groups treated with single drugs and the group treated with their combination. In MIA PaCa-2 cells, the combination therapy exerted additive antitumor activity. Our results illustrate possible application of the farnesyltransferase inhibitor L-744,832 and butyrate as a combination therapy of cancer.

Alkyl and Aryl Transferases↗
PubMed2004

Conversion regular patterns of acetic acid, propionic acid and butyric acid in UASB reactor.

On the basis of continuous tests and batch tests, conversion regular patterns of acetate, propionate and butyrate in activated sludge at different heights of the UASB reactor were conducted. Results indicated that the conversion capacity of the microbe is decided by the substrate characteristic when sole VFA is used as the only substrate. But when mixed substrates are used, the conversion regulations would have changed accordingly. Relationships of different substrates vary according to their locations. In the whole reactor, propionate's conversion is restrained by acetate and butyrate of high concentration. On the top and at the bottom of the reactor, conversion of acetate, but butyrate, is restrained by propionate. And in the midst, acetate's conversion is accelerated by propionate while that of butyrate is restrained. It is proved, based on the analysis of specific conversion rate, that the space distribution of the microbe is the main factor that affects substrates' conversion. The ethanol-type fermentation of the acidogenic-phase is the optimal acid-type fermentation for the two-phase anaerobic process.

Acetic Acid↗
PubMed1999

Ileal effluent as a fermentation substrate: implications for butyrate production in the colon.

Fermentation of fiber can lead to an enhanced production of short chain fatty acids (SCFA) and, hence, contribute to the proposed anticarcinogenic properties of butyrate in the colon. The fermentation of fiber isolates and the corresponding ileal effluents has been compared under in vitro conditions. Yield of SCFA per gram of substrate fermented was similar for isolates and fiber-enriched effluents (approximately 4.9 mmol/g) and it could be inferred that nonfiber components of effluent also generated SCFA. Butyrate production was highest for glucan-based polymers (approximately 30% total SCFA) and, from the measured acidogenic profile, production of SCFA will occur mainly in the proximal colon. The buffering capacity of ileal effluents during fermentation restrict the potential for a reduction in pH during acidogenesis compared to fiber isolates. This buffering capacity could limit the bioavailability of butyrate in the colon and, hence, the ability to satisfy the proposed antineoplastic properties of butyrate in the colon.

Anticarcinogenic Agents↗
PubMed2005

Modulation of sensitivity to doxorubicin by the histone deacetylase inhibitor sodium butyrate in breast cancer cells.

The histone deacetylase inhibitor sodium butyrate induces several gene products that modify cellular metabolism. Here, we investigated its ability to modulate glutathione-related detoxification enzymes in the breast cancer cell line MCF-7 and a derivative resistant to vincristine (VCREMS). We found that sodium butyrate induced glutathione S-transferase and glutathione-dependent peroxidase activities and triggered glutathione depletion. Expression of MRP1, an ATP-dependent GS-X pump, was unmodified. Moreover, isobologram analysis showed that sodium butyrate sensitized VCREMS to doxorubicin-mediated toxicity. Verapamil, an inhibitor of MRP1, did not significantly affect this chemosensitizing effect, suggesting that the observed toxicity stems from multifactorial mechanisms. Interestingly, synergism between sodium butyrate and doxorubicin was more pronounced in resistant VCREMS cells than in parental sensitive MCF-7 cells.

Breast Neoplasms↗
PubMed1984

Methyl butyrate-hydrolyzing activity of hepatic triglyceride lipase from rat post-heparin plasma.

Hepatic triglyceride lipase was obtained from post-heparin plasma of rats in an electrophoretically homogeneous form. The enzyme had an isoelectric point at pH 4.9 and molecular weight of 65,000. The relation between the "lipase" and "esterase" activities of the enzyme was studied using emulsified triolein and water-soluble methyl butyrate (80 mM) as substrates. The same enzyme protein catalyzed the hydrolyses of both emulsified triolein and water-soluble methyl butyrate. The relation of activity to the methyl butyrate concentration differed from those for pancreatic lipase and liver esterase. During purification, the ratio of methyl butyrate to triolein-hydrolyzing activity of the enzyme increased. On digestion of the enzyme with trypsin, the "lipase" activity was retained. However, the trypsin-treated enzyme was adsorbed to a heparin-Sepharose column and eluted with 0.75 M NaCl, like the untreated enzyme. These results suggest that rat hepatic triglyceride lipase contains a so-called "hydrophobic recognition site" that is destroyed by trypsin treatment and is distinct from the heparin-binding and catalytic sites.

Animals↗
PubMed1981

The effect of butyrate on sulfated glycoprotein biosynthesis by human kidney tumor cells.

Human kidney tumor cells in culture incorporate [3H]glucosamine and 35SO4 into several classes of glycoconjugate products. After a 24-h labeling period, the 3H/35S-glycosaminoglycans and 3H-glycoproteins synthesized were found associated with both the cell layer and the culture medium. These tumor cells also synthesized a class of 35S-glycoproteins which contained alkali-stable 35S-oligosaccharide chains. These 35S-glycoproteins did not accumulate with the cell layers but were preferentially found in the culture medium (82-96%). After treatment with 2.5 mM butyrate for 24 h, the tumor cells assumed a more flattened and spread morphology with more clearly defined cell borders. These butyrate-treated cell cultures showed less than a 2-fold increase in the cell-associated form of both 3H/35S-glycosaminoglycans and 3H-glycoproteins, compared to cells cultured in the absence of butyrate. In contrast, butyrate-treated cell cultures had a 3-fold increase in the total incorporation of 35SO4 into glycoproteins and a dramatic 10-30-fold increase in the cell-associated form of these 35S-glycoprotein products as compared to untreated cell cultures.

Butyrates↗
PubMed1980

Effects of lactate, pyruvate, butyrate and ammonia on gluconeogenesis from propionate by isolated rabbit liver cells.

The rate of gluconeogenesis in isolated rabbit liver cells has been measured from propionate, lactate, pyruvate and from the combination of propionate at different concentrations either with lactate or pyruvate. The glucose formed from propionate according to its concentration is about 74 to 87% of the glucose formed from lactate. No lag period was observed with preincubated cells and gluconeogenesis is linear at least from 90 min when the substrates are present at a concentration of 5 micrometers or more. Combinations of lactate + propionate increase the glucose formed as compared with propionate alone by a factor 1.5 - 1.7 according to substrates concentrations. Combinations of propionate + pyruvate decrease glucose formation in comparison with propionate alone. Conversion of pyruvate into lactate is enhanced by propionate. Glucose formation from lactate is strongly decreased by 14 micrometers quinolinate but has no significant effect on glucose formation from propionate. Amino-oxyacetate (0.2 micrometers) which decreases gluconeogenesis from lactate produced a slight enhancement of gluconeogenesis from propionate. 10 micrometers n-butylmalonate decreases gluconeogenesis by about 20-30% from three substrates. These observations are consistent with a predominant conversion of propionate into phosphoenolpyruvate intramitochondrially. Butyrate is rapidly metabolized by isolated rabbit liver cells with formation of ketone bodies. It inhibits glucose formation from propionate. 10 micrometers ammonium chloride + 2 micrometers ornithine in presence of propionate give an important ureogenesis and strongly decrease gluconeogenesis from propionate. At low concentration (0.5 micrometers), butyrate partially raises the inhibiting effect of ammonia on gluconeogenesis. This effect is progressively annulled as butyrate concentration rises to 10 micrometers. These observations are consistent with the fact that butyrate modifies the intramitochondrial ratio NADH/NAD and thereby the oxidation of malate formed from propionate.

Ammonia↗
PubMed1994

Butyrate derivatives. New agents for stimulating fetal globin production in the beta-globin disorders.

PURPOSE: Stimulating expression of the normal fetal globin genes is a preferred method of ameliorating sickle cell disease and beta-thalassemia for the majority of patients in North America who do not have appropriate bone marrow donors. PATIENTS AND METHODS: Due to increased survival of red blood cells that contain both hemoglobin S and hemoglobin F, as little as 4-8% fetal globin synthesis in the bone marrow can produce levels of hemoglobin F of approximately 20% in the peripheral circulation. Some success has been achieved in stimulating hemoglobin F using chemotherapeutic agents (such as hydroxyurea and 5-azacytidine) and growth factors (erythropoietin) that alter erythroid growth kinetics. However, there is reluctance to treat children with chemotherapeutic agents because of possible undesirable long-term side effects. RESULTS: Butyric acid and butyrate derivatives are generally safe compounds that stimulate the promoters of individual fetal and embryonic globin genes and thus provide a more specific therapy. An initial trial with the parent compound, given as arginine butyrate, has demonstrated rapid stimulation of fetal globin expression to levels that can ameliorate these conditions. Phase I trials of an oral butyrate derivative with a long plasma half-life have begun. CONCLUSIONS: These agents may provide a new and specific approach for ameliorating the clinical manifestations of sickle cell disease and beta-thalassemia.

Adolescent↗
PubMed1994

Fetal hemoglobin induction by acetate, a product of butyrate catabolism.

Butyrate induces fetal hemoglobin (HbF) synthesis in cultures of erythroid progenitors, in primates, and in man. The mechanism by which this compound stimulates gamma-globin synthesis is unknown. In the course of butyrate catabolism, beta oxidation by mitochondrial enzymes results in the formation of two acetate molecules from each molecule of butyrate. Studies were performed to determine whether acetate itself induces HbF synthesis. In erythroid burst-forming unit (BFU-E) cultures from normal persons, and individuals with sickle cell disease and umbilical-cord blood, dose-dependent increases in gamma-globin protein and gamma mRNA were consistently observed in response to increasing acetate concentrations. In BFU-E cultures from normal adults and patients with sickle cell disease, the ratio of gamma/gamma + beta mRNA increased twofold to fivefold in response to acetate, whereas the percentage of BFU-E progeny staining with an anti-gamma monoclonal antibody (MoAb) increased approximately twofold. Acetate-induced increases in gamma-gene expression were also noted in the progeny of umbilical cord blood BFU-E, although the magnitude of change in response to acetate was less because of a higher baseline of gamma-chain production. The effect of acetate on HbF induction in vivo was evaluated using transgenic mouse and primate models. A transgenic mouse bearing a 2.5-kb mu locus control region (mu LCR) cassette linked to a 3.3-kb A gamma gene displayed a near twofold increase in gamma mRNA during a 10-day infusion of sodium acetate at a dose of 1.5 g/kg/d. Sodium acetate administration in baboons, in doses ranging from 1.5 to 6 g/kg/d by continuous intravenous infusion, also resulted in the stimulation of gamma-globin synthesis, with the percentage of HbF-containing reticulocytes (F reticulocytes) approaching 30%. Surprisingly, a dose-response effect of acetate on HbF induction was not observed in the baboons, and HbF induction was not sustained with prolonged acetate administration. These results suggest that both two-carbon fatty acids (acetate) and four-carbon fatty acids (butyrate) stimulate synthesis of HbF in vivo.

Acetates↗
PubMedDate not supplied

Effects of arginine butyrate and tributyrylxylitol on cultured human sarcoma cells.

The effects of arginine butyrate and tributyrylxylitol were studied comparatively in a human sarcoma cell line. Both induced important structural and functional modifications suggestive of cell differentiation, as shown by the dose-dependent increase of alkaline phosphatase activity and total protein content, at concentrations ranging from 1mM to 5 mM expressed in butyrate equivalents. hCG beta-subunit present in the culture medium increased with differentiation. Our results show that most of the differentiation changes previously reported for sodium butyrate in cancer cell lines are also produced by both drugs. Tributyrylxylitol appears to be the more potent and effective inducer of differentiation but its use is limited << in vitro >> on account of its relative toxicity at concentrations above 3 mM butyrate equivalents.

Alkaline Phosphatase↗
PubMed1994

Effects of butyrate on the erythropoietin receptor of cell line IW201.

The murine erythroleukemic cell line, IW201, normally expresses only low-affinity erythropoietin receptors. Exposure of these cells for 48 hours to sodium butyrate results in a change in receptor kd from about 600 pmol/L to 100 to 200 pmol/L. This change in affinity is accompanied by downregulation of both receptor number and receptor mRNA. Cells exposed to sodium butyrate for 2 hours show a similar change in kd but no change in receptor number. The butyrate effect on kd at 2 hours is abrogated by either cycloheximide or actinomycin D. These data indicate that an accessory protein induced by sodium butyrate is responsible for high-affinity binding of erythropoietin.

Animals↗
PubMed2002

Potentiating antitumor effects of a combination therapy with lovastatin and butyrate in the Lewis lung carcinoma model in mice.

Lovastatin, the drug used for the treatment of hypercholesterolemia, has previously been reported to exert antitumor activity in experimental murine models. Butyrate and butyric acid derivatives are well known to induce differentiation and apoptosis of tumour cells and also have recently gained acceptance as potential anticancer agents. In this study, we examined the antitumor effects of the combination of lovastatin and butyrate or its prodrug tributyrin in vitro and in vivo against a murine Lewis lung carcinoma (3LL). This combination therapy showed synergistic antitumor activity against 3LL cells in vitro. These effects were at least in part due to apoptosis induction that occurred after 12 hr of incubation with lovastatin and butyrate and was preceded by changes in cell cycle distribution of treated cells and expression of p21, p53 and cyclin D1. Remarkably, a systemic treatment of syngeneic mice inoculated with 3LL cells with both drugs resulted in significant tumour growth retardation.

Animals↗
PubMed1981

Differentiation of macrophages from Lewis lung carcinoma tumour cells in tissue sections by their alpha-naphthyl butyrate esterase activity.

The activities of alpha-naphthyl butyrate esterase, non-specific esterase, indoxyl esterase and acid phosphatase were studied histochemically in macrophages in cultures and in tissue sections of primary tumours and metastases of Lewis lung carcinoma (3LL). All macrophages in culture were stained by the alpha-naphthyl butyrate esterase procedure. In tissue sections, macrophages were intensely stained by the butyrate esterase procedure, while the tumour cells were not stained at all; macrophages were easily differentiated from 3LL cells. Non-specific esterase was evident in both tumour cells and macrophages. Indoxyl esterase and acid phosphatase were present in macrophages at the margin of the tumour only. The alpha-naphthyl butyrate esterase-positive macrophages differed in shape and location from acid phosphatase and indoxyl esterase-positive macrophages. This may indicate a difference in characteristics between macrophages found inside a tumour and those found at the tumour margins.

Acid Phosphatase↗
PubMed2004

Identification and quantitation of extractables from cellulose acetate butyrate (CAB) and estimation of their in vivo exposure levels.

The purpose of this study was to qualitatively and quantitatively determine potential cellulose acetate butyrate (CAB) extractables in a way to meaningfully predict the in vivo exposure resulting from clinical administration. Extractions of CAB-381-20 were performed in several solvent systems, consistently resulting in the detection of three extractables. The extractables have been identified as acetic acid, butyric acid, and E-2-ethyl-2-hexenoic acid (E-EHA) by LC/UV, LC/MS and NMR. Extraction studies of CAB powders in acetonitrile/phosphate buffer demonstrated quantitative extraction in 1 h for acetic acid (approximately 150 microg/g), butyric acid (approximately 200 microg/g), and EHA (approximately 20 microg/g). Subsequently, extraction studies for CAB powders and coated tablets in USP simulated gastric and intestinal fluids were performed to evaluate potential in vivo exposure. Similarly, acetic and butyric acids were quantitatively extracted from CAB-381-20 powder after 24 h exposure in both USP simulated fluids. The amounts of EHA extracted from CAB powder after 24 h were determined to be 2 and 16 microg/g in USP simulated gastric and intestinal fluids, respectively. After 24 h exposure in USP simulated fluids, the maximum amount of EHA extracted corresponds to < 0.3 microg of EHA per tablet. Pepsin and pancreatin in USP simulated fluids had no effect on EHA extraction and quantitation.

Cellulose↗