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PubMed1985

The role for butyrate and propionate in mediating HeLa-cells growth inhibition by human dental plaque fluid from adult periodontal disease.

To determine to what extent propionate and butyrate, secreted in vitro by various oral bacteria, account for the growth-inhibiting activity of plaque fluid in gingivitis in the absence or presence of chronic periodontitis, the fluid phase of plaque from each of these disease forms was obtained by homogenizing the bacteria with 0.13 M NaCl, centrifuging the mixture and Millipore-filter-sterilizing the plaque-fluid-extract supernatant. Toxins were detected and measured by growth inhibition of HeLa cells grown in minimal Eagle medium supplemented with calf serum and antibiotics. Samples of butyrate, propionate or plaque-fluid extract were added and inhibition of growth was determined relative to control cultures. The toxins in each extract were characterized by their stability to heat, freeze-drying and elution on gel filtration. Butyrate and propionate contents were measured with a Hewlett-Packard 5880A gas chromatograph. The plaque-fluid extracts from each group had similar contents of butyrate, but most of the activity was due to heat-sensitive high mol. wt components. Butyrate and propionate accounted for only 5 to 15 per cent of the total activity. High mol. wt exotoxins, rather than butyrate or propionate, were the most prominent and freeze-drying-stable tissue-destructive agents in the plaque fluid from subjects with or without periodontitis.

Acetates↗

PubMed1984

Regulation of enzymes responsible for neurotransmitter synthesis and degradation in cultured rat sympathetic neurons. III. Effects of sodium butyrate.

The effects of Na butyrate on the differentiation of newborn rat sympathetic neurons in primary cultures have been studied. Butyrate did not affect the long-term survival of these neurons in the presence of optimal concentrations of nerve growth factor, but decreased in a dose-dependent manner their protein content. In the range, 0.5-20 mM, butyrate did not modify the specific activity of lactate dehydrogenase in these cultures. Choline acetyltransferase activity developed at a 4.5- to 12-fold higher rate in cultures grown with 1-5 mM butyrate than in its absence. Concomitantly, tyrosine hydroxylase, dopa decarboxylase, dopamine-beta-hydroxylase, and acetylcholinesterase were depressed in cultures grown with butyrate. The deficit in acetylcholinesterase total activity was accompanied by an inhibition of the development of the asymmetric 16 S form of the enzyme. The deficit in tyrosine hydroxylase activity did not result from either a modification of the app Km for the enzyme's cofactor or a modification of its state of cAMP-dependent phosphorylation, but from a decrease in the number of immunoprecipitable enzyme molecules. A similar result was obtained with acetylcholinesterase. Butyrate thus reproduced in a qualitative manner the effects of a macromolecular factor purified from muscle conditioned medium on these neurons (J. P. Swerts, A. LeVan Thaï, A. Vigny, and M. J. Weber (1983) Dev. Biol. 100, 1-11; J. P. Swerts, Le Van Thai, and M. J. Weber (1984) 103, 230-234), raising the hypothesis of a common pathway in the regulation of neurotransmitter phenotype by these two agents.

Acetylcholinesterase↗

PubMed1987

Regulation of beta-adrenoceptor number and subtype in 3T3-L1 preadipocytes by sodium butyrate.

In mouse 3T3-L1 preadipocytes, the glucocorticoid dexamethasone has been shown to promote a switch in beta-adrenoceptor subtype expression from beta 1 to beta 2 and to increase the total number of beta-adrenoceptors. The present study demonstrates that sodium butyrate also modulates beta-adrenoceptor expression in these cells. Incubation of preadipocytes with 2-10 mM butyrate for 24-48 h promoted a dose- and time-dependent switch in beta-adrenoceptor subtype from a near equal mixture of beta 1 and beta 2 to greater than 85% beta 2 and caused an approximate doubling of the receptor number. beta-Adrenoceptors were assayed in membranes prepared from 3T3-L1 cells using the radiolabeled antagonist [125I]iodocyanopindolol and the beta 2-selective antagonist ICI 118.551. Other short chain acids were not as effective as butyrate in promoting changes in beta-adrenoceptor expression. Cycloheximide (1.0 microgram/ml) inhibited the effects of butyrate on both beta-adrenoceptor subtype and number. Alterations in beta-adrenoceptor phenotype promoted by either butyrate or dexamethasone were functionally correlated with cAMP accumulation in these cells. Comparison of the effects of butyrate and dexamethasone on beta-adrenoceptor expression suggests that these two agents regulate beta-adrenoceptors by different mechanisms.

Adipose Tissue↗

PubMed1983

Extent of histone modifications and H1(0) content during cell cycle progression in the presence of butyrate.

The effects of butyrate upon the extents of phosphorylation of histones H1 and H1(0) during cell-cycle progression have been investigated. Chinese hamster (line CHO) cells were synchronized in early S phase and released into medium containing 0 or 15 mM butyrate to resume cell-cycle traverse into G1 of the next cell cycle. Cells were also mechanically selected from monolayer cultures grown in the presence of colcemid and 0 or 15 mM butyrate to obtain greater than 98% pure populations of metaphase cells. Although cell cycle progression is altered by butyrate, electrophoretic patterns of histones H1, H1(0), H3, and H4 indicate that butyrate has little, if any, effect on the extents of H1 and H1(0) phosphorylation during the cell cycle or the mitotic-specific phosphorylation of histone H3. Butyrate does, however, inhibit removal of extraordinary levels of histone H4 acetylation (hyperacetylation) during metaphase, and it appears to cause an increase in the content of H1(0) in chromatin during the S or G2 phases of the cell cycle.

Acetylation↗

PubMed1993

Regulation of c-myc expression by sodium butyrate in the colon carcinoma cell line Caco-2.

The human colon carcinoma cell line Caco-2 spontaneously undergoes enterocytic differentiation in culture. We used sodium butyrate to modify differentiation and growth properties of this cell line and considered c-myc expression as a potential target. Degradation of normal c-myc mRNAs with a half-life of 20 min is not coupled to translation in this cell line, as determined by cycloheximide treatment. We show that butyrate reduces c-myc mRNA levels after a 30 min delay. Butyrate does not affect c-myc expression at the level of transcriptional initiation or elongation, as determined by run-on analysis, but at a post-transcriptional level. Cycloheximide blocks butyrate-dependent reduction of c-myc mRNA levels. Cross-linking experiments show that a 34 kDa protein binds specifically to the c-myc AU-rich instability determinant found in the 3'-untranslated region (ARE). Binding of this protein to the ARE is not modulated by butyrate or cycloheximide. These experiments suggest that butyrate induces a factor involved in c-myc mRNA degradation that differs from the known ARE-associated proteins. Post-transcriptional modification of gene expression could be one of the major targets for this anti-proliferative agent.

Blotting, Northern↗

PubMed1986

Effects of differing concentrations of sodium butyrate on 1,2-dimethylhydrazine-induced rat intestinal neoplasia.

The incidence, distribution, size, and histopathology of small and large bowel tumors induced by parenteral administration of 1,2-dimethylhydrazine were examined in rats given 1% or 2% sodium butyrate dissolved in drinking water. Although previous in vitro reports on colon cancer cell lines have suggested that sodium butyrate might have a role to play as a chemotherapeutic "differentiating agent," the results of this in vivo study indicate that sodium butyrate treatment enhanced the development of colonic neoplasia and was associated with increased fecal butyric acid concentrations. In contrast, no changes were seen in the incidence of small bowel tumors, luminal butyric acid concentrations, mucosal morphology, or brush-border enzyme activities (i.e., sucrase, alkaline phosphatase). This study suggests that dietary butyrate has an important, possibly indirect, regulatory role in carcinogenesis associated with an experimental animal model of colonic neoplasia.

Animals↗

PubMed1984

Induction of retinol esterification in retinal pigment epithelial cells by butyrate.

Butyrate induced marked morphological changes in cultured human retinal pigment epithelial (RPE) cells. The cells assumed a flattened structure within six hours of exposure to butyrate. The butyrate-treated retinal pigment epithelial cells possessed an enhanced capacity to esterify retinol. Among all short chain organic acids tested, butyrate was by far the most effective, followed by pentanoate and hexanoate. The inductive effect of butyrate was specific for retinol esterification, since the incorporations of fatty acid into phosphatidyl choline and cholesteryl ester were not enhanced. Time-dependent, butyrate-enhanced retinol esterification may be related to the inhibition of cell proliferation. This represents the first report on the induction of retinol esterification in cultured retinal pigment epithelial cells.

Adolescent↗

PubMed1989

Mutational analysis of sodium butyrate inducible elements in the human immunodeficiency virus type I long terminal repeat.

Sodium butyrate induces gene expression directed by the human immunodeficiency virus type 1 (HIV-1) long terminal repeat (LTR) in HeLa cells. Inducible regions of the HIV-1 LTR were elucidated by using 5' and 3' LTR deletion mutants and LTR site-directed mutants within the Sp1 binding sites and the trans-activation responsive (TAR) region. Two LTR regions inducible by sodium butyrate were located: one at -117 to -103 (distal site) and one at -65 to -17 (proximal site). In HeLa cells trans-fected with pZ6neo, a biologically active HIV-1 proviral clone, sodium butyrate stimulated virus production following a 3-day treatment. Inducibility of HIV-1 gene expression by sodium butyrate was unrestricted in many human cell types, including CD4+ lymphoid cells and non-CD+ brain cells and fibroblasts. Additionally, sodium butyrate transiently induced HIV-2 LTR-directed gene expression in HeLa cells. Using the HIV-1SF-2 tat gene cotransfected with pLTR-CAT site-directed TAR mutants in HeLa cells, the boundaries of tat-trans-activation were delineated more precisely. These results suggest that the induction of HIV-1 gene expression is mediated by the interaction of sodium butyrate with cellular transcription factors that bind to the HIV-LTR.

Base Sequence↗

PubMed1983

Enhanced transglutaminase activity in transformed human lung fibroblast cells after exposure to sodium butyrate.

The low level of transglutaminase activity in virus-transformed human embryonic lung fibroblasts (WI-38 VA13A) increased markedly when cells were exposed to sodium butyrate. The effect of sodium butyrate was time- and concentration-dependent and fully reversible. Transformed cells exposed for 5 days to 1 mM sodium butyrate had fewer cells, showed an 8-10 fold higher transglutaminase activity, and stained more abundantly for transglutaminase and pericellular fibronectin than control cells when examined by indirect immunofluorescence. Non-transformed cells (WI-38) showed only a 2-4-fold increase in transglutaminase activity when treated in a similar manner. Studies with metabolic inhibitors revealed the increase in activity was the result of synthesis of new protein. Kinetic studies showed the affinity of putrescine for the enzyme was essentially unchanged but the number of active sites increased 9-fold following exposure to sodium butyrate. Enhanced transglutaminase activity returned to control levels within 7 days after subculture and sodium butyrate removal. These findings suggest that sodium butyrate offers a potential model system to understand better the role of transglutaminase in cells in culture; particularly growth control in transformed cells.

Acyltransferases↗

PubMed1988

Effect of pyrimidine deoxynucleosides and sodium butyrate on expression of the glycoprotein hormone alpha-subunit and placental alkaline phosphatase in HeLa cells.

Production of the glycoprotein hormone common alpha-subunit and placental alkaline phosphatase activity can be modulated in HeLa cells by a variety of deoxynucleosides. Dose response curves for thymidine (Thd), fluorodeoxyuridine (FdUrd), bromodeoxyuridine (BrdUrd) and iododeoxyuridine (IdUrd) demonstrate that, in general, alkaline phosphatase was increased by lower concentrations of inducer than was alpha-subunit. The deoxynucleosides were not as effective as sodium butyrate as inducers of either protein. Whereas Thd and the halogenated dUrd derivatives enhanced protein expression, deoxycytidine (dCyd) had negative effects. Induction by deoxynucleosides of both alkaline phosphatase and alpha-subunit was inhibited by dCyd, but induction of alkaline phosphatase by butyrate was more sensitive to dCyd inhibition than was the butyrate-mediated induction of alpha-subunit. These results suggest that the two proteins are not regulated in a coordinate manner. Reversal of alkaline phosphatase induction by dCyd was not observed in cells preincubated with sodium butyrate for 6-24 h before the addition of dCyd, indicating that the deoxynucleoside interferes with an early event in the butyrate-mediated response. Combinations of butyrate with Thd, BrdUrd or IdUrd were synergistic with respect to the induction of HeLa-alpha. It is concluded that incorporation of the deoxynucleosides into DNA may not be required for the synergistic response since 2',5'-dideoxythymidine was an effective as Thd. Cytoplasmic dot hybridizations demonstrate that a primary effect of the various effectors is to increase the steady-state levels of alpha-subunit mRNA. There was a good correlation between alpha-subunit accumulation and corresponding levels of alpha-mRNA, suggesting that regulation occurs at a pretranslational site. Although the mechanism(s) is not understood, these data provide evidence that nucleosides or their derivatives can significantly affect gene expression.

Alkaline Phosphatase↗

PubMed1992

Effects of sodium butyrate on the expression of sodium channels by neuronal cell lines derived from the rat CNS.

We have studied the effects of sodium butyrate on cell morphology and the expression of mRNAs encoding voltage-gated sodium channels in five neuronal cell lines, B35, B50, B65, B103 and B104, all derived from the rat CNS. The cells were grown in medium supplemented with 2.5 mM sodium-n-butyrate and examined daily by phase-contrast microscopy. Sodium butyrate caused slowing of cell division and the formation of longer and more highly branched cytoplasmic processes than were present in untreated cells. Expression of sodium channel mRNA was analysed by PCR with primers that allow the transcripts encoding the different types of sodium channel to be distinguished according to the lengths of the PCR products. The identity of the PCR products was confirmed by restriction enzyme digestion. Southern blotting and hybridization with internal radiolabelled probes. Prior to sodium butyrate treatment, expression of sodium channel mRNA was largely restricted to B50 and B104 cells: B50 cells showed expression of rat brain types I and II sodium channel and B104 cells expressed rat brain type III sodium channel. After treatment for 5 days with sodium butyrate, sodium channel mRNA was detected in all five cell lines. In addition to type I and type II sodium channel, B50 cells expressed rat brain type III sodium channel. These three types of sodium channel were also expressed by B35, B65 and B103 cells. Even after butyrate treatment, B104 cells expressed only type III sodium channel. The treatment also induced expression of rat skeletal muscle SkM1 sodium channel in B35 cells but only trace amounts in the other neuronal cell lines.

Animals↗

PubMed1987

Effects of intravenous injection of butyrate on the exocrine pancreatic secretion in guinea pigs.

1. The stimulus-secretion coupling in the pancreatic exocrine responses to i.v. injection of sodium butyrate was investigated in guinea pigs in vivo and in vitro. 2. Intravenous single injection of sodium butyrate (12.5-100 mumol/100 g body wt) caused an increase in fluid and amylase secretion in a dose-dependent manner. The responses evoked by sodium butyrate (100 mumol/100 g body wt) were not affected by prior injection of atropine (0.14 mumol/100 g body wt) or hexamethonium (4 mumol/100 g body wt). 3. The chloride concentration in secreted fluid increased slightly with an increase in flow rate in response to sodium butyrate, but decreased in response to secretin. 4. The amylase release from the pancreatic segments evoked by sodium butyrate (10(-6)-10(-2) M) increased dose-dependently. The responses were potentiated in the presence of secretin (1 C.H.R.u./ml), but were suppressed in the presence of acetylcholine (10(-6) M) or in a Ca-free solution containing EGTA (10(-4) M). 5. These results suggest that the secretory effects in response to i.v. injection of sodium butyrate probably arise from direct action on the acinar cells, and that an increase in cellular calcium concentration might be an important step in the secretion process, in guinea pig exocrine pancreas.

Acetylcholine↗

PubMed1992

Effects of sodium butyrate on 1,25-dihydroxyvitamin D3 receptor activity in primary chick kidney cells.

The genomic effects of the steroid hormone 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) are mediated by high affinity nuclear associated specific receptors that belong to the superfamily of ligand induced transcription factors. The carboxylic acid, sodium butyrate--a potent inhibitor of histone deacetylase--is known to modulate gene expression in a variety of systems. Specific binding of 1,25(OH)2D3 to its receptor was examined in primary chick kidney cells, the chick macrophage cell line HD-11, and other mammalian cell lines such as ROS 17/2.8, HT-29 and CV-1 cells, that were all cultured in the presence or absence of 1 mM sodium butyrate. Treatment with n-butyrate resulted in significant (4.0-4.5-fold) increases in 1,25(OH)2D3 receptor binding without changing binding affinity only in the primary cultures of chick renal epithelial cells and the chick macrophage cell line but not in the other heterologous receptor-positive cell lines. The maximum increase in receptor binding was evident at 1 mM butyrate concentration. This effect reached a maximum at 15 h treatment, beyond which there was slow attenuation in increased binding until 24 h. The butyrate induced increases in receptor activity was associated with increases in the 1,25(OH)2D3-mediated induction of calbindin-D28K protein only in primary chick kidney cultures but not in the macrophage cell line (HD-11). Similarly, calbindin-D28K promoter activity was enhanced only in butyrate-treated primary chick kidney cultures, transfected with chimeric plasmids containing the 5' flanking sequence of the calbindin-D28K promoter fused to the chloramphenicol acetyl transferase (CAT) reporter gene but not in HD-11 cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1985

Effects of sodium n-butyrate on alpha-fetoprotein and albumin secretion in the human hepatoma cell line PLC/PRF/5.

The in vitro effects of sodium n-butyrate (butyrate) on the growth, morphology and secretion of alpha-fetoprotein (AFP) and albumin by the human heptoma cell line PLC/PRF/5 were studied. Butyrate caused a marked reduction in the growth rate, colony forming efficiency in soft agar and de novo synthesis of DNA as well as remarkable morphological changes including cell enlargement, flattening and a decreased number of nucleoli. Secretion of AFP was reduced during culture with butyrate, while that of albumin was increased. The requirement of de novo protein synthesis for the increase in albumin and decrease of AFP by butyrate was demonstrated by inhibition studies with cycloheximide. These results suggest that butyrate caused the hepatoma cells to acquire in vitro properties that are considered to be more consistent with normal liver cells.

Albumins↗

PubMed1986

Diffusion of butyrate through pig colonic mucus in vitro.

Using a modified equilibrium dialysis cell the rate of diffusion of butyrate through pig colonic mucus has been compared with that through other gels and unstirred layers. Relative diffusion coefficients were calculated for each layer. Layers of 8% polyacrylamide, and of caecal, mid-colonic and terminal colonic mucus, had coefficients that were 50-60% of the apparent free diffusion coefficient for butyrate, determined using layers made up of Millipore filters alone. The apparent free diffusion coefficients for butyrate (layers of agarose or filters) were 70% of previously determined values in the literature. This discrepancy can be explained by elements of the experimental procedure. All mucus layers differed significantly from layers of 2% agarose and Millipore filters but were not significantly different from layers of 8% polyacrylamide or from each other. Diffusion coefficients for butyrate in the mucus samples correlated with water content and carbohydrate content but had no relationship to protein content. The rate of diffusion of butyrate in colonic mucus layers was significantly reduced when compared with unstirred layers (P less than 0.05). Whether this has an effect on the butyrate supply to colonocytes in vitro and whether mucus in colonic disease behaves differently are subjects for further investigation.

Animals↗

PubMed1996

Sodium butyrate delays neutrophil apoptosis: role of protein biosynthesis in neutrophil survival.

Sodium butyrate, which directly affects chromatin structure and function in many cells, is as effective as granulocyte-macrophage colony-stimulating factor (GM-CSF) in delaying apoptosis in human neutrophils. Both butyrate and GM-CSF preserved the ability of neutrophils cultured for 22 h in vitro to generate reactive oxidants and express receptors such as CD16. They also delayed apoptotic morphology and DNA fragmentation, and stimulated de novo biosynthesis: newly-labelled polypeptides detected by 2D-polyacrylamide gel electrophoresis after treatment with GM-CSF and butyrate were very similar. Cycloheximide abrogated the effects of both GM-CSF and butyrate. Exposure to butyrate for 1 h did not prime oxidant production and did not up-regulate expression of CD11b. Hence, unlike GM-CSF, butyrate does not stimulate translocation of granules to the plasma membrane. These data suggest that active gene expression is involved in the regulation of neutrophil apoptosis and changes in chromatin structure and function may control apopotosis in these cells.

Apoptosis↗

PubMed1996

Butyrate enemas in experimental colitis and protection against large bowel cancer in a rat model.

BACKGROUND & AIMS: Butyrate is effective in experimental colitis by increasing transglutaminase activity. Because ulcerative colitis increases the risk of colonic neoplasia, the aim of this study was to investigate whether butyrate treatment reduces mucosal sensitivity to colon cancer development in rats with experimental colitis. METHODS: Colon cancer was induced by azoxymethane injections in 10 rats with trinitrobenzensulfonic acid-induced colitis and 10 rats without colitis. Three additional groups of rats with colitis were treated with butyrate, mesalamine, and saline enemas, respectively, twice daily for 8 weeks; 1 week after colitis induction, tumors were induced. Biopsy specimens for assessment of proliferation pattern and transglutaminase activity were obtained during the latent period of cancer development. Characteristics of tumors were recorded 27 weeks after the first exposure to azoxymethane. RESULTS: Experimental colitis enhanced carcinogenesis; butyrate therapy reduced both incidence and size of tumors and also affected colonic proliferation pattern. Transglutaminase levels were restored by butyrate treatment in rats with colitis. CONCLUSIONS: The protective effect of butyrate against large bowel cancer in experimental colitis suggests its usefulness in long-term therapy to decrease disease relapses and to reduce colon cancer risk in ulcerative colitis.

Animals↗

PubMed1990

Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate.

Our laboratory has previously developed cell lines derived from mouse NIH 3T3 fibroblasts and C127 mammary tumor cells that stably express mouse mammary tumor virus (MMTV) long terminal repeat fusion genes in bovine papillomavirus-based episomes. Glucocorticoid hormone strongly activates transcription from episomes and induces the disruption of a single nucleosome in an array of phased nucleosomes on the MMTV promoter. Sodium butyrate inhibits the glucocorticoid hormone-dependent development of a nuclease-hypersensitive site that is due to the displacement of this nucleosome, and inhibits induction of RNA transcripts from episomes. Saturation binding studies show that butyrate treatment does not significantly affect the amount or the hormone-binding affinity of the glucocorticoid receptor. In a transient transfection assay, glucocorticoid hormone can activate transcription from a MMTV long terminal repeat-driven luciferase gene construct equivalently in untreated and butyrate-treated cells, indicating that the soluble factors necessary for transactivation of the MMTV promoter are unaffected by butyrate. The differential effect of butyrate on the induction of stable chromatin templates and transiently expressed plasmids suggests that butyrate prevents nucleosome displacement and represses transcription by inducing a modification of chromatin.

Animals↗