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PubMed1995

Cell cycle perturbation by sodium butyrate in tumorigenic and non-tumorigenic human urothelial cell lines assessed by flow cytometric bromodeoxyuridine/DNA analysis.

The effect of sodium butyrate on cell proliferation was studied in eight human urothelial cell lines differing in transformation grade (TGr): Hu 1752 (mortal, TGr I); HCV29 (immortal and tumorigenic, TGr II); HCV29T, T24, T24A, T24B, Hu 961A and Hu 1703He (tumorigenic, TGr III). In all cell lines, except Hu 1752, addition of 4 mM sodium butyrate at 18 h after replating resulted in a significantly decreased population of adherent cells after a further 24-48 h. This might partially be explained by detachment of cells, probably mainly S phase cells, from the substrate in the lines HCV29, HCV 29T, Hu 961A and Hu 1703He. Flow cytometric DNA analysis of the adherent cell population showed that all TGr II and III urothelial cell lines were DNA aneuploid, and that butyrate perturbed the cell cycle distribution in these cell lines, mainly by a decrease of the S phase fraction. Flow cytometric bromodeoxyuridine (BrdUrd)/DNA analysis of continuously BrdUrd labelled cultures, using a 'washless' BrdUrd/DNA staining technique, showed that butyrate inhibited the G0/1-S phase transition, indicated by a delayed depletion of BrdUrd negative G0/1 cells in the cell lines HCV29, HCV29T, T24B, Hu 961A and Hu 1703He. BrdUrd/DNA analysis further showed that butyrate inhibited the G2M-G0/1 phase transition, indicated by a pronounced accumulation of BrdUrd positive G2M cells in the cell lines HCV 29T, T24B, Hu 961A and Hu 1703He. Microscopy of HCV29T and Hu 961A cells indicated that this block did not occur in mitosis. The parental cell line T24 and the cell line T24A did not show an accumulation of BrdUrd negative G0/1 cells or BrdUrd positive G2M cells like that occurring in the derived cell line T24B.

Amnion↗
PubMed1982

Effect of sodium butyrate on messenger RNA populations in myogenic cells in culture.

Sodium butyrate, when added in millimolar concentrations to a culture of myoblasts of the L6 cell line, inhibits reversibly cell proliferation and differentiation. The aim of this work was to study the effect of sodium butyrate on the nuclear and cytoplasmic RNAs in these cells. We have prepared (3H) DNAs complementary to cytoplasmic polyadenylated RNAs from treated and untreated cells and performed homologous and heterologous hybridizations with cytoplasmic polyadenylated RNAs and with total nuclear RNAs. The hybridization kinetics led to the following conclusions: a) Hybridization with nuclear RNAs shows that butyrate allows the transcription of most of the RNA sequences synthesized in proliferating myoblasts, including the sequences that are no longer synthesized in untreated myotubes. However some differences in the hybridization saturation levels indicate that sodium butyrate might modify the expression of a limited number of genes involved in cell proliferation, muscular differentiation, or both. b) Hybridization with cytoplasmic polyadenylated RNAs shows that sodium butyrate acts also at a post-transcriptional level, it produces a large decrease in the frequency of the abundant sequences present in untreated cells, but has little effect on the total number of different RNA species.

Animals↗
PubMed1996

High-level expression of rat D1A dopamine receptor cDNA in mouse fibroblast LTK- cells by n-butyrate.

1. In order to develop a simple, efficient system for the high-level expression of dopamine receptors in eukaryotic cells, we have studied the effects of n-butyrate on the expression of rat D1A dopamine receptor cDNA in mouse fibroblast LTK- cells as compared with those of n-butyrate on endogenous D1 receptor levels in opossum kidney cells. 2. In the transfected LTK- cell membranes with pRc/CMV-D1A receptor cDNA, a selective D1 dopamine antagonist, [3H]-SCH 23390, exhibited a Kd of 0.9 +/- 0.1 nmol/L and a Bmax of 0.35 +/- 0.05 pmol/mg protein (n = 5). 3. Addition of n-butyrate (2-10 mmol/L) to the culture medium for 48 h dose-dependently increased the D1A receptor level up to 1.5 +/- 0.3 pmol/mg protein (n = 7), although the Kd values were not affected. The increase in receptor level was accompanied by an elevation of selective D1 agonist-induced adenylyl cyclase activity. 4. In contrast, n-butyrate treatment (2-10 mmol/L) did not affect either endogenous D1 receptor levels or fendoldopam-induced adenylyl cyclase activity in opossum kidney cells. 5. These results suggest n-butyrate is a useful tool for obtaining high-level expression of D1A dopamine receptor cDNA in mouse fibroblast LTK- cells.

Adenylyl Cyclases↗
PubMed1990

Cyclic AMP and butyrate modulate melatonin synthesis in Y79 human retinoblastoma cells.

Melatonin is synthesized by cultured Y79 human retinoblastoma cells and is secreted into the medium. Activity of the two key enzymes involved in the synthesis of melatonin, N-acetyltransferase (NAT) and hydroxyindole-O-methyltransferase (HIOMT), are present in retinoblastoma cells. The activity of these enzymes and the resulting synthesis and release of melatonin are modulated by the addition of a cyclic AMP analogue and butyrate to the culture medium. Melatonin levels increase dramatically over control levels after the addition of dibutyryl cyclic AMP (dbcAMP), whereas melatonin levels decrease after butyrate treatment. HIOMT activity is inhibited by both dbcAMP and butyrate, and NAT activity is stimulated by both of these differentiating agents, suggesting that the rise in melatonin levels in response to dbcAMP is the result of increased activity of NAT, whereas the decline in melatonin levels in response to butyrate may be due to a drop in HIOMT activity. Melatonin synthesis is dose- and time-dependent, and the effect of dbcAMP is readily reversible, whereas the effect of butyrate does not appear to be reversible. These effects probably reflect basic differences in the regulatory mechanisms of the inducing agents.

Acetylserotonin O-Methyltransferase↗
PubMed1992

Inhibition of human endothelial cell proliferation in vitro in response to n-butyrate and propionate.

The study aimed to investigate the effects of n-butyrate and propionate on the proliferation and viability of human endothelial cells in culture. Proliferation was assessed by a 24-hour bromodeoxyuridine pulse labelling and immunoperoxidase method and viability was assessed by a colorimetric viability (MTT) assay. Endothelial cells were isolated from human umbilical vein by collagenase digestion. Experiments were performed on 96-well plates and cultures were exposed to different concentrations of n-butyrate and propionate for 2 days. n-butyrate and propionate caused significant reductions in the proliferation of endothelial cells at concentrations of 1.25 mM and 10 mM respectively (p less than 0.05); the reduction in proliferation was dose-dependent for both agents. n-butyrate was a more potent inhibitor of proliferation than propionate. However, there were no significant effects on the viability of the cells with both agents up to the highest concentrations tested (25 mM). The data indicate that n-butyrate and propionate inhibit endothelial cell proliferation which may contribute to the pathogenic effects of dental plaque in periodontal disease.

Analysis of Variance↗
PubMed1965

NATURE OF BUTYRATE OXIDATION BY MYCOPLASMA HOMINIS.

VanDemark, P. J. (Cornell University, Ithaca, N.Y.), and P. F. Smith. Nature of butyrate oxidation by Mycoplasma hominis. J. Bacteriol. 89:373-377. 1965.-Cell-free extracts of butyrate - grown Mycoplasma hominis strain O7, though lacking thiokinase activity on butyric acid, were found to activate butyrate via an acetyl-butyric thiophorase. These extracts also contained an aceto-coenzyme A (CoA) kinase, a butyryl-CoA dehydrogenase, a crotonase, a reduced nicotinamide adenine dinucleotide-specific beta-hydroxybutyryl-CoA dehydrogenase, and a thiolase. Thiolase activity was stimulated by the addition of magnesium ions. The presence of these enzyme activities in this Mycoplasma species supports the hypothesis that a fatty acid oxidation represents an energy source for the nonfermentative pleuropneumonia-like organisms.

3-Hydroxyacyl CoA Dehydrogenases↗
PubMed1991

5'-flanking sequences mediate butyrate stimulation of embryonic globin gene expression in adult erythroid cells.

A stable transfection assay was used to test the mechanism by which embryonic globin gene transcription is stimulated in adult erythroid cells exposed to butyric acid and its analogs. To test the appropriate expression and inducibility of chicken globin genes in murine erythroleukemia (MEL) cells, an adult chicken beta-globin gene construct was stably transfected. The chicken beta-globin gene was found to be coregulated with the endogenous adult mouse alpha-globin gene following induction of erythroid differentiation of the transfected MEL cells by incubation with either 2% dimethyl sulfoxide (DMSO) or 1 mM sodium butyrate (NaB). In contrast, a stably transfected embryonic chicken beta-type globin gene, rho, was downregulated during DMSO-induced MEL cell differentiation. However, incubation with NaB, which induces MEL cell differentiation, or alpha-amino butyrate, which does not induce differentiation of MEL cells, resulted in markedly increased levels of transcription from the stably transfected rho gene. Analysis of histone modification showed that induction of rho gene expression was not correlated with increased bulk histone acetylation. A region of 5'-flanking sequence extending from -569 to -725 bp upstream of the rho gene cap site was found to be required for both downregulation of rho gene expression during DMSO-induced differentiation and upregulation by treatment with NaB or alpha-amino butyrate. These data are support for a novel mechanism by which butyrate compounds can alter cellular gene expression through specific DNA sequences. The results reported here are also evidence that 5'-flanking sequences are involved in the suppression of embryonic globin gene expression in terminally differentiated adult erythroid cells.

Acetylation↗
PubMed1992

Sodium butyrate inhibits myogenesis by interfering with the transcriptional activation function of MyoD and myogenin.

Sodium butyrate reversibly inhibits muscle differentiation and blocks the expression of many muscle-specific genes in both proliferating myoblasts and differentiated myotubes. We investigated the role of the basic helix-loop-helix (bHLH) myogenic determinator proteins MyoD and myogenin in this inhibition. Our data suggest that both MyoD and myogenin are not able to function as transcriptional activators in the presence of butyrate, although both apparently retain the ability to bind DNA. Transcription of MyoD itself is extinguished in butyrate-treated myoblasts and myotubes, an effect that may be due to the inability of MyoD to autoactivate its own transcription. We present evidence that the HLH region of MyoD is essential for butyrate inhibition of MyoD. In contrast to MyoD and myogenin, butyrate does not inhibit the ubiquitous basic HLH protein E2-5 from functioning as a transcriptional activator.

Base Sequence↗
PubMed1985

Enhanced nitrosourea cytotoxicity in cell culture by sodium butyrate.

In HeLa S3 cells, sodium butyrate was found to potentiate the cytotoxicity of chloroethylnitrosoureas and alkylating agents in vitro. Using a soft-agar colony-forming assay, 2.5 and 5.0 mM sodium butyrate pretreatment for 22 h increased the cell killing efficacy of both methyl- and chloroethylnitrosoureas by between 30 and 70%. The potentiation of cytotoxicity of bifunctional nitrogen mustards by butyrate was less than that of nitrosoureas, with a 15-30% increased cell kill at 5 mM butyrate. Sodium butyrate per se reduced plating efficiency and caused growth delay if residual levels (calculated at 100 microM for starting concentrations of 5 mM) were not removed by washing prior to plating.

Butyrates↗
PubMed1987

Determination by anti-bromodeoxyuridine monoclonal antibody of cells in S phase in the human Y79 retinoblastoma line maintained in an organ culture system: effects of butyric acid.

Using bromodeoxyuridine (BrdU) and an anti-BrdU monoclonal antibody (Mab), the fraction of cells in S phase of the Y79 human retinoblastoma line maintained in an organ culture system was determined. The average labeling index (LI) (S phase cell fraction) was 21.5% after 2-15 days in vitro. The effect of butyric acid, which has been reported by others to inhibit the growth of Y79 retinoblastoma cells, was then evaluated in a similar in vitro system. Following treatment with 2 and 3 mM of butyric acid, extensive necrosis was seen in the cultures, and the LI of the surviving cells was significantly (p less than 0.01) lower (4.1 and 2.9%, respectively) than that of the control cultures (21.1%). Forty-eight hours after removal of butyric acid, the LI of the cultures treated respectively with 2 and 3 mM of butyric acid returned to the control level. Our findings suggest that the effect of butyric acid on the cell kinetics of Y79 retinoblastoma cells may be a reversible blocking effect on the G1 phase of the cell cycle.

Antibodies, Monoclonal↗
PubMedDate not supplied

Sodium butyrate inhibits carcinoma development in a 1,2-dimethylhydrazine-induced rat colon cancer.

BACKGROUND: Butyric acid is one of the most important by-products of dietary fiber degradation. It is an important trophic agent for the intestinal mucosa under different experimental conditions. Data obtained from several in vitro studies strongly suggest that butyrate can be a potential therapeutic agent in controlling the growth of some cancer cells. However to date in vivo animal studies have failed to show conclusive results. METHODS: We evaluated the effects of intracecal administration of butyrate in an experimental model of colonic carcinogenesis induced by 1,2-dimethylhydrazine (DMH), administered at the site where it is naturally produced, the cecum. We studied the incidence of colon tumors and their main histologic features. RESULTS: Direct application of sodium butyrate significantly decreased the total number of tumors and the incidence of malignancies and carcinoma in the colon. CONCLUSIONS: Butyrate may inhibit the growth of tumors induced by DMH.

1,2-Dimethylhydrazine↗
PubMed1984

Sodium butyrate stimulates somatostatin production by cultured cells.

Expression of the neuropeptide SRIF can be enhanced by sodium butyrate, a known modulator of gene transcription. Two different cell lines, RIN cells (derived from a rat pancreatic islet tumor) as well as HeLa cells, showed basal secretion of SRIF immunoreactive material that was induced between 5- and 15-fold by sodium butyrate. The induction was dose and time dependent, fully reversible, and specific for sodium butyrate. Analysis of the induced mRNAs by Northern blot hybridization using a SRIF specific cDNA probe revealed a 12-fold increase in the level of SRIF mRNA caused by butyrate treatment. These results suggest that sodium butyrate may be a useful tool for studying the regulation of SRIF gene expression.

Adenoma, Islet Cell↗
PubMed1985

Coordinate regulation of the messenger ribonucleic acids encoding the alpha- and beta-subunits of human chorionic gonadotropin in HeLa cells and butyrate-resistant variants.

Short term exposure of HeLa S3 cells to sodium butyrate induces accumulation of the mRNAs encoding both the alpha- and beta-subunits of hCG. Both mRNAs accumulate with the same kinetics and reach maximal levels with the same concentration of butyrate, suggesting that the levels of alpha and hCG beta mRNAs are coordinately regulated. In addition, induction of both mRNAs is tightly coupled with a similar increase in secreted levels of hCG subunit protein, further suggesting that regulation of CG biosynthesis in HeLa cells occurs before translation. To determine whether HeLa cells which have overcome the growth inhibitory properties of butyrate show uniformly high levels of alpha and hCG beta mRNAs, we isolated clonal variants by stepwise selection with increasing concentrations of butyrate. Of 69 isolated variants, at least 2 (AO and B2) display different patterns of CG gene expression. In AO cells, alpha-subunit mRNA was not detectable, while in B2 cells, the level of alpha-subunit mRNA was similar to that of wild-type HeLa S3 cells. Conversely, hCG beta mRNA levels in both variant cell lines approximated levels found in butyrate-treated HeLa S3 cultures, suggesting that the mRNAs for alpha and hCG beta are regulated independently. Analysis of genomic DNA by blot hybridization indicated that the alpha-subunit gene was present as a single unrearranged copy in HeLa S3 cells and in both variants, indicating that differences in alpha-subunit gene expression are not associated with major genomic alterations, but probably reflect more subtle changes.

Butyrates↗
PubMed1991

Rapid induction of parathyroid hormone-like peptide gene expression by sodium butyrate in a rat islet cell line.

The PTH-like peptide (PLP) gene is expressed in a diverse number of normal and neoplastic cell types, and induction of PLP gene expression has been observed after the induction of cellular differentiation. The differentiation of islet cells can be studied in vitro, after the exposure of rat islet cell lines to sodium butyrate. The present work found that rat RIN 1056A islet cells express the PLP gene and treatment with sodium butyrate resulted in rapid (detectable by 30 min) induction of PLP gene expression. PLP gene expression was rapidly and transiently induced by serum and cycloheximide, but the butyrate induction of PLP mRNA transcripts was not dependent on serum or new protein synthesis. Dexamethasone inhibited PLP gene expression and blocked the butyrate induction of PLP mRNA transcripts. The rapid induction of PLP gene expression after the exposure of islet cells to sodium butyrate, serum, and cycloheximide suggests that PLP may be a member of a class of early response genes involved in the regulation of cellular growth or differentiation.

Animals↗
PubMed1982

Cell-cycle-dependent effects of sodium-n-butyrate in Physarum polycephalum.

Sodium-n-butyrate affects the length of the mitotic cycle of Physarum polycephalum. Application during S- or early G2-period results in a delay of the subsequent mitosis, whereas application later in the cycle has no delaying effect. Interestingly, the second mitotic cycle after application is considerably shortened when butyrate has been administered during S- or early G2-period of the preceding cycle. In comparison, other homologous short-chain fatty acids were tested; the retarding effect on mitosis increases with the number of carbon atoms, although only butyrate can shorten the second mitotic cycle. It is shown that butyrate causes an immediate depression of synthesis of DNA, RNA and protein. After a certain time-interval the plasmodium overcomes the butyrate block. DNA synthesis is fully recovered and the inhibition of RNA and protein synthesis is even overcompensated until the next mitosis, as reflected by elevated levels of RNA and protein.

Butyrates↗
PubMed1993

n-Butyrate enhances induction of thyroid hormone-responsive nuclear protein.

Effects of n-butyrate on nuclear thyroid hormone receptors and on thyroid hormone-responsive nuclear protein were investigated by means of a perfusion system in rat liver. Treatment with 5 mM n-butyrate resulted in an increase (150%) in the maximal binding capacity of 3,5,3'-L-triiodothyronine (T3) nuclear receptors without altering the affinity of receptor for T3. However, further perfusion for 4 h decreased the number of the receptors to the control level. n-Butyrate increased the amount of acetylated histone H4. The ability of nuclear T3 receptors to bind to core histones was diminished by acetylation of the core histones. Thyroid hormone-responsive nuclear protein (n protein) was increased by T3. The induction of the n protein by T3 was augmented by n-butyrate. These results suggested that n-butyrate modulates thyroid hormone-responsive gene expression in rat liver via the increased number of nuclear receptors or changes in the chromatin constitution.

Acetylation↗
PubMed1988

The effect of sodium butyrate and retinoic acid on growth and CEA production in a series of human colorectal tumor cell lines representing different states of differentiation.

The effect of sodium butyrate and retinoic acid added singly or in combination on substrate-dependent growth, colonization efficiency in soft agar, and carcino-embryonic antigen (CEA) production in three human colorectal carcinoma cell lines differing in their degree of differentiation was studied. All three colon cancer cell lines regardless of their state of differentiation had their growth markedly slowed by sodium butyrate, and to a lesser extent by retinoic acid. When both agents were added together, a small synergistic inhibition of growth was noted in all the cell lines. Butyrate eliminated colony formation in soft agar in all three cell lines, however, retinoic acid only reduced colony formation in the well differentiated cell line DLD-2. Sodium butyrate was able to induce CEA production in the undifferentiated cell (MIP-101) and the moderately differentiated cells (clone D) which were previously negative for this marker. It also enhanced the baseline production of CEA in the well differentiated cells (DLD-2). Retinoic acid did not induce CEA production in clone D or MIP-101 cells, but did enhance the production of CEA in DLD-2 cells. When both retinoic acid and sodium butyrate were added together, CEA production was either additive (DLD-2) or was inhibited (clone D and MIP-101). One explanation of these results is that only well differentiated cells have functional cellular retinoic acid-binding protein (cRABP), and that certain actions of retinoic acid (inhibition of anchorage-dependent growth) are independent of the presence of cRABP.

Butyrates↗
PubMed1989

Characterization and tumorigenicity of a butyrate-adapted T24 bladder cancer cell line.

We have adapted T24P, a tumorigenic subline of the T24 human bladder cancer cell line, to grow in 5 mM butyrate. In the presence of butyrate, the adapted cells (T24P/B) grow more slowly than the unadapted cells (T24P/C), have a lower saturation density, increased serum requirement for growth, loss of ability to form colonies when plated at low cell density, and decreased ouabain sensitivity. Morphologically, T24P/B cells in butyrate are large and flattened with increased cytoplasm. When T24P/B cells are grown without butyrate, the morphological changes, growth rate, plating efficiency, and ouabain sensitivity return to those of T24P/C. While the saturation density increases, it does not return to levels of T24P/C, and the size of colonies never reaches that of the T24P/C colonies. Both T24P/C and T24P/B are tumorigenic in nude mice, however, the T24P/B tumors differ grossly and microscopically from those produced by T24P/C in that they contain large cystic structures filled with clear fluid and lined by transitional cell epithelium with flattened surface layers. Although the transformed phenotype and tumorigenicity of T24P are modified by adaptation to growth in butyrate, no significant changes in ras oncogene RNA or protein expression were identified.

Acetylation↗