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PubMed1983

Butyrate increases type-A and type-R virus-like particles in BKV-transformed hamster spleen cells.

A cell line derived from hamster spleen transformed by human papovavirus BK was adapted to grow in 5 mM butyrate. Ultrastructurally, the butyrate-adapted cells were found to contain large numbers of type-R and intracytoplasmic type-A virus-like particles (VLP). In contrast, the unadapted cells contained only rare VLP. Treatment of the unadapted cells with nontoxic and toxic concentrations of butyrate for 24 and 48 hr failed to induce VLP, indicating the importance of butyrate adaptation in the induction of VLP. The increase in type-R VLP was stable after removal of the adapted cells from butyrate; however, the increase in type-A VLP was not.

Animals↗
PubMed1989

Effect of experimental azotemia on intestinal transport of butyric acid.

Earlier studies have revealed an impairment of jejunal absorption of long chain fatty acids in experimental uremia. We investigated the intestinal absorption of butyric acid which is a short chain fatty acid in experimental renal failure (RF). Sprague-Dawley rats were randomized into the RF group which had subtotal nephrectomy, a sham-operated control group, and a pair-fed group. In vivo recirculating perfusion (n = 5) and in vitro everted sac incubation (n = 8) were employed. The in vitro experiments were repeated substituting the serosal buffer by either predialysis or postdialysis sera from uremic individuals, or normal serum (n = 10). The rate of in vivo butyric acid absorption was significantly lower while the in vitro absorption was significantly higher in the RF group than those observed in the sham-operated and pair-fed groups which showed comparable values. The normality of butyric acid absorption in the pair-fed animals despite comparable weight loss with the RF group tends to exclude anorexia and weight loss as a cause of altered butyric acid transport in RF animals. The disparity between the in vivo and in vitro data is suggestive of an inhibitory influence of uremic environment which is present in vivo and absent in vitro. This viewpoint was corroborated by the observed fall in butyric acid absorption by sacs containing predialysis uremic serum as compared with those containing normal or postdialysis sera. The latter further suggests that the inhibitory factor(s) is dialyzable.

Animals↗
PubMed1998

Differential effects of sodium butyrate on the transcription of the human TIS11 family of early-response genes in colorectal cancer cells.

The tetradecanoyl phorbol acetate (TPA)-inducible sequence 11 (TIS11) family of early-response proteins consists of at least five members. They share a highly conserved Cys3His zinc-binding motif, but otherwise have little sequence similarity. Their function remains unknown, but all are induced rapidly and transiently in response to extracellular hormone and growth factor signals. Sodium butyrate, a fermentation product of dietary fibre, effects colorectal cancer cell proliferation by inducing growth arrest, differentiation and apoptosis. In this communication, we report that butyrate has differential effects on the transcription of the three human TIS11 family members identified so far in T84 and HT-29 human colorectal cancer cell lines. Butyrate response factor 1 (BRF1) transcription is repressed, butyrate response factor 2 (BRF2) transcription is activated and there is no apparent effect on the transcription of human TIS11 (HTIS11). Induction and repression occur rapidly, with altered mRNA levels detectable within 15 min of butyrate addition. Two other short-chain fatty acids, propionate and acetate, have no detectable effects on BRF1 or BRF2 transcription.

Butyrate Response Factor 1↗
PubMed1992

Effect of sodium butyrate on glucocorticoid-sensitive and -resistant P1798 lymphosarcoma.

This study aims to examine the effect of sodium butyrate on the viability and the level of glucocorticoid receptors and cells cycle progression in glucocorticoid-sensitive and -resistant P1798 cells. Our results indicated that low levels of sodium butyrate had no effect on either the viability or the receptor level. However, high-level (5 mM) sodium butyrate appeared to reduce cell viability as well as the glucocorticoid receptor level. On the other hand, sodium butyrate inhibited cell cycle progression in a dose-dependent manner. This response was similar in both the glucocorticoid-sensitive and -resistant P1798 cells. Results from this study suggested that the sodium butyrate induced effect may be cell cycle related.

Butyrates↗
PubMed1991

Transcriptional regulation and the effects of sodium butyrate and glycosylation on catalytic activity of human germ cell alkaline phosphatase.

Human choriocarcinoma cells, the malignant trophoblasts, synthesize germ cell alkaline phosphatase (GCAP) which shares 98% sequence identity with the placental alkaline phosphatase (AP). The two isozymes are immunologically similar but react differentially toward inhibition by L-leucine or EDTA. Administration of sodium butyrate to choriocarcinoma cells greatly increased the transcription rate of the GCAP gene, resulting in an increase in mRNA expression and enzyme biosynthesis. The butyrate-modulated AP induction was blocked by cycloheximide, suggesting that a mediator protein may be involved. Protein sequence deduced from complementary DNA analysis suggests that GCAP contains two potential sites for asparagine (N)-linked glycosylation. The marked increase in GCAP expression by butyrate in choriocarcinoma cells allowed us to study the extent of N-linked glycosylation and its role on GCAP enzyme activity. After limited tunicamycin treatment, Mr 65,000 (fully processed), Mr 58,000 (nonglycosylated), and Mr 62,000 polypeptides were synthesized by these cells in the presence of butyrate. This suggests that the Mr 62,000 product may be the singly glycosylated GCAP monomer and that both sites are glycosylated in this phosphatase. The glycosylated and nonglycosylated GCAPs, synthesized by butyrate-treated choriocarcinoma cells in the absence or presence of tunicamycin, respectively, were similarly inhibited by L-leucine or EDTA. Moreover, the specific enzyme activity of glycosylated and nonglycosylated GCAP remained unchanged, indicating that AP lacking N-linked oligosaccharide side chains was catalytically active. This is supported by the finding that nonglycosylated GCAP incorporated inorganic phosphate which binds to the active site of AP. Since the active form of AP is a homodimer, our data indicate that the glycan moieties are not required for the dimerization and catalytic activity of GCAP.

Alkaline Phosphatase↗
PubMed1989

Modulation by sodium butyrate of the differentiated status of a clonal pancreatic B-cell line (RIN).

RINmRH cells are a cloned cell line derived from a transplantable rat insulinoma. These cells display only some of the differentiated structure/function features of native pancreatic B-cells. In particular, they do not efficiently or reproducibly express islet B-cell surface antigens, which would otherwise render them useful for screening for the presence of anti-islet cell surface antibodies in the serum of suspected diabetic patients or their relatives. This study examines whether sodium butyrate can enhance expression of B-cell differentiation antigens on RIN cells. RIN cells were exposed to 1,2 or 4 mM butyrate for nine days, and cell growth followed. At 1 mM, butyrate inhibited cell growth by 90%. At the higher concentrations, there was a net loss in the number of cells per culture dish. Exposing the cells to 1 mM or 2 mM butyrate for two days, resulted in a 50% increase in cellular insulin content at the expense of a partial (1 mM) or complete (2 mM) loss of stimulated insulin release in response to glyceraldehyde or serine. A concentration of 1 mM butyrate was therefore used for subsequent studies. The binding to RIN cells of a panel of monoclonal antibodies (mAb's) known to bind native islet cells (R2D6, A2B5, A1D2, 3G5) as well as of serum from a diabetic patient known to carry anti-islet cell antibodies, was screened by cytofluorography or by a radio-binding assay. The relative binding affinity of the mAb's was 3G5 greater than A1D2 greater than A2B5 greater than R2D6. Only 2-3% of the cells were bound by the diabetic patient serum.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1985

Effect of butyrate on the expression of microinjected or transfected genes.

We have studied the effect of sodium n-butyrate on the expression of specific genes. For this purpose, tk-ts13 cells (a thymidine kinase-deficient mutant originating from Syrian hamster cells) were microinjected or transfected with pC2, a plasmid containing the entire SV40 genome and the herpes simplex virus thymidine kinase gene (HSV-TK), cloned in pBR322. As a measure of the expression of these two genes, one of which is spliced (SV40) and the other one (HSV-TK) which is not, we have taken the protein levels (amount of T antigen for SV40 and incorporation of [3H]thymidine for HSV-TK) and the levels of RNA (by dot blot hybridization). The expression of the microinjected genes was inhibited when tk-ts13 cells were exposed to butyrate, actinomycin D, cycloheximide, and mitomycin C, but not when the cells were treated with insulin or dexamethasone. Further studies showed that a decrease in the percentage of T-positive cells occurs at lower concentrations of butyrate than a decrease in the levels of specific mRNA. In tk-ts13 cells transfected with pC2 and treated with butyrate at a concentration of 3 mM, SV40 mRNA levels are not decreased but the percentage of T-positive cells is decreased 50%. At 5 mM, the amount of T antigen/cell is decreased a further 40%. These results indicate that butyrate may have at least two sites of action, one at the level of mRNA amount and a second at the level of protein amount. In addition, our studies show that the use of microinjected or transfected genes offers certain unique possibilities for studies on the effects of environmental manipulations on gene expression.

Antigens, Viral, Tumor↗
PubMed1986

Emergence of differentiated subclones from a human salivary adenocarcinoma cell clone in culture after treatment with sodium butyrate.

A human salivary gland adenocarcinoma cell line, which has ultrastructure and biological markers specific to the intercalated duct cells of human salivary glands, was cultured in 5 mM sodium butyrate for 12 days; then the cells were trypsinized, subcultured for an additional 16 days, and then transferred to growth medium without sodium butyrate. Morphological changes appeared about 1 wk after return to growth medium without sodium butyrate; cells being spindle or stellate in shape appeared in the treated cells, whereas the untreated cells were polygonal in shape. This morphologically altered phenotype persists after more than 14 mo of culture in growth medium without sodium butyrate. Of 40 subclones isolated, 2 clonal cell lines were established from the subculture and characterized. The other 38 subclones were accompanied by cell death during the subcultures. The clonal lines exhibited a phenotype similar to myoepithelial cells such as myosin, beta-chain of S-100 protein, myofilaments, and oxytocin receptor in addition to decreased tumorigenicity and anchorage-independent growth. These findings indicate that commitment to differentiation into myoepithelial cells and conversion from malignant to normal phenotype occur in a human salivary gland adenocarcinoma cell line following the sodium butyrate treatment.

Adenocarcinoma↗
PubMed1988

Effect of sodium butyrate and other differentiation inducers on poorly differentiated human ovarian adenocarcinoma cell lines.

We have studied the effects of sodium butyrate, retinoic acid, and dimethyl sulfoxide on two human ovarian carcinoma cell lines PE04 and PE01. PE04 cells, after treatment with sodium butyrate at cytostatic doses (2-3 mM for 4 days), exhibited phenotypic changes including induction of alkaline phosphatase and determinants recognized by the monoclonal antibodies 123C3 and 123A8. These effects are not simply the result of cytostasis as they were not produced by dimethyl sulfoxide or retinoic acid. Other markers are also modified by sodium butyrate including lipid, acid mucin, and glycogen. Retinoic acid modulated expression of lipid and CA125, while dimethyl sulfoxide reduced expression of CA125. Other short chain fatty acids such as propionic acid and valeric acid (in addition to butyric acid) also induced alkaline phosphatase and the determinants recognized by 123C3 and 123A8 in PE04 cells. Other differentiation inducers and cytotoxic agents studied did not induce these markers at cytostatic concentrations. The effects of sodium butyrate (and related short chain fatty acids) thus appear to be relatively specific for this cell line.

Adenocarcinoma↗
PubMed1988

Effects of sodium butyrate and 3-aminobenzamide on survival of Chinese hamster HA-1 cells after X irradiation.

HA-1 cells were grown in medium containing 2 mM sodium butyrate and then exposed to graded doses of 250 kVp X rays. After irradiation, some of the butyrate-treated cultures were treated with either 10 or 20 mM 3-aminobenzamide for 2 h at 37 degrees C. The butyrate treatment produced a small degree of radiation sensitization as indicated by an increase in the alpha parameter using a linear-quadratic description of survival responses. The dose-modifying factor at the 10% survival level (DMF10) was 1.15. Similarly, both 10 and 20 mM 3-aminobenzamide treatments produced concentration-dependent increases in radiosensitization, again as indicated by an increase in the value of the alpha constant, with DMF10 values of 1.22 and 1.40, respectively. However, the combination of the 2 mM sodium butyrate + 10 mM 3-aminobenzamide treatments produced a supraadditive response in terms of increased cell killing (DMF10 = 1.76). We interpret this to mean that 3-aminobenzamide inhibits a sodium butyrate associated increase in poly(ADP-ribose) which then predisposes hyperacetylated chromatin to attack by endogenous nucleases leading to increased cytotoxicity.

Animals↗
PubMed1988

Age-dependent effects of sodium butyrate and hydrocortisone on acetylation of high mobility group proteins of rat liver.

The in vitro acetylation of high mobility group (HMG) proteins and its modulation by sodium butyrate and hydrocortisone have been studied using liver slices of young (13-) and old (114-week-old) rats. Acetylation of total HMG proteins was significantly higher in young than old rats. HMG 1, in particular, showed greater acetylation than others. Whereas acetylation of HMG 1 and 2 decreased drastically, that of HMG 14 and 17 increased in old age. In young rats, sodium butyrate and hydrocortisone stimulated acetylation of HMG 14 and 17, and decreased that of HMG 2. Butyrate had no effect on HMG 1, but hydrocortisone decreased it. In old rats, butyrate and hydrocortisone decreased acetylation of all HMGs, except HMG 17, which was stimulated to a slight extent by butyrate.

Acetylation↗
PubMed1984

Sodium butyrate induction of milk-related antigens in human MCF-7 breast carcinoma cells.

We have monitored the effects of sodium butyrate on expression of a human breast tumor-associated antigen defined by a murine monoclonal antibody designated DF3. This cell surface antigen has a molecular weight of approximately 300,000 and is related to a higher-molecular-weight antigen detectable in human milk. The results demonstrate that butyrate increases the membrane expression of the DF3 tumor-associated antigen. Further, butyrate treatment specifically enhances production of the DF3-related milk antigen. These effects occur at butyrate concentrations lower than that required for maximal expression of carcinoembryonic antigen and occur in the absence of changes in the expression of nonspecific cross-reacting antigen. The results suggest that butyrate induces a more differentiated MCF-7 phenotype and that this model may be useful in studying maturation of human breast cancer cells.

Antibodies, Monoclonal↗
PubMed1984

Effects of butyrate, retinol, and retinoic acid on human Y-79 retinoblastoma cells growing in monolayer cultures.

The effects of butyrate, retinol, and retinoic acid were tested on growth and differentiation of human Y-79 retinoblastoma cells in monolayer cultures. Treatment with 4 mM butyrate resulted in marked growth inhibition of cells, due mostly to increased death rate. The effect was greater in serum-supported cultures in which the proliferation rate was high and the effect was less in the serum-free, defined medium in which the cells were differentiated and the growth rate was slow, suggesting a cell-cycle-specific action of this substance. Moreover, butyrate induced morphologic changes in the viable cells; these changes consisted of an elongated appearance of the cells and of retraction of long processes formed in the serum-free-supported cultures. Retinol at 20 microM also affected the cell viability both in serum-containing and in serum-free culture medium. Retinoic acid at 50 microM induced reversible growth inhibition of cells growing in serum-containing medium and cell death in the defined medium-supported cultures. Combination of 0.5 mM butyrate with 50 microM retinoic acid resulted in an enhanced inhibition of growth in an apparently synergistic fashion. These results demonstrated that butyrate, retinol, and retinoic acid suppressed Y-79 cell growth in vitro and could be useful in future studies of these compounds in retinoblastoma tumors in vivo.

Butyrates↗
PubMed1982

Histone hypoacetylation following release of HTC cells from butyrate.

Exposure of HTC cells to 6 mM sodium butyrate for 20 h results in significantly reduced amounts of nuclear histone acetyltransferase. While the direct butyrate inhibition of histone deacetylases is rapidly reversed upon removal of cells from butyrate, histone acetyltransferase activity increases only gradually following release of cells from butyrate, requiring several hours to regain control cell levels. As a result, HTC cells released from a 20-h exposure to butyrate display normal kinetics of histone acetate turnover but markedly reduced rates of histone acetylation, the imbalance in these two processes produces histone hypoacetylation.

Acetylation↗
PubMed1982

Effect of sodium butyrate on alkaline phosphatase in HRT-18, a human rectal cancer cell line.

Treatment of the human rectal cancer cell line HRT-18 with sodium butyrate caused a reversible elevation of alkaline phosphatase activity which was inhibited by cycloheximide and actinomycin D. The alkaline phosphatase in untreated cells was heat stable at neutral pH and inhibited by phenylalanine but not by homoarginine, and 80% of the enzyme activity was precipitated by antibody against human term-placental enzyme. Following butyrate treatment, the enzyme became more sensitive to all the inhibitors tested and more heat stable, compared to the enzyme in control cells. In addition, the butyrate-induced enzyme could be completely precipitated by anti-placental alkaline phosphatase antibody. The electrophoretic pattern of the butyrate-induced enzyme was different from that of control cells. Control HRT-18 cells contained a butyrate-insensitive heat-labile alkaline phosphatase component with an electrophoretic mobility similar to the enzyme from human colon cancer tissues. The alkaline phosphatase from four human colon cancer tissues was of the early placental form, while the enzyme from human normal mucosa was of the intestinal type.

Alkaline Phosphatase↗
PubMed1994

Transcriptional modulation by n-butyric acid of beta 1-, beta 2-, and beta 3-adrenergic receptor balance in 3T3-F442A adipocytes.

3T3-F442A adipocytes, which express major beta 3-adrenergic receptors (beta 3-AR) (90%) and minor beta 1-AR (< 10%) and beta 2-AR (< 1%) populations, were used to investigate regulation by n-butyric acid of beta-AR subtype expression. Following butyrate treatment, EC50 values of beta 1- and beta 2-selective agonists, dobutamine and fenoterol, were decreased, whereas that of the beta 3-selective agonist BRL37344 was increased. Direct binding and competition of (-)-[125I]iodocyanopindolol binding by selective beta 1- and beta 2-AR antagonists, CGP20712A and ICI118551, and by the beta 3-AR agonist, BRL37344, revealed that both beta 1- and beta 2-AR were increased in butyrate-treated adipocytes, whereas beta 3-AR almost totally disappeared. In control adipocytes, beta 1-, beta 2-, and beta 3-AR transcripts (quantitated by a polymerase chain reaction assay) represented 6.5, 0.5, and 93% of total beta-AR mRNA, respectively. In butyrate-exposed cells, proportions of beta-AR proteins and mRNAs were, respectively, 87 and 94% for beta 1 and 9 and 1% for beta 2-AR. beta 3-ARs were barely detectable in binding assays and accounted for 4.5% of beta-AR transcripts. Variations of beta-AR protein and mRNA levels were accompanied by parallel changes in the transcription rates of the corresponding genes. The differential regulation of the three beta-ARs by n-butyric acid, a dietary factor produced from colonic fermentation, may have significant nutritional and energetic consequences.

3T3 Cells↗
PubMed1993

Effects of sodium butyrate, dimethylsulfoxide and dibutyryl cAMP on the poorly differentiated ovarian adenocarcinoma cell line AMOC-2.

To determine whether the poorly differentiated AMOC-2 human ovarian adenocarcinoma cell line was capable of undergoing differentiation, AMOC-2 cells were exposed to 2 mM sodium butyrate, 2.5% dimethylsulfoxide, or 4 mM dibutyryl cyclic adenosine monophosphate (dibutyryl cAMP) for 6 days. These treatments resulted in growth inhibition, a reduction in clonogenicity and an increase in cellular glycogen content. Significant increases in heat stable alkaline phosphatase activity also occurred after exposure to sodium butyrate. In addition, a thorn-like microfilament structure observed in untreated cells was diminished concomitantly with morphological changes that included flattening, enlargement and extended cytoplasmic processes after exposure to sodium butyrate or dibutyryl cAMP. Furthermore, treatment with sodium butyrate increased the intracellular concentrations of beta-tubulin, vimentin, neurofilaments (M(r) 210,000) and cytokeratin (M(r) 56,000-58,000). These changes were completely reversed after removal of the inducing agent. The findings suggest that treatment of AMOC-2 cells with sodium butyrate induced a more differentiated phenotype, although terminal differentiation was not achieved.

Adenocarcinoma↗
PubMed1983

Effect of polar organic compounds on leukemic cells. Butyrate-induced partial remission of acute myelogenous leukemia in a child.

Polar organic compounds, such as dimethylsulfoxide and butyric acid, are known to induce differentiation in Friend erythroleukemia cells as well as in other cell types. It has been found that many of the compounds that induce cellular differentiation, inhibit 3H-thymidine incorporation and induce cell damage when incubated with leukemic cells from patients with acute or chronic myelogenous or acute lymphocytic leukemia. These effects are time and dose dependent. Among the compounds tested, butyrate was the most potent. Parenteral administration of butyrate (500 mg/kg/day) for ten days to a child with acute myelogenous leukemia in relapse, and resistant to conventional therapy, resulted in elimination of myeloblasts from the peripheral blood, an increase in mature myeloid cells and a reduction in 3H-thymidine uptake by the patient's peripheral blood cells. Bone marrow myeloblasts were reduced from 70-80% to 20% following the course of intravenous butyrate. No impairment of liver or renal function and no coagulation abnormalities were observed during butyrate treatment. Organic agents that induce cell differentiation may provide additional reagents for the clinical management of selected cases of leukemia.

Adult↗