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At least 307 records · Page 17Linked to original sources
PubMed2005

Upregulation of 25-hydroxyvitamin D(3)-1(alpha)-hydroxylase by butyrate in Caco-2 cells.

AIM: To investigate the possible involvement of 25-hydroxyvitamin D(3)-1(alpha)-hydroxylase [1alpha-25(OH) (2) D(3)] in butyrate-induced differentiation in human intestinal cell line Caco-2 cells. METHODS: Caco-2 cells were incubated either with 3 mmol/L butyrate and 1 micromol/L 25(OH) (2) D(3) or with 1 micromol/L 1alpha-25(OH) (2) D(3) for various time intervals ranging from 0 to 72 h. Additionally, cells were co-incubated with butyrate and either 25(OH) (2) D(3) or 1alpha-25(OH) (2) D(3). 1alpha-25(OH) (2) D(3) mRNA was determined semi-quantitatively using the fluorescent dye PicoGreen. Immunoblotting was used for the detection of 1alpha-25(OH) (2) D(3) protein. Finally, enzymatic activity was measured by ELISA. RESULTS: Both butyrate and 1alpha-25(OH) (2) D(3) stimulated differentiation of Caco-2 cells after a 48 h incubation period, while 25(OH) (2) D(3) had no impact on cell differentiation. Synergistic effects on differentiation were observed when cells were co-incubated with butyrate and vitamin D metabolite. Butyrate transiently upregulated 1alpha-25(OH) (2) D(3) mRNA followed by a timely delayed protein upregulation. Coincidently, enzymatic activity was enhanced significantly. The induction of the enzyme allowed for comparable differentiating effects of both vitamin D metabolites. CONCLUSION: Our experimental data provide a further mechanism for the involvement of the vitamin D signaling pathway in colonic epithelial cell differentiation by butyrate. The enhancement of 1alpha-25(OH) (2) D(3) followed by antiproliferative effects of the vitamin D prohormone in the Caco-2 cell line suggest that 25(OH) (2) D(3) in combination with butyrate may offer a new therapeutic approach for the treatment of colon cancer.

25-Hydroxyvitamin D3 1-alpha-Hydroxylase↗
PubMed2006

Effects of tachyplesin and n-sodium butyrate on proliferation and gene expression of human gastric adenocarcinoma cell line BGC-823.

AIM: To investigate the effects of tachyplesin and n-sodium butyrate on proliferation and gene expression of human gastric adenocarcinoma cell line BGC-823. METHODS: Effects of tachyplesin and n-sodium butyrate on proliferation of BGC-823 cells were determined with trypan blue dye exclusion test and HE staining. Effects of tachyplesin and n-sodium butyrate on cell cycle were detected by flow cytometry. Protein levels of c-erbB-2, c-myc, p53 and p16 were examined by immunocytochemistry. RESULTS: The inhibiting effects were similar after 2.0 mg/L tachyplesin and 2.0 mmol/L n-sodium butyrate treatment, the inhibitory rate of cellular growth was 62.66% and 60.19% respectively, and the respective maximum mitotic index was decreased by 49.35% and 51.69% respectively. Tachyplesin and n-sodium butyrate treatment could markedly increase the proportion of cells at G(0)/G(1) phase and decrease the proportion at S phase. The expression levels of oncogene c-erbB-2, c-myc, and mtp53 proteins were down-regulated while the expression level of tumor suppressor gene p16 protein was up-regulated after the treatment with tachyplesin or n-sodium butyrate. The effects of 1.0 mg/L tachyplesin in combination with 1.0 mmol/L n-sodium butyrate were obviously superior to their individual treatment in changing cell cycle distribution and expression of c-erbB-2, c-myc, mtp53 and p16 protein. The inhibitory rate of cellular growth of BGC-823 cells after combination treatment was 62.29% and the maximum mitotic index was decreased by 51.95%. CONCLUSION: Tachyplesin as a differentiation inducer of tumor cells has similar effects as n-sodium butyrate on proliferation of tumor cells, expression of correlative oncogene and tumor suppressor gene. It also has a synergistic effect on differentiation of tumor cells.

Adenocarcinoma↗
PubMed1999

Sustained induction of fetal hemoglobin by pulse butyrate therapy in sickle cell disease.

High levels of fetal hemoglobin (Hb F) protect from many of the complications of sickle cell disease and lead to improved survival. Butyrate and other short chain fatty acids were previously shown to increase Hb F production in erythroid cells in vitro and in animal models in vivo. However, butyrates are also known to inhibit the proliferation of many cell types, including erythroid cells. Experience with the use of butyrate in animal models and in early clinical trials demonstrated that the Hb F response may be lost after prolonged administration of high doses of butyrate. We hypothesized that this loss of response may be a result of the antiproliferative effects of butyrate. We designed a regimen consisting of intermittent or pulse therapy in which butyrate was administered for 4 days followed by 10 to 24 days with no drug exposure. This pulse regimen induced fetal globin gene expression in 9 of 11 patients. The mean Hb F in this group increased from 7.2% to 21.0% (P <.002) after intermittent butyrate therapy for a mean duration of 29.9 weeks. This was associated with a parallel increase in the number of F cells and F reticulocytes. The total hemoglobin levels also increased from a mean of 7.8 g/dL to a mean of 8.8 g/dL (P <.006). The increased levels of Hb F were sustained in all responders, including 1 patient who has been on pulse butyrate therapy for more than 28 months. This regimen, which resulted in a marked and sustained increase in Hb F levels in more than two thirds of the adult sickle cell patients enrolled in this study, was well tolerated without adverse side effects. These encouraging results require confirmation along with an appropriate evaluation of clinical outcomes in a larger number of patients with sickle cell disease.

Adolescent↗
PubMed2000

Butyrate-induced erythroid differentiation of human K562 leukemia cells involves inhibition of ERK and activation of p38 MAP kinase pathways.

Butyrate induces cytodifferentiation in many tumor cells of different origin, suggesting that an as yet unidentified common mechanism inherent to malignant cells is the target of butyrate action. This study determined the role of different mitogen-activated protein (MAP) kinase signal transduction pathways in butyrate-induced erythroid differentiation of K562 human leukemia cells. Using a panel of anti-ERK, JNK, and p38 phosphospecific antibodies, the study showed that phosphorylation of ERK and JNK is decreased following treatment of cells with butyrate, whereas phosphorylation of p38 is increased. In contrast, a K562 subline defective in butyrate-mediated induction of erythroid differentiation did not reveal these changes in phosphorylation patterns. Inhibition of ERK activity by UO126 induces erythroid differentiation and acts synergistically with butyrate on hemoglobin synthesis and inhibition of cell proliferation, whereas inhibition of p38 activity by SB203580 completely abolished induction of hemoglobin expression by butyrate. Taken together, our data suggest a model in which butyrate induces erythroid differentiation of K562 cells by inhibition of ERK and activation of p38 signal transduction pathways.

Butyrates↗
PubMed2000

The inhibitory action of butyrate on lipopolysaccharide-induced nitric oxide production in RAW 264.7 murine macrophage cells.

The effect of butyrate, a natural bacterial product of colonic bacterial flora, on lipopolysaccharide (LPS)-induced nitric oxide (NO) production in RAW 264.7 murine macrophage cells was studied. Butyrate significantly reduced NO production in LPS-stimulated RAW cells. The inhibition was abolished by the removal of butyrate. Butyrate also inhibited the expression of inducible type NO synthase (iNOS) in LPS-stimulated RAW cells. Furthermore, butyrate prevented the activation of nuclear factor (NF)-kappaB through the stabilization of IkappaB-alpha and IkappaB-beta. Butyrate did not affect the phosphorylation of mitogen-activated protein (MAP) kinases by LPS. It was, therefore, suggested that butyrate down-regulated LPS-induced NO production in RAW cells through preventing the expression of iNOS, and that it was due to the inhibitory action of butyrate on the activation of NF-kappaB.

Animals↗
PubMed2000

Potato and high-amylose maize starches are not equivalent producers of butyrate for the colonic mucosa.

Portal appearance of short-chain fatty acids (SCFA) produced from fermentation of three different resistant starch (RS) sources (raw potato starch, high-amylose maize starch and retrograded high-amylose maize starch) was investigated in pigs. The catheterization technique coupled with determination of portal blood flow was used to estimate SCFA uptake by the colonic mucosa. Our hypothesis was that these three RS were not equivalent butyrate providers for the colonic mucosa and that butyrate uptake would therefore be different after in vivo fermentation of each starch. The starches induced different patterns of appearance of SCFA in the portal blood; raw potato starch was the only RS source to show a significant appearance of butyrate in the portal blood. Thus, uptake of butyrate by the colonic mucosa apparently differed between starches. This finding suggests that butyrate uptake does not only depend on the flow of butyrate appearing in the lumen. Indeed, for unexplained reasons, utilization of butyrate by the colonic mucosa appeared to be less efficient when the butyrate was produced from fermentation of potato starch than when it was produced from fermentation of the other RS sources.

Amylose↗
PubMed2003

Inhibition of interferon gamma signaling by the short chain fatty acid butyrate.

The short chain fatty acid butyrate promotes proliferation and survival of normal epithelial cells, but induces G(1) or G(2)-M arrest in transformed cells, which is coupled to differentiation and apoptosis. Local administration of butyrate has been shown to ameliorate inflammation in ulcerative colitis; however, the precise mechanism of its anti-inflammatory activity is not known. IFN-gamma is one of the principle cytokines secreted by lamina propria cells in inflamed mucosa and elevated levels of the transcription factor required for IFN-gamma signaling, STAT1 (signal transducer and activator of transcription 1), are present in the colonic mucosa of patients with ulcerative colitis and Crohn's disease. Here we report that butyrate is a strong inhibitor of signaling by IFN-gamma. We demonstrated that this short chain fatty acid inhibits IFN-gamma-induced tyrosine and serine phosphorylation of STAT1. IFN-gamma-induced JAK2 activation was inhibited by butyrate, implicating JAK2 as a target of butyrate action. Accordingly, STAT1 nuclear translocation and its DNA binding were completely inhibited in butyrate-treated cells. Transient transfection experiments using a reporter gene construct containing eight GAS sites (gamma-activated sites) revealed that butyrate inhibits IFN-gamma induced, STAT1-dependent, transcriptional activation. Proinflammatory cytokines, including IFN-gamma, play an important role in the pathogenesis of inflammatory bowel disease, and abnormal activity of STAT1 is associated with human malignancies and intestinal inflammatory diseases. Thus, our data suggest that butyrate negatively regulates mucosal inflammation through the inhibition of IFN-gamma/STAT1 signaling.

Butyrates↗
PubMed2004

[Influence of sodium butyrate on growth of HT-29 colon carcinoma cells and expression of inducible nitric oxide synthase (iNOS)].

BACKGROUND & OBJECTIVE: Sodium butyrate could inhibit several cancer cell lines in vitro. This study was designed to investigate the effects of sodium butyrate on the growth of HT-29 colon carcinoma cells, the expression of iNOS, and the excretion of NO. METHODS: The HT-29 cells were co-incubated with sodium butyrate at various concentration. The cell proliferation was determined by MTT test, and the iNOS protein of HT-29 cells was stained by immunochemical SP method. The absorbance value (A value) of iNOS was measured by automatic image analysis system. Griess's technique was used to examine the excretion of nitric oxide (NO). RESULTS: The survival rates of HT-29 cells treated by sodium butyrate decreased in a time-dependent and dose-dependent manner. IC(50) value of sodium butyrate was decreased with prolonged incubation time (15.4 mmol/L at 12 hours, 5.7 mmol/L at 24 hours, 2.5 mmol/L at 36 hours, 0.9 mmol/L at 48 hours). Simultaneously sodium butyrate decreased the expression of iNOS in the cytoplasm and the excretion of NO in a similar manner. CONCLUSION: Sodium butyrate could inhibit the expression of iNOS, consequently reduce the excretion of NO. It may play an important role in the mechanism that sodium butyrate inhibits the growth of HT-29 colon carcinoma cells.

Butyrates↗
PubMed2004

Effect of sodium butyrate on the small intestine development in neonatal piglets fed [correction of feed] by artificial sow.

Feeding of neonates with artificial milk formulas delays the maturation of the gastrointestinal mucosa. Na-butyrate has a complex trophic effect on the gastrointestinal epithelium in adults. The present study aimed to determine the effect of milk formula supplementation with Na-butyrate on the gut mucosa in neonatal piglets. Sixteen 3 day old piglets were randomly divided into two groups: control (C, n = 8), and Na-butyrate (B, n = 8). Animals were feed for 7 days with artificial milk formula alone (C) or supplemented with Na-butyrate (B). At the 10(th) day of life the piglets were sacrificed and whole thickness samples of the upper gut were taken for analyses. Administration of Na-butyrate led to significant increase in daily body weight gain as compared to control. In the duodenum, the villi length and mucosa thickness were reduced, however, in the distal jejunum and ileum, the crypt depth, villi length and mucosa thickness were increased in Na-butyrate supplemented piglets as compared to control. Supplementation with Na-butyrate did not affect the intestinal brush border enzyme activities but increased plasma pancreatic polypeptide and cholecystokinin concentrations. These results suggest that supplementation with Na-butyrate may enhance the development of jejunal and ileal mucosa in formula-fed piglets.

Animals↗
PubMed2006

Butyrate sensitizes the release of substance P and calcitonin gene-related peptide evoked by capsaicin from primary cultured rat dorsal root ganglion neurons.

OBJECTIVES: To investigate whether butyrate increases substance P (SP) and calcitonin gene-related peptide (CGRP) release evoked by capsaicin from primary cultured dorsal root ganglion (DRG) neurons. METHODS: DRG was dissected out from embryonic 15-day-old Wistar rat and cultured as dissociate cells for 24 h then exposed to butyrate (0.01 mmol/L, 0.1 mmol/L, 1 mmol/L, 10 mmol/L, respectively) for another 48 h. The neurons cultured continuously in media served as normal control. All above cultured samples were processed for detecting expression of mRNA for SP, CGRP and vanilloid receptor 1 (VR1) of DRG neurons by RT-PCR, and VR1 protein expression by Western blot. SP and CGRP basal release levels were measured by radioimmunoassay (RIA). After that, the DRG cells for RIA were stimulated by capsaicin (300 nmol/L) for 5 min and the culture media were harvested for detecting SP and CGRP release levels by RIA. The neurons exposed to vehicle solution served as vehicle controls. RESULTS: Exposure of butyrate on DRG neurons at higher concentrations (1 mmol/L, 10 mmol/L) for 48 h increased expression mRNA for SP and CGRP than that at lower concentrations (0.01 mmol/L, 0.1 mmol/L) and normal control (P<0.001). VR1 mRNA and VR1 protein expression increased in a dose-dependent manner after exposure of different concentrations of butyrate. Butyrate did not alter the basal release, significantly enhanced neuropeptide release evoked by capsaicin. SP and CGRP release levels in the culture media exposed by butyrate at higher concentrations (1 mmol/L, 10 mmol/L) for 48 h and then stimulated by capsaicin were higher than that at lower concentrations (0.01 mmol/L, 0.1 mmol/L) (P<0.001). The exposure of vehicle solution did not produce any increase of SP and CGRP release from primary cultured DRG neurons. DISCUSSION: Butyrate may promote the expression of mRNA for SP, CGRP and increase sensitivity of capsaicin on SP and CGRP release from primary cultured rat dorsal root ganglion neurons. The promotion of VR1 mRNA and VR1 protein expression by butyrate implicated that VR1 may be involved in the mechanisms of sensory neuropeptide release evoked by capsaicin.

Animals↗
PubMed1990

[Subacute butyric acid exposure in cattle. 4. Clinical influence and effect on the carbohydrate-fat metabolism and liver function of cows].

Eleven cows in late lactation were exposed to butyric acid for three weeks and were compared to five controls. Two intraruminal doses were daily applied, that is 1.0 g/kg B.W. of butyric acid to six animals and 1.0 g/kg B.W. of sodium butyrate to another five. Decline in milk yield was clinically recorded in response to butyric acid, while muscle tremor and diarrhoea resulted additionally from sodium butyrate. Behaviours of the clinico-chemical parameters of beta-OH-butyrate, glucose, free fatty acids, bilirubin, ASAT, gamma-GT, AP, and cholesterol were comparable to those in fattening bulls. Liver damage was not safely established. Some of the clinico-chemical alterations were more strongly pronounced after administration of sodium butyrate. One cow fell ill with ketosis under butyric acid load.

Animals↗
PubMed1989

Effect of intraruminal butyrate infusion on the plasma insulin level in sheep.

After intraruminal infusion of butyrate to sheep at dose rates of 0.25, 0.5, 1 and 2 g sodium n-butyrate per kg body mass, butyrate concentration of the rumen fluid and total secreted insulin rose in direct proportion to the butyrate dose infused. The half-life of butyrate in the rumen was always longer than that of insulin. At 90 min after the infusion of 1 g butyrate per kg body mass, butyrate concentration in the ruminal papillae reached the level corresponding to an extracellular concentration that reduced cell division by 50% in vitro. It can be concluded that butyrate may be present in the ruminal papillae in concentrations inhibiting cell proliferation, simultaneously with the presence of blood plasma insulin concentrations stimulating the proliferation of ruminal epithelial cells.

Animals↗
PubMed1981

Induction of prostacyclin formation by sodium n-butyrate in a cloned epithelial liver cell line.

The effect of sodium n-butyrate on prostaglandin synthesis in cultured cells was examined. Exposure of BC-90 cells, a clone of an epithelial rat liver cell line, to 1 mM sodium n-butyrate for 40 h induced prostacyclin production. Prostacyclin synthesis was proved by demonstrating: (1) production of labeled 6-ketoprostaglandin F1 alpha by treating [14C]arachidonic acid pre-labeled cells with calcium ionophore A23187, (2) production of unstable substance that inhibited adenosine diphosphate-induced platelet aggregation, and (3) conversion of [14C]arachidonic acid to 6-ketoprostaglandin F1 alpha in homogenates of n-butyrate-treated cells. Untreated control cells showed negligible prostaglandin synthesis. Untreated cell homogenates did not convert [14C]arachidonic acid to any prostaglandins, but they converted [14C]prostaglandin H2 to prostacyclin. Induction of prostacyclin production by n-butyrate was also demonstrated with cells that had been treated with acetylsalicylic acid before n-butyrate treatment in acetylsalicylic acid-free medium. Incorporation of [3H]acetylsalicylic acid by sodium n-butyrate-treated cells increased in accordance with treatment time, while that of untreated cells did not change during culture. There was no difference in the phospholipase A2 activities of n-butyrate-treated and -untreated cells. From these findings, the possibility that n-butyrate induced prostacyclin in BC-90 cells through induction of fatty acid cyclooxygenase activity is discussed.

6-Ketoprostaglandin F1 alpha↗
PubMed1988

Reductive carboxylation of propionate to butyrate in methanogenic ecosystems.

During the batch degradation of sodium propionate by the anaerobic sludge from an industrial digestor, we observed a significant amount of butyrate formation. Varying the initial propionate concentrations did not alter the ratio of maximal butyrate accumulation to initial propionate concentration within a large range. By measuring the decrease in the radioactivity of [1-C]butyrate during propionate degradation, we estimated that about 20% of the propionate was converted to butyrate. Labeled butyrate was formed from [1-C]propionate with the same specific radioactivity, suggesting a possible direct pathway from propionate to butyrate. We confirmed this hypothesis by nuclear magnetic resonance studies with [C]propionate. The results showed that [1-C]-, [2-C]-, and [3-C]propionate were converted to [2-C]-, [3-C]-, and [4-C]butyrate, respectively, demonstrating the direct carboxylation on the carboxyl group of propionate without randomization of the other two carbons. In addition, we observed an exchange reaction between C-2 and C-3 of the propionate, indicating that acetogensis may proceed through a randomizing pathway. The physiological significance and importance of various metabolic pathways involved in propionate degradation are discussed, and an unusual pathway of butyrate synthesis is proposed.

Journal Article↗
PubMed1988

Bioenergetic conditions of butyrate metabolism by a syntrophic, anaerobic bacterium in coculture with hydrogen-oxidizing methanogenic and sulfidogenic bacteria.

The butyrate-oxidizing, proton-reducing, obligately anaerobic bacterium NSF-2 was grown in batch cocultures with either the hydrogen-oxidizing bacterium Methanospirillum hungatei PM-1 or Desulfovibrio sp. strain PS-1. Metabolism of butyrate occurred in two phases. The first phase exhibited exponential growth kinetics (phase a) and had a doubling time of 10 h. This value was independent of whether NSF-2 was cultured with a methanogen or a sulfate reducer and likely represents the maximum specific growth rate of NSF-2. This exponential growth phase was followed by a second phase with a nearly constant rate of degradation (phase b) which dominated the time course of butyrate degradation. The specific activity of H(2) uptake by the hydrogen-oxidizing bacterium controlled the bioenergetic conditions of metabolism in phase b. During this phase both the Gibbs free energy (DeltaG') and the butyrate degradation rate (v) were greater for NSF-2-Desulfovibrio sp. strain PS-1 (DeltaG' = -17.0 kJ/mol; v = 0.20 mM/h) than for NSF-2-M. hungatei PM-1 (DeltaG' = -3.8 kJ/mol, v = 0.12 mM/h). The DeltaG' value remained stable and characteristic of the two hydrogen oxidizers during phase b. The stable DeltaG' resulted from the close coupling of the rates of butyrate and H(2) oxidation. The addition of 2-bromoethanesulfonate to a NSF-2-methanogen coculture resulted in the total inhibition of butyrate degradation; the inhibition was relieved when Desulfovibrio sp. strain PS-1 was added as a new H(2) sink. When the specific activity of H(2) consumption was increased by adding higher densities of the Desulfovibrio sp. to 2-bromoethanesulfonate-inhibited NSF-2-methanogen cocultures, lower H(2) pool sizes and higher rates of butyrate degradation resulted. Thus, it is the kinetic parameters of H(2) consumption, not the type of H(2) consumer per se, that establishes the thermodynamic conditions which in turn control the rate of fatty acid degradation. The bioenergetic homeostasis we observed in phase b was a result of the kinetics of the coculture members and the feedback inhibition by hydrogen which prevents butyrate degradation rates from reaching their theoretical V(max).

Journal Article↗
PubMed1995

Effects of butyrate and glucocorticoids on gamma- to beta-globin gene switching in somatic cell hybrids.

Butyrate and its analogs have been shown to induce fetal hemoglobin in humans and primates and in erythroid cell cultures. To obtain insights concerning the cellular mechanisms of butyrate action, we analyzed the effects of butyrate on human globin gene expression in hybrids produced by fusing mouse erythroleukemia cells (MEL) with human fetal erythroid cells (HFE). These hybrids initially express human fetal hemoglobin but subsequently switch to adult globin expression after several weeks in culture. We found that alpha-aminobutyric acid, a butyrate analog which does not induce terminal maturation, strikingly delays the rate of the gamma- to beta-globin gene (gamma-to-beta) switch in the HFE x MEL hybrids. The effect of butyrate on globin expression is transient, with the result that the delay of globin gene switching requires the continuous presence of this compound in culture. Furthermore, butyrate fails to induce fetal hemoglobin expression in hybrids which have switched, suggesting that the effect of this compound on gamma-globin expression is due to inhibition of gamma gene silencing rather than to induction of gamma gene transcription. Since in other cellular systems, glucocorticoids antagonize the action of butyrate, the effect of dexamethasone on the gamma-to-beta switch in HFE x MEL hybrids was examined. Dexamethasone strikingly accelerated the gamma-to-beta switch, and its effect was irreversible. The effects of dexamethasone and butyrate on the gamma-to-beta switch of the HFE x MEL hybrids appear to be codominant. These results indicate that steroids can have a direct effect on globin gene switching in erythroid cells.

Aminobutyrates↗
PubMed1998

Butyrate enhances interleukin (IL)-8 secretion by intestinal epithelial cells in response to IL-1beta and lipopolysaccharide.

Intestinal epithelial (Caco-2) cells secrete the chemokine, IL-8, after stimulation with IL-1beta, but not after lipopolysaccharide. Butyrate is a short chain fatty acid derived from the metabolism of intestinal contents by gut bacteria. Butyrate concentrations reflect, therefore, the bacterial microenvironment established within the intestine. We hypothesized that butyrate may alter the secretion of IL-8 by intestinal epithelial cells in response to stimulation by IL-1beta or lipopolysaccharide. Caco-2 cells were incubated in varying concentrations of sodium butyrate (0-20 mM) for 24 h before stimulation with lipopolysaccharide or IL-1beta. IL-8 secretion was measured over 24 h by ELISA. IL-8 mRNA accumulation was detected by Northern blots. Lipopolysaccharide induced the secretion of IL-8 only after Caco-2 cells cells had been cultured with sodium butyrate. Furthermore, butyrate significantly enhanced IL-8 secretion by cells stimulated with IL-1beta. Butyrate also increased IL-8 mRNA accumulation in stimulated Caco-2 cells. Intestinal epithelial cells can, therefore, be primed by butyrate to become activated by lipopolysaccharide and proinflammatory cytokines. This may represent a mechanism by which intestinal epithelial cells can regulate intestinal inflammation in response to changes in the intestinal milieu.

Blotting, Western↗
PubMed2001

Presence of Butyrivibrio fibrisolvens in the digestive tract of dogs and cats, and its contribution to butyrate production.

Numbers of Butyrivibrio fibrisolvens, a major butyrate-producing bacterium in the rumen, in feces of dogs and cats were estimated by competitive PCR. The type IIb of B. fibrisolvens, which produces much more lactate than butyrate, was detected at the levels (cells per g of feces dry weight) of 2.4x10(3)-9.0x10(5) for dogs and 1.7x10(4-)-6.2x10(5) for cats. However, the type I that produces much more butyrate than the type IIb was not detected in cat or dog feces (less than 6.0x10(4) cells per g of feces dry weight). Butyrate production by B. fibrisolvens type IIb in feces was estimated to be at most 30% of the butyrate production by mixed fecal microbes, which suggested that more butyrate is produced by microbes other than B. fibrisolvens in the intestines. Addition of B. fibrisolvens ATCC19171 (type I) to a culture of mixed fecal microbes increased butyrate production, and OB156 (type IIb) increased lactate production. When both the types were added, both the products were increased. Thus, introduction of both the types of B. fibrisolvens as a probiotic may increase butyrate and lactate production in the large intestine, which is possibly beneficial for the maintenance or improvement of the health of dogs and cats.

Journal Article↗