Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “BUTYRATES”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,171 records · Page 65Linked to original sources
PubMed1994

Absorption and metabolism of hydrocortisone 21-butyrate, 21-hemisuccinate and hydrocortisone by skin of the rabbit ear during single-pass perfusion.

1. Rabbit ear was single-pass perfused with protein-free buffer solution at a rate of 0.02 ml/min per cm2 surface area for up to 6 h. 2. Hydrocortisone or hydrocortisone 21-butyrate or hydrocortisone 21-hemisuccinate was applied dermally (0.01-1.0% w/w) in suspension with isopropyl myristate or dissolved in 1,2-propanediol. The ointments were stiffened with 5% polyethylene 1500 or 1.2% methylcellulose respectively. 3. Hydrocortisone was slowly absorbed and did not reach a steady-state absorption rate during the experimental period. 4. No metabolites of hydrocortisone were found during ear perfusion. In the supernatant of skin homogenate, however, cortisone, hydrocortisone-20 alpha-ol and another, as yet unidentified metabolite, were observed. 5. Hydrocortisone 21-butyrate was completely hydrolysed during dermal absorption, showing steady-state concentrations of hydrocortisone in the effluent. Hydrocortisone 21-hemisuccinate did not reach steady-state concentrations in the effluent. About two-thirds was hydrolysed during absorption. 6. During arterial perfusion approximately 30% of hydrocortisone 21-butyrate was hydrolysed whereas 97% of hydrocortisone 21-hemisuccinate remained intact. 7. First-pass ester hydrolysis in skin may be complete for the poorly absorbed glucocorticoids leading to metabolites of less lipophilicity.

Absorption↗
PubMed2005

Sodium butyrate-mediated differentiation of colorectal cancer cells: regulation of PKCbetaII by PI 3-kinase.

The present study focuses on a putative regulation of PKCbetaII by phosphatidylinositol-3 kinase (PI 3-kinase) in colorectal carcinoma cells; little is known about the role and activity of PKCbetaII in these cells. We examined the activity of PI 3-kinase in two adenocarcinoma cell lines, HT29 cells that differentiate only after stimulation with appropriate agents, and Caco-2 cells that can differentiate spontaneously. The activity of PI 3-kinase as well as the activity of PKCbetaII appeared to decrease only in HT29 cells in which differentiation was induced by sodium butyrate. In HT29 cells infected with recombinant adenovirus encoding constitutively active PI 3-kinase, the activity of alkaline phosphatase was almost completely blocked, and this PI 3-kinase significantly potentiated the activity of PKCbetaII in HT29 cells despite the presence of NaBT in the culture medium. On the contrary, in differentiating Caco-2 cells, the activity of PI 3-kinase was not butyrate-sensitive. In agreement with these findings, the alkaline phosphatase activity was not affected by constitutively active PI 3-kinase overexpressed in Caco-2 cells. These observations suggest that PKCbetaII is regulated by PI 3-kinase in HT29 cells and that the mechanisms of spontaneous differentiation versus butyrate-induced differentiation of adenocarcinoma cells may be different.

Adenocarcinoma↗
PubMedDate not supplied

[Content of homocarnosine, gamma-amino butyric acid and histidine in brain tissue of different age normal rabbits and under hyperoxia].

The content of homocarnosine, gamma-amino butyric acid and histidine was studied in the brain of newborn, 1, 7, 14, 21 and 30-day rabbits in normalcy and under hyperoxia. For 30 days of the postnatal life the amount of peptide in the animal brain is 2.5, histidine 1.6, gamma-amino butyric acid--2.2 times as high. At the preconvulsive stage of oxygen poisoning the content of homocarnosine lowers sharply in the brain of rabbits of all age groups. The most considerable decrease is observed in the brain of 14, 21 and 30-day rabbits by 53, 60 and 85%, respectively. The content of gamma-amino butyric acid lowers only in the brain of 21 and 30-day animals by 39 and 47%, respectively; the content of histidine in these animals under hyperoxia, vice versa, increases by 10 and 25%.

Aging↗
PubMedDate not supplied

Alpha-naphthyl butyrate esterase (a selective cytochemical monocyte marker).

This paper describes a cytochemical technique for alpha-naphthyl butyrate esterase demonstration in monocytes obtained from peripheral blood of normal subjects, of a patient with reactive monocytosis and of a patient with myelomonocytic leukemia. It utilizes pH 6.1 alpha-naphthyl butyrate as substrate. At this pH value, alpha-naphthyl butyrate is a specific monocyte marker. The cytochemical procedure proposed is simple, rapid and standardized, as it utilizes stable and easily available reagents.

Carboxylic Ester Hydrolases↗
PubMed1978

Plasma alpha-amino-n-butyric acid to leucine ratio: nonspecificity as a marker for alcoholism.

Recent studies suggest that the ratio of plasma alpha-amino-n-butyric acid to leucine is increased specifically by chronic heavy alcohol consumption. To test this hypothesis, we determined this ratio in normal controls and (1) currently drinking chronic heavy alcoholics; (2) currently abstaining chronic alcoholics; (3) patients with nonalcoholic liver disease; (4) chronically alcohol-fed rats and mice; (5) mice infected with murine hepatitis virus; and (6) mice exposed to carbon tetrachloride. Mean ratios in control persons, drinking alcoholics, abstaining alcoholics, and nonalcoholic liver disease patients were not statistically different. Of 5 drinking alcoholics followed serially from the beginning of abstinence, 1 had an elevated ratio on admission and a persistently elevated ratio even 2 weeks later; another had a ratio more elevated after 2 weeks of abstinence, than on admission; and 3 had ratios in the normal elevated after 2 weeks of abstinence than on admission; and 3 had ratios in the normal range. Compared to control rats, chronically alcohol-fed rats had a significantly elevated mean ratio after 1 month and an even higher ratio after 2 months (P less than 0.001). In control, alcohol-fed and carbon tetrachloride-treated mice, alpha-amino-n-butyric acid was undetectable, but in two sets of mice with severe murine hepatitis virus infection, elevated ratios were found. We conclude that because the ratio of alpha-amino-n-butyric acid to leucine is not necessarily elevated in chronic heavy alcoholics but can be elevated in acute experimental liver cell injury, it does not appear to be a specific marker for the detection of alcoholism.

Alcoholism↗
PubMed1996

Comparison of fluticasone propionate cream, 0.05%, and hydrocortisone-17-butyrate cream, 0.1%, in the treatment of eczema.

This is a randomized, double-blind, parallel-group, multicenter study involving 120 patients comparing the safety and tolerability of two midpotency topical preparations, fluticasone propionate cream, 0.05%, and hydrocortisone-17-butyrate cream, 0.1%, in the treatment of moderate-to-severe eczema. Safety of the study medications was determined over a twelve-week period using laboratory tests for selected fasting blood chemical levels, hematologic analysis, urinalysis, and morning plasma cortisol levels, and by analyzing both the nature and frequency of reported adverse events. Efficacy was evaluated during the first four weeks of the study. None of the fluticasone-treated patients experienced any severe drug-related adverse events, but one hydrocortisone-17-butyrate-treated patient's eczema was severely exacerbated by drug therapy. Plasma cortisol monitoring revealed minimal hypothalamic-pituitary-adrenal axis suppression. Overall, the nature of drug-related adverse events in patients as young as 12 years old treated with fluticasone propionate cream, 0.05%, indicates this topical application was safe and well tolerated throughout the twelve-week study. Fluticasone cream was also found to be similar in efficacy to hydrocortisone-17-butyrate cream.

Administration, Topical↗
PubMed1997

Modulation of p53 expression in cultured colonic adenoma cell lines by the naturally occurring lumenal factors butyrate and deoxycholate.

The high incidence of colorectal cancer in Western society is believed to be strongly related to diet. Mutation of the p53 gene is a late event in colorectal carcinogenesis, and thus, the majority of pre-malignant adenomas express wild-type p53. As loss of p53 protein function is an important step in colorectal carcinogenesis, we investigated whether naturally occurring lumenal factors can modulate the expression of p53 in non-tumorigenic human colonic adenoma cell lines. Levels of p53 protein and mRNA were measured in adherent cells which had been incubated with growth-inhibitory concentrations of sodium butyrate (a by-product of dietary fibre fermentation) or sodium deoxycholate (a bile acid) for up to 48 hr. We report that both butyrate and deoxycholate can down-regulate the expression of wild-type and mutant p53. In contrast, incubation for 48 hr with the endogenous inhibitory growth factor TGFbeta1 did not alter p53 protein expression. Thus, in addition to cellular mechanisms which regulate p53 function, such as post-translational stabilisation, nuclear exclusion, negative feedback inhibition of p53 mRNA translation or binding of p53 by cellular proteins, p53 protein levels also may be regulated by changes in the level of p53 gene transcription. Furthermore, we show that lumenal factors are able to affect directly the expression of p53 protein in colonic epithelial cells.

Adenoma↗
PubMed1986

Modification of the hyperthermic response on neuroblastoma cells by cAMP and sodium butyrate.

The role of adenosine 3',5'-cyclic monophosphate (cAMP) and sodium butyrate in modifying the effect of heat on murine neuroblastoma cells (NBP2) in culture was evaluated on the criterion of survival. An elevation of cellular cAMP level by prostaglandin (PG) A2, a stimulator of adenylate cyclase, and 4-(3-butoxy-4-methoxybenzyl)-2-imidazolidinone (R020-1724), an inhibitor of cyclic nucleotide phosphodiesterase, only during heat treatment (43 degrees C and 40 degrees C) was sufficient to enhance the effect of heat. The extent of enhancement (additive versus synergistic) depended upon the cAMP stimulating agent and the experimental condition. When these agents were added after heat treatment for the entire observation period, they produced similar results. PGA2 and R020-1724 are known to increase the intracellular level of cAMP in these cells by three and fivefold, respectively; therefore, the effect of these agents in enhancing the heat-response may be mediated by cAMP-dependent mechanisms. The presence of sodium butyrate during heat treatment alone was ineffective; however, when it was added before or after heat treatment for the entire observation period, the survival of heated cell was markedly reduced.

4-(3-Butoxy-4-methoxybenzyl)-2-imidazolidinone↗
PubMed1994

Butyrate and acetyl-carnitine inhibit the cytogenetic expression of the fragile X in vitro.

Cytogenetic expression of the fragile site at Xq27.3 is only found in those patients who have a full mutation of the FMR1 gene, i.e., a large amplification of the CGG repeat. However, an expansion of this repeat, although necessary, does not seem to be sufficient to cause expression of fra(X)(q27.3). Other factors are clearly needed, e.g., thymidylate stress. Little or no attention has been paid to the possible role of histones in the expression of the fragile sites, in spite of their structural and regulatory role in the chromatin complex. Histones can be modified by treating intact cells in vitro with butyrate, a substance that causes histone acetylation. The purpose of the present work is to test the effect of butyrate and of the acetylating compound acetyl-L-carnitine on the expression of fra(X)(q27.3) by treating peripheral lymphocytes of fragile X syndrome patients with these substances in vitro. We show that this treatment causes a significant inhibition of fra(X)(q27.3) expression.

Acetylation↗
PubMedDate not supplied

Enhanced Ii expression after n-butyrate treatment of a P3HR-1 Burkitt's lymphoma subline which does not express HLA-D.

Treatment of P3HR-1 Burkitt's lymphoma cultured cells with 4 mM n-butyrate for 48 h induced the abundant expression of a 35 000 dalton, microsomal membrane protein which was demonstrated to be the electrophoretically invariant Ii molecule. To prove this point, [35S]methionine-labelled, microsomal membrane proteins or immunoprecipitates of such detergent-solubilized proteins were subjected to electrophoresis either in SDS gels or in two-dimensional, nonequilibrium pH gradient gels. The induced p35 molecule was judged to be Ii by molecular weight and isoelectric characteristics and by immune complex associations. The abundant expression of Ii on butyrate-treated P3HR-1 cells mimicked the high level of expression of p35 or Ii on leukemic cells of a subset of patients with hairy cell leukemia. Alpha and beta chains of the HLA-D complex were absent from the P3HR-1 cell line and present in the Jijoye parent from which mutant P3HR-1 was derived. This relatively simple model can lead to the study of inducible synthesis, processing and expression of Ii, with or without HLA-D alpha and beta chains.

Burkitt Lymphoma↗
PubMed1983

Sodium butyrate produces concordant expression of "early placental" alkaline phosphatase, pregnancy-specific beta 1-glycoprotein and human chronic gonadotropin beta-subunit in a newly established uterine cervical cancer cell line (SKG-IIIa).

The production of early and term placental alkaline phosphatase (ALP), human chorionic gonadotropin beta-subunit (beta-hCG) and pregnancy-specific beta 1-glycoprotein (SP1) was confirmed in the newly established uterine cervical cancer call line SKG-IIIa. Treatment of these cells in culture with sodium butyrate caused an increase of all of these oncodevelopmental proteins. On the other hand, prednisolone treatment enhanced only term placental ALP, while it reduced early placental ALP, beta-hCG and SP1. These data suggested that such oncotrophoblastic proteins as early placental ALP, beta-hCG and SP1 were concordantly modulated by butyrate and prednisolone. These findings may support the possibility of the reexpression of sets of development phase-specific genes in cancer cells.

Alkaline Phosphatase↗
PubMed1984

Human globin gene transcription in injected Xenopus oocytes: enhancement by sodium butyrate.

We have studied the expression of the human adult (beta) and foetal (gamma) globin genes by injecting a cosmid containing the complete -G gamma-A gamma-psi beta-delta-beta cluster into Xenopus oocytes. The transcripts from the gamma and beta genes were characterised with respect to their 5' termini by S1 nuclease mapping using probes which extend 5' to the cap site and 3' into the first exon. The only beta transcripts detectable in injected oocytes spanned from either -231 or -177 (cap site +1) into the first exon. The sensitivity of this transcription to inhibition by a low concentration of alpha-amanitin indicated that polymerase II was responsible. S1 analysis of gamma gene transcripts showed that the predominant transcript mapped from a site at -227, but a low level of transcription from the cap site was also detectable. Incubation of oocytes in saline solution containing sodium butyrate prior to injection resulted in a significant stimulation of transcription from the gamma gene cap site. In contrast, transcription from the beta gene upstream sites was only slightly increased. The possible role of sodium butyrate in promoting this effect is discussed in the context of its known property as a modifier of cellular chromatin.

Adult↗
PubMed1984

Effects of sodium butyrate on growth and cell-cycle kinetics of cultured rabbit articular chondrocytes.

The sodium salt of n-butyric acid was found to inhibit the growth of asynchronous cultures of rabbit articular chondrocytes. This inhibitory effect was dose-dependent between 1 mM and 5 mM, reversible, and accompanied by volume enhancement and modification of cellular morphology. Flow-cytometric analysis showed that drug exposure led to a slowing-down of the cell-cycle progression; after 1 day's exposure, cells accumulated in G1, and after 2 or 3 days' treatment, in G2, without a blockage in M; the increase of cells in G2 was in fact due to an enhancement of binculeated cells. The treated cells had an increased RNA content. Articular chondrocytes seem to be target cells for sodium butyrate and therefore it represents a valuable biological tool for studying the mechanisms of their growth regulation.

Animals↗
PubMed1985

Formation of proliferative tetraploid cells after treatment of diploid cells with sodium butyrate in rat 3Y1 fibroblasts.

When randomly proliferating rat 3Y1 fibroblasts were treated with sodium butyrate, more than 90% of their cells were arrested reversibly with a 2C DNA content at least 12 h before the G1/S boundary. When cells synchronized in the early S phase were treated with butyrate, approximately 70% of all cells were arrested with a 4C DNA content. The arrests in both G1 and G2 phases by the single inhibitor suggest that the two phases share a common mechanism. The ability of cells to undergo mitosis on time was quickly lost with time of arrest in the G2 phase. Upon removal of the inhibitor, the cells arrested with a 4C DNA content entered a new S phase without intervening mitosis. The tetraploid cells thus produced kept proliferating as fast as diploid cells. These results suggest that the inhibition of the normal G2 traverse is somehow responsible for the formation of the proliferative polyploid cells.

Animals↗
PubMed1994

Development of dexamethasone-inducible tyrosine aminotransferase activity in WB-F344 rat liver epithelial stemlike cells cultured in the presence of sodium butyrate.

Sodium butyrate acts as a differentiation-promoting agent for a wide variety of cell types, including some tumor cell lines. In this study, we examined the effects of sodium butyrate (SB) on the functional differentiation of cultured WB-F344 rat liver epithelial stemlike cells. Treatment of WB-F344 cells with 3.75 mM SB resulted in an inhibition of cellular proliferation, alterations to normal cellular morphology (increased cell size and decreased nuclear/cytoplasmic ratio), and significant increases in cellular protein synthesis. The SB-mediated changes in cell morphology, proliferative status, and protein catabolism were accompanied by development of dexamethasone-inducible tyrosine aminotransferase (TAT) enzyme activity. Culture of WB-F344 cells in growth medium containing SB and dexamethasone (DEX; 1 x 10(-6) M) resulted in greater than sevenfold increase in the basal TAT activity compared with control cultures. An additional sixfold increase in TAT activity was observed when cells cultured in medium containing SB and DEX were exposed to 1 x 10(-7) M DEX during the last 24 hours of culture. The DEX-inducible TAT activity developed by SB-treated WB-F344 cells responded to the modulating effects of insulin and L-tyrosine in a manner that closely resembled that reported for cultured hepatocytes and hepatoma cell lines. These studies show that treatment of WB-F344 rat liver epithelial stemlike cells with the differentiation-promoting agent SB in vitro leads to expression of the differentiation-specific hepatocyte enzyme TAT.

Animals↗
PubMed1993

Induction of recombinant human gamma-glutamyl transferase by sodium butyrate in transfected V79 and CHO Chinese hamster cells.

Sodium butyrate was used to enhance biosynthesis rates of recombinant human gamma-glutamyl transferase (GGT) expressed under the control of the SV40 or the cytomegalovirus immediate early promoter, respectively, in transfected V79 and CHO Chinese hamster cell lines. Maximal induction of GGT specific activity in butyrate-treated cells ranged from 3 to 5-fold and resulted from a strong increase in the GGT mRNA ratio. We also observed that maximal transcription level in V79 cells occurred within 12 hr of treatment, whilst the cell proliferation was transiently arrested. Despite its processing requirements, induced GGT exhibited unchanged catalytic and physico-chemical features relative to human serum or hepatoma enzyme, thus appearing as an excellent model for further studies on human GGT.

Animals↗
PubMed1998

Differential expression of human histone deacetylase mRNAs in response to immune cell apoptosis induction by trichostatin A and butyrate.

The reversible acetylation of histones by histone deacetylases (HDACs) and acetyltransferases (HATs) plays a fundamental role in gene transcription. We previously showed that HDAC mRNA is upregulated in immune cells upon PHA-induced activation. Little is known, however, about the differential regulation of HDAC mRNAs by the HDAC inhibitors Trichostatin A (TSA) and butyrate, agents known to block proliferation and induce apoptosis. We report that apoptosis-inducing concentrations of TSA and butyrate upregulate the expression of HDAC mRNAs in a differential manner and act synergistically with PHA to induce HDAC expression, suggesting the presence of independent HDAC regulatory mechanisms. Moreover, we show that HDAC inhibitor-induced apoptosis is associated with early abrogation of gamma-IFN production by Th1 lymphocytes and with p53 mRNA downregulation. Our findings highlight the dynamic interplay of cell cycle-, activation- and apoptosis-related proteins in association with time-dependent expression of HDACs and are suggestive of different specific roles for these enzymes.

Acetyltransferases↗
PubMed1989

Butyric acid modulates developmental globin gene switching in man and sheep.

The developmental switch from production of fetal (gamma) to adult (beta) globin occurs on a normally set biologic clock which proceeds even if the adult (beta) globin genes are defective. Preventing or reversing the globin gene switch would be beneficial for subjects with abnormal beta globin genes. We have now identified a class of agents which, when present in elevated plasma concentrations during gestation, appears to inhibit the gamma beta globin gene switch in developing humans. Further investigation has shown that butyric acid and related compounds can increase gamma globin and decrease beta globin expression in erythroid cells cultured from subjects with diseases of abnormal beta globin. Butyrate compounds were therefore infused in an in vivo fetal animal model, and the globin switch was inhibited in most and reversed in some fetal lambs. These data suggest that inhibiting expression of abnormal beta globin genes may be possible in future generations. Histone modification may be a mechanism of action involved. The developmental switch from production of gamma globin to beta globin results in significant morbidity when the beta globin genes are defective. The globin switch has therefore been extensively studied, appearing to be set on a biologic clock and proceeding despite the site of blood production and solely on the basis of gestational age. We previously found that this developmental gene switch is delayed in human fetuses developing in the presence of maternal diabetes. A number of metabolites present in abnormal concentrations in these infants were therefore tested for effects on globin expression.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetylation↗