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PubMed1995

The proteoglycan perlecan is expressed in the erythroleukemia cell line K562 and is upregulated by sodium butyrate and phorbol ester.

Perlecan is a modular heparan sulfate proteoglycan that harbors five domains with homology to the low density lipoprotein receptor, epidermal growth factor, laminin and neural cell adhesion molecule. Using a monoclonal antibody directed against the laminin-like domain of perlecan, we have recently shown that perlecan is widely expressed in all lymphoreticular systems. To investigate further this observation we have studied the expression of perlecan in two human leukemic cell lines. Using reverse transcriptase-PCR, ribonuclease protection assay, and metabolic labeling we detected significant perlecan expression in the multipotential cell line K562, originally derived from a patient with chronic myelogenous leukemia. In contrast, the promyelocytic cell line HL-60 expressed perlecan at barely detectable levels. These results were intriguing because the K562 cells do not assemble or produce a classical basement membrane. Following induction with either sodium butyrate or the phorbol diester 12-0-tetradecanoylphorbol-13-acetate (TPA), K562 and HL-60 differentiate into early progenitor cells with erythroid or megakaryocytic properties, respectively. Following treatment of K562 and HL-60 cells with either of these agents, perlecan expression was markedly increased in K562 cells. In contrast, we could detect perlecan protein synthesis in HL-60 cells only at very low levels, even after induction with TPA or sodium butyrate. Collectively, these results indicate that perlecan is actively synthesized by bone marrow derived cells and suggest that this proteoglycan may play a role in hematopoietic cell differentiation.

Base Sequence↗
PubMed1991

Characterization of nuclear T3 receptors in human neuroblastoma cells SH-SY5Y: effect of differentiation with sodium butyrate and nerve growth factor.

Nuclear receptors for the thyroid hormone triiodothyronine (T3) have been identified in vivo in brain tissues and in vitro in mouse and rat neuroblastoma and glioma cells. The present study characterizes nuclear T3 receptors in human neuroblastoma SH-SY5Y cells and compares their level before and after differentiation. Undifferentiated cells, grown in DME/HAM F-12 medium supplemented with 10% fetal calf serum, show an abundant single type of nuclear receptor, indicated by a straight Scatchard plot, with a Kd of 0.11 nmol/l. After treatment with sodium butyrate (0.5 mM for 4 days) or NGF (2 nM for 6 days), the cells showed neuronal-like patterns (extension of neurites, slowing of growth, increased tyrosine hydroxylase activity), with a decrease in the number of nuclear T3 receptors. As sodium butyrate and NGF treatments differentiate neuroblastoma SH-SY5Y cells, these data suggest a down-regulation of T3 receptors with cell maturation.

Butyrates↗
PubMed1985

Sodium butyrate selectively inhibits host cell glycoprotein synthesis in human fibroblasts infected with cytomegalovirus.

Host cell as well as viral DNA synthesis in human fibroblasts infected with human cytomegalovirus was found to be largely resistant even to high concentrations of sodium butyrate. Likewise, production of viral progeny was reduced by 1-2 orders of magnitude but not abolished. On the other hand, the drug allowed (modified) glycosylation only of viral polypeptides whereas that of host proteins was suppressed. Immunofluorescence studies on living cells suggested that butyrate may interfere with processing and intracellular transport of virus-specific surface membrane antigens.

Antigens, Surface↗
PubMed1994

Inhibition of cell cycle progression by sodium butyrate in normal rat kidney fibroblasts is altered by expression of the adenovirus 5 early 1A gene.

The effect of sodium butyrate (NaBut) on cell growth was studied in normal rat kidney (NRK) fibroblasts, and in NRK cells stably transfected with either the adenoviral gene E1A (wild-type), or mutated E1A (E1Amut; with a deletion in the CR1 domain), or with the transforming Ha-ras (EJ) gene. The growth of all these cell lines was inhibited by milimolar concentrations of sodium butyrate (NaBut). However, whereas the NRK cells as well as the NRK-E1Amut and NRK-ras cells were arrested in the G1 phase of the cell cycle, the NRK-E1A cells progressively accumulated in the G2 phase, suggesting that the E1A gene expression caused a "leaky" inhibition of G1 phase progression. The expression of late cell cycle-related genes cdc2 and PCNA (proliferating cell nuclear antigen) was not affected by NaBut in the NRK-E1A cells while it was totally suppressed in the other NRK-derived cell lines.

Adenovirus E1A Proteins↗
PubMed1983

Conservation of the acetylation pattern of histones and the transcriptional activity in Ehrlich ascites tumor cells by sodium butyrate.

Histone deacetylases of Ehrlich ascites tumor cells are active at low temperatures (0-4 degrees C). The so-called hyperacetylated state of histones is the physiological state of histones in intact Ehrlich ascites tumor cells which is conserved by the continuous presence of 10 mM sodium butyrate during the preparation of nuclei and histones. Isolation of histones in the absence of butyrate causes an artificial decrease in histone acetylation. This artificial loss of histone acetylation produces a decrease of the elongation reaction in the RNA synthesis. The initiation of RNA synthesis is not affected.

Acetylation↗
PubMed1984

Sodium butyrate (SB) augments the effects of 1,25 dihydroxyvitamin D3 (1,25(OH)2D3) on neoplastic and osteoblastic phenotype in clonal rat osteosarcoma cells.

1,25 Dihydroxyvitamin D3 suppressed colony formation in soft agar and increased alkaline phosphatase activity in clonal rat osteosarcoma cells. Sodium butyrate enhanced these effects of the hormone partly through a mechanism involving an alteration of nuclear binding of the hormone. It is suggested that 1,25 dihydroxyvitamin D3 in conjunction with sodium butyrate might be able to regulate differentiation and proliferation of neoplastic cells.

Alkaline Phosphatase↗
PubMed1991

Melatonin and its precursors in Y79 human retinoblastoma cells: effect of sodium butyrate.

We studied the release of melatonin and the production of its precursors, 5-hydroxytryptophan and serotonin, in cultured Y79 human retinoblastoma cells. This biosynthetic capability was found to be dependent on cell differentiation, which was initiated by culturing Y79 cells for 7 days in dishes coated with poly-D-lysine to promote cell adhesion to the surface of the culture dishes. Differentiation was further induced by exposing the cell monolayer to sodium butyrate (3 mM) for 3 days. This protocol dramatically increased the release of melatonin and the syntheses of 5-hydroxytryptophan and serotonin in response to forskolin stimulation. Exposure to dopamine (10 microM) or L-DOPA (100 microM) markedly diminished the forskolin-stimulated release of melatonin, as well as the production of 5-hydroxytryptophan and serotonin. These observations indicate that Y79 cells represent a primitive cell line which, following appropriate differentiation (e.g. treatment with sodium butyrate) can display biochemical characteristics similar to those of the human retina. Moreover, serotonin synthesis and melatonin release appear to be coupled in Y79 cells. The inhibition of melatonin release by dopamine supports the hypothesis that in these cells, melatonin and dopamine are components of a retinal feedback loop.

5-Hydroxytryptophan↗
PubMed1983

Erythroid properties of K562 cells. Effect of hemin, butyrate and TPA induction.

Two sublines of the human leukemia cell line K562 including the original cell line and three clones have been investigated for their erythroid features. All of them produce embryonic and fetal hemoglobins, glycophorin A, spectrin and true acetylcholinesterase, but to a varying extent among the cell lines. The Hb and glycophorin contents were correlated in the different K562 cell lines, whereas acetylcholinesterase was independently expressed from these two other erythroid markers. Hb accumulation is enhanced by exposure of the cells to 100 microM hemin without a significant modification of the expression of the other erythroid markers. Butyrate greatly increased the activity of acetylcholinesterase, slightly enhanced the production of hemoglobin, but did not modify the expression of glycophorin and spectrin. 12-O-tetradecanoyl-phorbol-13-acetate (TPA) induced an almost complete disappearance of glycophorin, reduced the synthesis of Hb by K562 cells and also abolished the action of hemin on Hb accumulation. Therefore, all the different K562 cell lines exhibit clear erythroid features including acetylcholinesterase. Butyrate or hemin did not induce terminal differentiation of K562 cells, whereas TPA significantly diminished the erythroid phenotype.

Acetylcholinesterase↗
PubMed1986

Butyrate converts rat 3T3 fibroblasts into giant cells.

Butyrate inhibits proliferation of rat 3T3 cells by blocking the cell cycle in late G1. In these cells, DNA synthesis is completely arrested 24 h after butyrate addition, whereas RNA and protein synthesis proceed unaffected. This partial inhibition of proliferation progressively converts normal cells into giant ones. Transcription and protein synthesis are both more intense in the giant cells than in normal cells. Cell enlargement is inhibited by cell-to-cell contact and the conversion of a normal into a giant cell is reversible. Giant cells may be of use when designing new approaches to the study of cell structure and motility as well as differentiation and proliferation.

Animals↗
PubMed1989

Induction of blood coagulation factor VIII by sodium butyrate in Balb/c 3T3 cells.

Balb/c 3T3 cells have long been used in cell biological studies. When cells were treated with 2 mM sodium butyrate they became flattened and their nuclei became small relative to the cytoplasm. Electron micrographically, intracellular organellae developed significantly: the number of mitochondria increased and membranous structures, namely the rough-surfaced endoplasmic reticulum and Golgi apparatus, developed markedly. Blood coagulation factor VIII was induced in the presence of 2 mM sodium butyrate in a cell sonicate, but not in culture medium. The amount of this factor was almost 100-fold that in the nontreated cells 4 days after culture initiation, indicating that the cloned Balb/c 3T3 cells were of endothelial origin.

Animals↗
PubMed1991

Effects of sodium butyrate on the rearranged c-myc expression in mouse plasmacytoma cells.

The expression of c-myc mRNA was examined after 4 h of sodium butyrate treatment in a mouse plasmacytoma (MPC) cell line (S194). Steady-state levels of rearranged c-myc mRNA were suppressed by the agent in S194 cells. Run-on assay demonstrated that the suppression of the rearranged c-myc mRNA in the MPC was correlated with the transcriptional downregulation of the gene. The suppression was also accompanied by the reduced DNase I sensitivity of the gene. These findings suggest that the rapid downregulation of c-myc mRNA by sodium butyrate is subject to regulation at the transcriptional level following the alteration of the DNase I sensitive chromatin structure in mouse plasmacytoma cells.

Animals↗
PubMed1984

Sodium butyrate inhibits the synthesis of the transformation related protein p 53 in 3T6 mouse fibroblasts.

Sodium butyrate, which blocks the cell cycle of many cell types in the G1 phase, strongly inhibits the synthesis of the transformation related, 53 kDa protein in 3T6 fibroblasts but much less so in SV 40 transformed mouse cells. By several criteria, this effect of the fatty acid appears to be indirect; p 53 synthesis takes place several hours after the butyrate-sensitive step in G1. The results are discussed in the light of a putative role of p 53 in growth control.

Animals↗
PubMed1989

Isolated colonocyte metabolism of glucose, glutamine, n-butyrate, and beta-hydroxybutyrate in malnutrition.

The colonic mucosa may be especially vulnerable during starvation and malnutrition, as luminal nutrients make the greatest contribution to its energy production. To investigate possible metabolic changes in the colonic mucosa during nutrient restriction, we studied substrate utilization by colonocytes isolated from three groups of 6-wk-old rats: control, fasted (72 h), and chronically malnourished animals. Isolated colonocytes were incubated with nonlabeled and 14C-labeled substrates (glucose, glutamine, n-butyrate, or beta-hydroxybutyrate). Substrate oxidation and net increase of intermediary metabolites were reduced in fasted and malnourished animals. The effect of fasting on substrate oxidation was greater than that of chronic malnutrition for all substrates tested except n-butyrate. The total ketone body concentrations and beta-hydroxybutyrate to acetoacetate ratios were higher in the fasted and malnourished groups than in controls. The findings suggest that the colonic mucosa responds to nutrient deprivation by a general reduction of oxidative metabolism that is associated with an altered redox state.

3-Hydroxybutyric Acid↗
PubMed1992

The effects of propionate and butyrate on acetate metabolism in rat hepatocytes.

1. Two mM propionate or butyrate inhibited the mitochondrial uptake of acetate by rat hepatocytes. 2. With propionate the inhibition was so strong that the net formation of acetate in the cytoplasm, usually masked by the mitochondrial uptake, appeared directly as a net output of acetate into the medium; showing that this net formation of acetate, reported by [Crabtree B., Gordon M.-J. and Christie S. L. (1990) Biochem. J. 270, 219-225] is not an artefact arising from a misinterpretation of isotopic data. 3. The results also suggest that propionate and butyrate inhibit peroxisomal metabolism.

Acetates↗
PubMed1983

Suppression of an ethanol withdrawal syndrome in rats by butyrate, lactate and beta-hydroxybutyrate.

Butyrate, lactate and beta-hydroxybutyrate, compounds which may be elevated in blood of ethanol dependent rats and substrates of the cerebral small-pool Krebs-cycle, were tested for their ability to suppress an ethanol withdrawal syndrome. Male Sprague-Dawley rats were rendered physically dependent on ethanol by intragastric administration of ethanol at a dosage of 9 to 15 grams per kilogram per day over a 4-day period. Oral administration of a mixture of butyrate, lactate and beta-hydroxybutyrate was effective in suppressing the tremulous component of the ethanol withdrawal syndrome.

3-Hydroxybutyric Acid↗
PubMed1985

Sodium butyrate-induced changes in cultured rabbit articular chondrocyte transmembrane electrical potentials. Relationship between these changes and the proliferative response.

Sodium butyrate at 5mM reversibly induced a significant increase of transmembrane potentials (Em) in normal chondrocytes (24 hours after seeding) and arrested their proliferation. This increase in Em levels, which could be temporarily abolished by Tetra-ethyl Ammonium (TEA 5mM), was related to an increase in membrane permeability to K+. This hyperpolarization was correlated with the reversible inhibition of growth in G1 induced by the sodium butyrate.

Animals↗
PubMedDate not supplied

Recovery of growth-arrested human fibroblasts from UV-induced lethal damage is inhibited by low cell density or sodium butyrate.

The influence of growth arrest on recovery from UV-induced lethal damage in human fibroblasts was investigated. Cells were arrested in G1 either by confluent holding (high cell density at 37 degrees C) or by temperature holding (low cell density at 30 degrees C) or by a combination of both methods. These experiments showed that survival recovery only occurred in cells arrested at high cell density, both at 37 degrees C and at 30 degrees C, and not in cells arrested at low cell density at 30 degrees C. Furthermore, it was demonstrated that the rate of transcription in unirradiated cells arrested at high density, both at 37 degrees C and at 30 degrees C, was much lower compared to that in cells arrested at low density. These observations can be explained by assuming that impaired transcription is responsible for UV-induced cytotoxicity and that recovery of RNA synthesis due to repair of damage in transcriptionally active genes may account for survival recovery. Sodium butyrate did not influence the absence of recovery during low temperature holding at low density but inhibited survival recovery during confluent holding. Sodium butyrate might prevent survival recovery at high cell density by inducing a chromatin structure resembling that of untreated cells arrested at low density.

Butyrates↗