Stimulation of DNA synthesis in primary cultures of adult rat hepatocytes by sodium butyrate

Staecker, Jeffrey L.; Sawada, Norimasa; Pitot, Henry C.

doi:10.1016/s0006-291x(87)80089-x

Cited by 9 publications

(5 citation statements)

References 26 publications

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“…Third, propionate is a known inhibitor of histone deacetylase, as has been shown in vitro in non‐neural cells (Samuels et al. 1980; Staecker et al. 1987; Okamura et al.…”

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confidence: 93%

Propionate increases neuronal histone acetylation, but is metabolized oxidatively by glia. Relevance for propionic acidemia

Nguyen

Morland

González

et al. 2006

Journal of Neurochemistry

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In propionic acidemia, propionate acts as a metabolic toxin in liver cells by accumulating in mitochondria as propionyl-CoA and its derivative, methylcitrate, two tricarboxylic acid cycle inhibitors. Little is known about the cerebral metabolism of propionate, although clinical effects of propionic acidemia are largely neurological. We found that propionate was metabolized oxidatively by glia: [3-14 C]propionate injected into mouse striatum or cortex, gave a specific activity of glutamine that was 5-6 times that of glutamate, indicating metabolism in cells that express glutamine synthetase, i.e., glia. Further, cultured cerebellar astrocytes metabolized [3-14 C]propionate; cultured neurons did not. However, both cultured cerebellar neurons and astrocytes took up [ 3 H]propionate, and propionate exposure increased histone acetylation in cultured neurons and astrocytes as well as in hippocampal CA3 pyramidal neurons of wake mice. The inability of neurons to metabolize propionate may be due to lack of mitochondrial propionyl-CoA synthetase activity or transport of propionyl residues into mitochondria, as cultured neurons expressed propionyl-CoA carboxylase, a mitochondrial matrix enzyme, and oxidized isoleucine, which becomes converted into propionyl-CoA intramitochondrially. The glial metabolism of propionate suggests astrocytic vulnerability in propionic acidemia when intramitochondrial propionyl-CoA may accumulate. Propionic acidemia may alter both neuronal and glial gene expression by affecting histone acetylation.

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“…Third, propionate is a known inhibitor of histone deacetylase, as has been shown in vitro in non‐neural cells (Samuels et al. 1980; Staecker et al. 1987; Okamura et al.…”

mentioning

confidence: 93%

Propionate increases neuronal histone acetylation, but is metabolized oxidatively by glia. Relevance for propionic acidemia

Nguyen

Morland

González

et al. 2006

Journal of Neurochemistry

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“…When cells are exposed to millimolar concentrations of sodium butyrate, it interferes at the level of the chromatin structure by inhibition of histone deacetylase(s), resulting in the accumulation of hyperacetylated core-particle histones. The chromatin structure relaxes under the influence of histone acetylation, which is reported to occur during rapid cell growth, maturation, and cell differentiation, i.e., when new genes are expressed (Perry and Chalkley, 1982;McCue et al, 1984;Staecker et al, 1987). Another possibility of how butyrate might affect differentiation is via increasing the levels of cyclic adenosine monophosphate (AMP) (Prasad and Sinha, 1976) and its differential effect on the cyclic AMP phosphodiesterase as described by Mori et al (1986).…”

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confidence: 99%

Sodium butyrate selectively antagonizes the inhibitory effect of retinoids on cornified envelope formation in cultured human keratinocytes

Schmidt¹,

Cathelineau²,

Cavey³

et al. 1989

Journal Cellular Physiology

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Sodium butyrate affects cell differentiation in confluent epidermal keratinocyte cultures by considerably increasing the spontaneous formation of cross-linked envelopes in normal human keratinocytes (NHK). It also favors the development of envelope competence in the Simian virus-40 (SV-40)-transformed human foreskin keratinocyte line SV-K14. It completely abolishes the inhibitory effect of serum and retinoic acid on the expression of plasma membrane-associated transglutaminase. However, other markers of epidermal differentiation that are also under the control of retinoids such as keratins or the enzyme cholesterol sulfotransferase are not affected by butyrate. The level of the cellular retinoic acid binding protein (CRABP) is considerably increased in its presence. Butyrate does not interfere with the binding of retinoids to their cellular binding proteins. Our observations suggest that sodium butyrate stimulates cornified envelope formation via the induction of the plasma membrane-associated transglutaminase required for cornified envelope synthesis and, additionally, by abolishing the inhibitory effect of retinoids on the expression of this enzyme.

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“…Various antiproliferative effects of sodium butyrate on different types of cells in vivo and in vitro have been described [13][14][15][16]. It has also been shown that butyrate can inhibit the development of grafted tumours in mice [17].…”

Section: Discussionmentioning

confidence: 99%

Induction of glutathione‐S‐transferase‐pi by short‐chain fatty acids in the intestinal cell line caco‐2

Stein¹,

Schröder²,

Bonk³

et al. 1996

Eur J Clin Investigation

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Glutathione S-transferases (GSTs) are a multigene family of detoxification and metabolizing enzymes that have been linked with the susceptibility of tissues to environmental carcinogens. In addition to their role as the main energy source in the colonic mucosa, short-chain fatty acids (SCFAs) have been found to act as potent antiproliferative and differentiating agents in various cancer cell lines. The objective of this study was to evaluate the effects of SCFAs on the induction of GSTpi in the intestine as a possible new anticarcinogenic mechanism of SCFAs. Studies were performed in Caco-2 cells, a cell line resembling functionally normal enterocytes. Cells, cultured in DMEM supplemented with 10% fetal calf serum, were studied from day 0 dpc (days post confluence) until 21 dpc and culture. SCFAs (acetate, propionate, butyrate) were added to give a final concentration of 5 mmol L(-1). At 0, 3, 6, 9, 15, and 21 dpc, protein, lactate dehydrogenase (LDH), alkaline phosphatase (AP) and GSTpi were measured. Butyrate supplementation significantly (P < or = 0.01) increased GSTpi levels compared with controls in a concentration-dependent manner. The effect was detectable within 3 dpc with a maximum at 15 dpc. In contrast to butyrate, the other SCFAs tested had no (acetate) or little effect (propionate). In conclusion, the data suggest that the anticancer effect of butyrate in part may be based on the induction of GSTpi activity, resulting in an enhanced detoxification capacity of the gut.

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Stimulation of DNA synthesis in primary cultures of adult rat hepatocytes by sodium butyrate

Cited by 9 publications

References 26 publications

Propionate increases neuronal histone acetylation, but is metabolized oxidatively by glia. Relevance for propionic acidemia

Propionate increases neuronal histone acetylation, but is metabolized oxidatively by glia. Relevance for propionic acidemia

Sodium butyrate selectively antagonizes the inhibitory effect of retinoids on cornified envelope formation in cultured human keratinocytes

Induction of glutathione‐S‐transferase‐pi by short‐chain fatty acids in the intestinal cell line caco‐2

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