Metabolism of ethanol and acetaldehyde in parenchymal and non-parenchymal rat liver cells

Sjöblom, Mats; Mørland, Jörg

doi:10.1016/0006-2952(79)90081-9

Cited by 16 publications

(4 citation statements)

References 38 publications

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“…These observations argue against either a nonspecific or a toxic effect of ethanol on the cells as a mechanism for the generation of chemotactic activity. Our inability to detect chemotactic activity in cultures of several nonparenchymal cell types is consistent with previous studies which have shown that, in contrast to hepatocytes, these cells do not metabolize ethanol (25).…”

Section: Discussionsupporting

confidence: 92%

“…After S min, 0.04% (wt/vol) bacterial collagenase (type I, Sigma Chemical Co., St. Louis, MO) and 2.0 mM CaC12 were added to the perfusate. After an additional 25 min of perfusion, the markedly softened liver was removed and transferred to a flask that contained minimal essential medium, 0.04% (wt/vol) bacterial collagenase, 2.0 mM CaC12, and 10 gg/ml DNase-l (Sigma Chemical Co.). After opening the liver capsule with scissors, the flask was placed on a rotatory shaker for 5 min at 370C to disperse enzymatically dissociated cells.…”

Section: Methodsmentioning

confidence: 99%

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Production of chemotactic activity for polymorphonuclear leukocytes by cultured rat hepatocytes exposed to ethanol.

Perez¹,

Roll²,

Bissell³

et al. 1984

J. Clin. Invest.

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Abstract. Acute alcoholic hepatitis is characterized by infiltration of the liver parenchyma with polymorphonuclear leukocytes. As a possible explanation for this phenomenon, we have found that ethanol stimulates cultured rat hepatocytes to generate potent chemotactic activity. Hepatocytes (>99% pure), isolated from the livers of Sprague-Dawley rats, responded to incubation with ethanol (2.0-10 mM) by releasing chemotactic activity for human polymorphonuclear leukocytes into culture supernatants in a time-and concentration-dependent fashion. Chemotactic activity was maximal after incubation of hepatocytes with 10 mM ethanol for 6 h. It was undetectable in the absence of ethanol and was reduced in the presence of either the alcohol dehydrogenase inhibitor, 4-methylpyrazole, or the acetaldehyde dehydrogenase inhibitor, cyanamide. Ethanol failed to stimulate generation of chemotactic activity by either rat dermal fibroblasts, hepatic sinusoidal endothelial cells, or Kupffer cells. The chemotactic activity generated by ethanol-treated rat hepatocytes was recovered from culture supernatants in the lipid phase after extraction with chloroform/methanol. Thin-layer Portions of this work were presented at

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Section: Discussionsupporting

confidence: 92%

Section: Methodsmentioning

confidence: 99%

Production of chemotactic activity for polymorphonuclear leukocytes by cultured rat hepatocytes exposed to ethanol.

Perez¹,

Roll²,

Bissell³

et al. 1984

J. Clin. Invest.

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“…The mean values of the metabolic rate of ethanol (40 mM) in control incubations were similar in hepatocytes from fasted and fed animals ranging from 0.44 to 0.49 pmol ethanol metabolized/mg cell protein/hour (table 1). Previous observations have shown similar rates of ethanol metabolism in hepatocyte preparations (Aune et al 1981b;Sjablom & Msrland 1979). The addition of ex-ogenous pyruvate (5 mM) enhanced the rate of elimination of ethanol 2and 3-fold in hepatocytes from fed and fasted animals respectively (table 1).…”

Section: Resultssupporting

confidence: 56%

Acute Interaction of Halothane and Enflurane with the Metabolism of Ethanol in Isolated Hepatocytes and Liver Cytosol Preparations from the Rat

Aune¹,

Normann²,

Olsen³

et al. 1985

Acta Pharmacologica et Toxicologica

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The effects of halothane and enflurane on ethanol (40 mM) oxidation were studied in isolated rat hepatocytes. Anaesthetic (halothane, enflurane and diethyl ether) effect on the activity of alcohol dehydrogenase (ADH) was studied in incubations of cytosol preparations from rat liver. Mean rates of ethanol metabolism ranged from 0.44 to 0.49 μmol ethanol metabolized/mg cell protein/hour in control hepatocytes from fasted and fed animals. These rates were enhanced by 2‐ and 3‐fold in hepatocytes from fed and fasted animals, respectively, when pyruvate (5 mM) was added. Halothane and enflurane both caused dose dependent inhibition of ethanol metabolism (15‐40%) in all hepatocytes without exogenous addition of pyruvate. The inhibitory effect was present also after pyruvate stimulation in hepatocytes from fasted animals, but disappeared in hepatocytes from fed animals when pyruvate was added. The rate of ethanol oxidation by cells from fed rats was enhanced by approximately 40% when the concentration of ethanol was increased from 20 mM to 80 mM. The anaesthetic inhibition of ethanol metabolism was about 20% more pronounced at the higher ethanol concentration compared to the lower concentration when no pyruvate was added. In the presence of pyruvate the effect of anaesthetics was again reversed regardless of ethanol concentration. Halothane (2 mM) and enflurane (2 mM) both caused about 25% inhibition of the ADH‐activity in cytosol preparations while ether (30 mM) caused more than 50% inhibition. No inhibition of hepatocyte uptake of ethanol was caused by any of the three anaesthetics. It was concluded that the volatile anaesthetic agents in addition to their well known membrane effects also seem to be able to interfere directly with the activity of the non‐membrane related enzyme ADH.

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“…Alcohol dehydrogenase (EC 1.1.1.1) is the major location of initial ethanol oxidation. Although this enzyme has been detected in various tissues in humans (Moser et al, 1968) and in rats (Raskin & Sokoloff, 1972;Sjoblom & Morland, 1979), the liver has always been considered to contain the greatest alcohol dehydrogenase activity and to be responsible for the major ethanol-oxidation capacity in the body. Acetaldehyde and NADH are formed by alcohol dehydrogenase action, and these two products are responsible for most of the toxic effects and metabolic disturbances produced by ethanol ingestion.…”

mentioning

confidence: 99%

Comparative kinetics of human and rat liver alcohol dehydrogenase

Herrera¹,

Zorzano²,

Fresneda³

1983

Biochemical Society Transactions

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Metabolism of ethanol and acetaldehyde in parenchymal and non-parenchymal rat liver cells

Cited by 16 publications

References 38 publications

Production of chemotactic activity for polymorphonuclear leukocytes by cultured rat hepatocytes exposed to ethanol.

Production of chemotactic activity for polymorphonuclear leukocytes by cultured rat hepatocytes exposed to ethanol.

Acute Interaction of Halothane and Enflurane with the Metabolism of Ethanol in Isolated Hepatocytes and Liver Cytosol Preparations from the Rat

Comparative kinetics of human and rat liver alcohol dehydrogenase

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