scholarly journals The action of pyruvate on ethanol oxidation by intact isolated liver cells

1971 ◽  
Vol 123 (4) ◽  
pp. 41P.2
Author(s):  
M N Berry
FEBS Letters ◽  
1981 ◽  
Vol 133 (2) ◽  
pp. 201-204 ◽  
Author(s):  
B.O. Christophersen ◽  
Jon Norseth

1983 ◽  
Vol 32 (1) ◽  
pp. 13-26 ◽  
Author(s):  
Bernard Portha ◽  
Hilda Chamras ◽  
Yvonne Broer ◽  
Luc Picon ◽  
Gabriel Rosselin

1960 ◽  
Vol 235 (5) ◽  
pp. 1354-1358
Author(s):  
Robert L. McGeachin ◽  
Betty Ann Potter

1974 ◽  
Vol 140 (3) ◽  
pp. 355-361 ◽  
Author(s):  
Michael N. Berry ◽  
Harold V. Werner ◽  
Ernest Kun

1. Incubation of isolated liver cells in a medium containing bicarbonate raises malate concentrations almost sixfold compared with values obtained in a bicarbonate-free phosphate medium. The malate concentration of about 0.3mm in bicarbonate medium is of the same order as the Km for malate dehydrogenase. 2. The utilization of ethanol, glyercol and sorbitol was increased by 20–35% in bicarbonate medium. 3. Fluoromalate, a specific inhibitor of malate dehydrogenase and the malate carrier, inhibited or ethanol oxidation by 23%, glycerol uptake by 20% and sorbitol uptake by 42% in bicarbonate medium, but had a much smaller inhibitory action in phosphate medium. In consequence fluoromalate almost abolished the stimulatory effects of bicarbonate on substrate utilization. 4. Difluoro-oxaloacetate, a specific inhibitor of aspartate aminotransferase, had about one-half the inhibitory activity of fluoromalate. The two inhibitors in combination were less effective than fluoromalate by itself. 5. It is concluded that bicarbonate stimulates the utilization of reduced substrates, which are oxidized in the cytoplasmic compartment of the liver cell, by increasing the activity of rate-limiting malate dehydrogenase-dependent intercompartmental hydrogen shuttles. Both malate–oxaloacetate and malate–aspartate systems are involved in these hydrogen-translocation processes.


1987 ◽  
Vol 242 (3) ◽  
pp. 655-660 ◽  
Author(s):  
M J Fisher ◽  
A J Dickson ◽  
C I Pogson

The stimulation of phenylalanine hydroxylation in isolated liver cells by sub-maximally effective concentrations of glucagon (less than 0.1 microM) is antagonized by insulin (0.1 nM-0.1 microM). This phenomenon is a consequence of a decrease in the glucagon-stimulated phosphorylation of phenylalanine hydroxylase from liver cells incubated in the presence of insulin. The impact of insulin on the phosphorylation state and activity of the hydroxylase is mimicked by incubation of liver cells in the presence of orthovanadate (10 microM). A series of cyclic AMP and cyclic GMP analogues enhanced phenylalanine hydroxylation: in each case insulin diminished the stimulation of flux. These results are discussed in the light of the characteristics of insulin action on other metabolic processes.


1976 ◽  
Vol 30b ◽  
pp. 345-352 ◽  
Author(s):  
Niels Grunnet ◽  
Herluf I. D. Thieden ◽  
Bjørn Quistorff ◽  
Michel Devreux ◽  
Jean Vialle ◽  
...  

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