Role of liver glutathione in 1,1-dichloroethylene metabolism and hepatotoxicity in intact rats and isolated perfused rat liver

1978 ◽  
Vol 41 (3) ◽  
pp. 169-178 ◽  
Author(s):  
D. Reichert ◽  
H. W. Werner ◽  
D. Henschler
Keyword(s):  
Rat Liver ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Liver Glutathione ◽  
Intact Rats

scholarly journals Ganglioside incorporation and release by the isolated perfused rat liver

1991 ◽  
Vol 274 (2) ◽  
pp. 581-585 ◽  
Author(s):  
S C Kivatinitz ◽  
A Miglio ◽  
R Ghidoni
Keyword(s):  
Rat Liver ◽  
The Other ◽  
Regulatory Role ◽  
Isolated Perfused Rat Liver ◽  
Order Kinetic ◽  
Perfused Rat Liver ◽  
Ganglioside Gm1 ◽  
First Order ◽  
Pseudo First Order

The fate of exogenous ganglioside GM1 labelled in the sphingosine moiety, [Sph-3H]GM1, administered as a pulse, in the isolated perfused rat liver was investigated. When a non-recirculating protocol was employed, the amount of radioactivity in the liver and perfusates was found to be dependent on the presence of BSA in the perfusion liquid and on the time elapsed after the administration of the ganglioside. When BSA was added to the perfusion liquid, less radioactivity was found in the liver and more in the perfusate at each time tested, for up to 1 h. The recovery of radioactivity in the perfusates followed a complex course which can be described by three pseudo-first-order kinetic constants. The constants, in order of decreasing velocity, are interpreted as: (a) the dilution of the labelled GM1 by the constant influx of perfusion liquid; (b) the washing off of GM1 loosely bound to the surface of liver cells; (c) the release of gangliosides from the liver. Process (b) was found to be faster in the presence of BSA, probably owing to the ability of BSA to bind gangliosides. The [Sph-3H]GM1 in the liver underwent metabolism, leading to the appearance of products of anabolic (GD1a, GD1b) and catabolic (GM2, GM3) origin; GD1a appeared before GM2 and GM3 but, at times longer than 10 min, GM2 and GM3 showed more radioactivity than GD1a. At a given time the distribution of the radioactivity in the perfusates was quite different from that of the liver. In fact, after 60 min GD1a was the only metabolite present in any amount, the other being GM3, the quantity of which was small. This indicates that the liver is able to release newly synthesized gangliosides quite specifically. When a recirculating protocol was used, there were more catabolites and less GD1a than with the non-recirculating protocol. A possible regulatory role of ganglioside re-internalization on their own metabolism in the liver is postulated.

Role of neutrophils in ischemia/reperfusion liver injury. A study in the isolated perfused rat liver

1991 ◽  
Vol 13 ◽  
pp. S109
Author(s):  
O. Chazouillères ◽  
C. Legendre ◽  
M. Vaubourdolle ◽  
M.T. Bonnefis ◽  
C. Rey ◽  
...  
Keyword(s):  
Liver Injury ◽  
Rat Liver ◽  
Ischemia Reperfusion ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver

Effect of glycogenolytic agents on phosphorylase activity of perfused rat liver

1965 ◽  
Vol 208 (2) ◽  
pp. 317-323 ◽  
Author(s):  
Robert A. Levine
Keyword(s):  
Rat Liver ◽  
Cyclic Nucleotide ◽  
Adenine Nucleotides ◽  
Adenosine Monophosphate ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Adrenocorticotrophic Hormone ◽  
Phosphorylase Activity ◽  
Glycogen Breakdown ◽  
Intact Rats

The effect of glycogenolytic agents on phosphorylase activity has been studied in the isolated perfused rat liver. Evidence is presented showing that endoportal administration of 10–6m glucagon, 10–5 m epinephrine, and 10–3 M cyclic 3',5'-adenosine monophosphate (3',5'-AMP) induced glycogenolysis, hyperglycemia, and increase in liver phosphorylase activity, usually within 1 hr after the onset of infusion. ATP, 10–3m, also caused glycogenolysis, but the onset was slower than with the cyclic nucleotide, and phosphorylase activation was inconstant Hyperglycemic effects of these two adenine nucleotides were also demonstrated in intact rats. Anoxia and hypoxia caused substantial glycogenolysis but did not stimulate phosphorylase activity, implying that some other mechanism accounts for the glycogen breakdown induced by reduced oxygen tension. Glycogenolysis and phosphorylase activation were not produced by administration of 10–2 M 5'-AMP, 10–4 M isoproterenol, adrenocorticotrophic hormone, or insulin.

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