The Effect of Dietary Cirrhosis and CCl14 Poisoning on Glucuronyl Transferase Activity of Rat Liver

1961 ◽  
Vol 40 (4) ◽  
pp. 521-531 ◽  
Author(s):  
Zygmunt Chojecki ◽  
Fred Kern
2006 ◽  
Vol 84 (12) ◽  
pp. 1259-1265 ◽  
Author(s):  
D. Suresh ◽  
K. Srinivasan

The effect of dietary supplementation of spice-active principles, curcumin (0.2%), capsaicin (0.015%), and piperine (0.02%) on the activities of the liver drug-metabolizing enzyme system was examined. All the 3 dietary spice principles significantly stimulated the activity of aryl hydroxylase. A synergistic action of dietary curcumin and capsaicin with respect to stimulating the activity of aryl hydroxylase was also evidenced when fed in combination. The activity of N-demethylase essentially remained unaffected by dietary curcumin, capsaicin, or their combination, but was significantly lowered as a result of piperine feeding. Uridine dinucleotide phosphate (UDP)-glucuronyl transferase activity was decreased by dietary piperine and the combination of curcumin and capsaicin. NADPH-cytochrome c reductase activity was significantly decreased by dietary piperine. The levels of hepatic microsomal cytochrome P450 and cytochrome b5 were not influenced by any of the dietary spice-active principles. These spice-active principles were also examined for their possible in vitro influence on the components of the hepatic drug-metabolizing enzyme system in rat liver microsomal preparation. Piperine significantly decreased the activity of liver microsomal aryl hydroxylase activity when included in the assay medium at 1 × 10−6 mol/L, 1 × 10−5 mol/L, and 1 × 10−4 mol/L level. Lowered activity of N-demethylase was observed in presence of capsaicin or piperine at 1 × 10−6 mol/L in the assay medium. Hepatic microsomal glucuronyl transferase activity was significantly decreased in vitro by addition of capsaicin or piperine. Capsaicin and piperine brought about significant decrease in liver microsomal cytochrome P450 when included at 1 × 10−6 mol/L and 1 × 10−5 mol/L, the effect being much higher in the case of piperine. The results suggested that whereas the 3 spice principles have considerable similarity in structure, piperine is exceptional in its influence on the liver drug-metabolizing enzyme system. The study also indicated that a combination of curcumin and capsaicin does not produce any significant additive effect on the liver drug-metabolizing enzyme system.


1983 ◽  
Vol 128 (2-3) ◽  
pp. 209-221 ◽  
Author(s):  
Nicola Tavoloni ◽  
Mary Jane T. Jones ◽  
Robert Wittman ◽  
Kiang Chih-Li ◽  
Paul D. Berk

1989 ◽  
Vol 264 (3) ◽  
pp. 737-744 ◽  
Author(s):  
P Steinberg ◽  
H Schramm ◽  
L Schladt ◽  
L W Robertson ◽  
H Thomas ◽  
...  

The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in parenchymal and non-parenchymal cells isolated from untreated rats were separated by chromatofocusing in an f.p.l.c. system: all glutathione S-transferase isoenzymes observed in the sinusoidal lining cells were also detected in the parenchymal cells, whereas Kupffer and endothelial cells lacked several glutathione S-transferase isoenzymes present in parenchymal cells. At 5 days after administration of Arocolor 1254 glutathione S-transferase activity was only enhanced in parenchymal cells; furthermore, selenium-dependent glutathione peroxidase activity decreased in parenchymal and non-parenchymal cells. At 13 days after a single injection of Aroclor 1254 a strong induction of glutathione S-transferase had taken place in all three cell types, whereas selenium-dependent glutathione peroxidase activity remained unchanged (endothelial cells) or was depressed (parenchymal and Kupffer cells). Hence these results clearly establish that glutathione S-transferase and glutathione peroxidase are differentially regulated in rat liver parenchymal as well as non-parenchymal cells. The presence of glutathione peroxidase and several glutathione S-transferase isoenzymes capable of detoxifying a variety of compounds in Kupffer and endothelial cells might be crucial to protect the liver from damage by potentially hepatotoxic substances.


1982 ◽  
Vol 201 (3) ◽  
pp. 653-656 ◽  
Author(s):  
B Burchell

1. Reconstitution of purified bilirubin UDP-glucuronyltransferase from Wistar-rat liver into Gunn-rat liver microsomes provides a better environment than phosphatidylcholine liposomes, such that the final specific activity of the Wistar-rat liver enzyme was increased up to 85 units/mg of protein. 2. Gunn- and Wistar-rat liver microsomes were equally effective for reconstitution of the purified enzyme. 3. The transferase activity does not appear to be fully expressed in the more rigid environment of foetal Wistar-rat liver microsomes. 4. These reconstitution experiments reveal a final specific activity for the purified bilirubin UDP-glucuronyltransferase consistent with the capacity of the whole rat liver to glucuronidate bilirubin and indicate that the absence of this enzyme activity in Gunn-rat liver microsomes is not due to an abnormal microenvironment.


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