Temperature Acclimation of Xenobiotic Metabolizing Enzymes in Cultured Hepatocytes and Whole Liver of the Gulf Toadfish, Opsanus beta

1991 ◽  
Vol 48 (7) ◽  
pp. 1212-1219 ◽  
Author(s):  
Christopher J. Kennedy ◽  
Kenneth A. Gill ◽  
Patrick J. Walsh

Changes in cytochrome P-450 and microsomal and soluble protein content and the activities of several microsomal and cytosolic xenobiotic metabolizing enzymes were examined in the whole livers of gulf toadfish, Opsanus beta, following acclimation to 18 or 28 °C and in isolated hepatocytes (prepared from 18 or 28 °C acclimated gulf toadfish) which were maintained in primary culture for 29 d on L-15 media. Cells isolated from both acclimation groups were cultured at 18 and 28 °C. In whole livers, significant differences were found in the activities of sulfotransferase (which showed perfect compensation) and UDP-glucuronosyltransferase (which showed "inverse compensation") between fish acclimated to 18 and 28 °C, but several other trends were obscured by interindividual variation. However, in hepatocyte cultures, temperature adaptations were seen in cytochrome P-450 content and in the activities of the microsomal enzymes aryl hydrocarbon hydroxylase, epoxide hydrolase, and UDP-glucuronosyltransferase. Glutathione-S-transferase activity appeared to be rather temperature insensitive in both whole livers and in cultured hepatocytes. Incomplete temperature acclimation for all enzymes was observed in cultured cells and this may be due to systemic factors which were not present in cell culture media.

1982 ◽  
Vol 204 (2) ◽  
pp. 441-447 ◽  
Author(s):  
M Matsui ◽  
H K Watanabe

Postnatal development of hepatic UDP-glucuronosyltransferase and sulphotransferase activities towards androsterone and 4-nitrophenol as well as cytochrome P-450 contents was studied in male and female Wistar rats. The rats with high and low UDP-glucuronosyltransferase activity towards androsterone were classified by the genotype of the parent animals. UDP-glucuronosyltransferase activity towards androsterone began rapidly to enhance after 30 days of age in the high-activity group, whereas the transferase activity remained low throughout in the low-activity group. Such a striking difference was not observed in UDP-glucuronosyltransferase activity towards 4-nitrophenol, sulphotransferase activity towards androsterone and 4-nitrophenol, and cytochrome P-450 contents. Sex-based difference in the sulphotransferase activity was marked after 30 days of age. Sulphotransferase activity towards androsterone was much higher in adult females than in adult males, whereas higher sulphation activity towards 4-nitrophenol was found in adult males. The results also indicate that the low level of the UDP-glucuronosyltransferase activity did not lead to compensatory stimulation of the sulphotransferase activity.


2019 ◽  
Vol 130 ◽  
pp. 32-43 ◽  
Author(s):  
Elias Begas ◽  
Maria Bounitsi ◽  
Thomas Kilindris ◽  
Evangelos Kouvaras ◽  
Konstantinos Makaritsis ◽  
...  

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