Triiodothyronine and Estradiol Increase the Serum Level of Androstanediol Glucuronide but Do Not Influence Androgen UDP-Glucuronyl Transferase Activity in the Female Rat

1994 ◽  
Vol 26 (05) ◽  
pp. 226-228 ◽  
Author(s):  
E. Pirog ◽  
D. Collins
1977 ◽  
Vol 198 (1132) ◽  
pp. 297-314 ◽  

Lesions of the suprachiasmatic nuclei that caused failure of spontaneous ovulation in female rats consistently produced abnormalities in other functions that are normally influenced by the light-dark cycle. In such animals morning plasma corticosterone concentrations were abnormally high and evening values abnormally low though the response to stress was unaffected. Pineal serotonin N -acetyl transferase activity was abnormally high in animals killed during the day and abnormally low in those killed at night. Although the animals were in persistent be­havioural oestrus, total voluntary wheel-running activity was not con­sistently altered but was distributed evenly between the light and dark periods rather than being confined principally to the dark periods as in normal animals. Similarly the proportion of the daily water and food intake that occurred during the dark period was reduced. The incidence of these associated abnormalities was low in lesioned rats that continued to ovulate spontaneously.


1992 ◽  
Vol 70 (5) ◽  
pp. 727-731 ◽  
Author(s):  
Cristina E. Carnovale ◽  
Viviana A. Catania ◽  
Juan A. Monti ◽  
Maria C. Carrillo

Microsomal glutathione S-transferase, UDP-glucuronyl transferase, and aniline hydroxylase activities were determined in liver, renal cortex, and small intestine of control, streptozotocin-diabetic, alloxan-diabetic, and untreated insulin-injected male Wistar rats. Renal microsomal glutathione S-transferase activity showed a direct linear relationship with insulin blood levels, in agreement with our previous report on cytosolic glutathione S-transferase. This result suggests a possible regulatory mechanism of insulin that needs to be further examined. The hepatic microsomal UDP-glucuronyl transferase was only decreased in streptozotocin-diabetic rats and was not restored by insulin treatment. Intestinal UDP-glucuronyl transferase exhibited an opposite response in streptozotocin-treated animals that was not normalized by the administration of insulin. Hepatic aniline hydroxylase showed the same behaviour as intestinal UDP-glucuronyl transferase. These results suggest that streptozotocin and (or) its metabolites have a direct effect on hepatic and intestinal UDP-glucuronyl transferase activity and on hepatic aniline hydroxylase activity. On the other hand, insulin regulation of enzyme activity varies from one organ to another.Key words: insulin, streptozotocin, alloxan, glutathione S-transferase, UDP-glucuronyl transferase, aniline hydroxylase.


PEDIATRICS ◽  
1967 ◽  
Vol 40 (6) ◽  
pp. 993-999
Author(s):  
Barbara Jones

In vitro studies using a mouse liver microsome system failed to demonstrate that menadiol sodium diphosphate, menadione sodium bisulfite, or phytonadione enhanced or inhibited the quantity of ortho-aminophenol glucuronide produced. In vivo studies in young rats with these vitamin K analogues also failed to show an effect on glucuronide conjugation. Based on this data, it is concluded that the hyperbilirubinemia seen in prematures after large doses of water-soluble vitamin K analogues is probably not due to an inhibitory effect of glucuronyl transferase. The evidence suggesting that it may be due in part to hemolysis is briefly reviewed.


1974 ◽  
Vol 52 (3) ◽  
pp. 203-207 ◽  
Author(s):  
Rosalind S. Labow ◽  
Denis G. Williamson ◽  
Donald S. Layne

Microsomal preparations from the liver of female sheep can effect the transfer of glucose from UDP-glucose to the 17α-hydroxyl group of 17α-estradiol-3-glucuronide, and, in much poorer yield, to some other steroids containing a 17 α-hydroxyl group. No evidence was found for steroid galactosyl or N-acetylglucosaminyl transferase activity in sheep liver. Glucuronyl transferase with an activity of a high order to a variety of substrates was present. Preliminary work indicated that the steroid glucosyl transfer is mediated by an enzyme distinct from glucuronyl transferase.


1983 ◽  
Vol 32 (14) ◽  
pp. 2143-2147 ◽  
Author(s):  
Nicola Tavoloni ◽  
Robert Wittman ◽  
Mary Jane T. Jones ◽  
Paul D. Berk

Sign in / Sign up

Export Citation Format

Share Document