Immunohistochemical localization of cytochrome P-450 b/e in hepatic and extrahepatic rat tissues

1988 ◽  
Vol 16 (4) ◽  
pp. 642-643 ◽  
Author(s):  
KIM J. RICH ◽  
ALAN R. BOOBIS ◽  
JOHN R. FOSTER ◽  
DOROTHEA SESARDIC ◽  
DONALD S. DAVIES
1989 ◽  
Vol 22 (3) ◽  
pp. 351-365 ◽  
Author(s):  
KAZUSHIGE DOBASHI ◽  
KOHTARO ASAYAMA ◽  
KIYOHIKO KATO ◽  
MAKIO KOBAYASHI ◽  
AKIRA KAWAOI

1988 ◽  
Vol 84 (2) ◽  
pp. 109-114 ◽  
Author(s):  
Christer Köhler ◽  
Lars G. Eriksson ◽  
Tiiu Hansson ◽  
Margaret Warner ◽  
Jan Åke-Gustafsson

1997 ◽  
Vol 16 (3) ◽  
pp. 131-137 ◽  
Author(s):  
Sarah J Crosbie ◽  
PG Blain ◽  
Faith M Williams

1 The in vitro metabolism ofn-hexane was studied in rat liver, lung, brain and skeletal muscle microsomes and in microsomes prepared from cell lines expressing human cytochrome P-450 2E1 or 2B6. The hydro xylated metabolites ofn-hexane were quantified by gas chromatography-mass spectometry. 2 Rat liver and extensor digitorum longus (EDL, fast- twitch skeletal muscle) microsomes and the CYP 2B6 microsomes produced the pre-neurotoxic metabolite of n-hexane, 2-hexanol as a major metabolite in contrast to the other rat tissues examined. 3 Inhibition of 2- and 3-hexanol production from n- hexane by rat lung microsomes using metyrapone, an inhibitor of cytochrome P-450 2B1 activity, resulted in almost complete inhibition of lung microsomal activ ity. 4 Production of all three hexanols was significantly increased with phenobarbital-induced rat liver micro somes, with a 10-fold increase in 2- and 3-hexanol production. A slight increase in 2-hexanol production with phenobarbital-induced rat EDL and brain micro somes was observed. No increase in n-hexane meta bolism was noted following induction with β- naphthoflavone or with ethanol.


1996 ◽  
Vol 105 (1) ◽  
pp. 71-79 ◽  
Author(s):  
Yuji Moriwaki ◽  
Tetsuya Yamamoto ◽  
Kei Yamaguchi ◽  
Sumio Takahashi ◽  
Kazuya Higashino

1993 ◽  
Vol 139 (3) ◽  
pp. 503-NP ◽  
Author(s):  
T. Tamura ◽  
J. Kitawaki ◽  
T. Yamamoto ◽  
Y. Osawa ◽  
S. Kominami ◽  
...  

ABSTRACT Immunohistochemical localization of 17α-hydroxylase/C17-20 lyase (P-45017α,lyase) and aromatase cytochrome P-450 (P-450arom) in polycystic ovary (PCO) syndrome was studied using specific polyclonal antibodies which had been raised against the corresponding enzymes. In the majority of follicles that were atretic and smaller than 7 mm in diameter, theca interna cells showed high P-45017α,lyase immunoreaction, while small numbers of granulosa cells showed little P-450arom immunoreaction. In some atretic follicles that were larger than 11 mm in diameter, the hyperplastic theca interna cell layer showed high immunoreaction to P-45017α,lyase, while the poorly proliferated granulosa cell layer showed a mixture of weak and negative immunoreaction to P-450arom. No immunoreaction to P-45017α,lyase or P-450arom was recognized in PCO stroma. These findings suggest that the theca interna cells and the granulosa cells from PCOs show abnormal steroidogenic function, while the localization of P-45017α,lyase and P-450arom in PCOs was essentially identical to that in the normal ovary. Theca interna cells in PCO atretic follicles are the main site of excess androgen production. Journal of Endocrinology (1993) 139, 503–509


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