In vitro metabolism of simazine, atrazine and propazine by hepatic cytochrome P450 enzymes of rat, mouse and guinea pig, and oestrogenic activity of chlorotriazines and their main metabolites

Xenobiotica ◽  
1999 ◽  
Vol 29 (12) ◽  
pp. 1213-1226 ◽  
Author(s):  
N. Hanioka ◽  
H. Jinno ◽  
T. Tanaka-Kagawa ◽  
T. Nishimura ◽  
M. Ando
1994 ◽  
Vol 38 (6) ◽  
pp. 557-566 ◽  
Author(s):  
JC Bloomer ◽  
SJ Baldwin ◽  
GJ Smith ◽  
AD Ayrton ◽  
SE Clarke ◽  
...  

2001 ◽  
Vol 16 (7) ◽  
pp. 541-544 ◽  
Author(s):  
Seetal Dodd ◽  
David W. Boulton ◽  
Graham D. Burrows ◽  
C. Lindsay De Vane ◽  
Trevor R. Norman

2005 ◽  
Vol 37 (2) ◽  
pp. 351-358 ◽  
Author(s):  
Arun K. Agrawal ◽  
Cornelis E.C.A. Hop ◽  
Jianmei Pang ◽  
Maria V. Silva Elipe ◽  
Ranjit C. Desai ◽  
...  

1994 ◽  
Vol 72 (02) ◽  
pp. 313-317 ◽  
Author(s):  
P Savi ◽  
J Combalbert ◽  
C Gaich ◽  
M-C Rouchon ◽  
J-P Maffrand ◽  
...  

SummaryClopidogrel and ticlopidine are two well known selective anti-ADP agents which are inactive in vitro and must be administered in vivo to fully exhibit their antiaggregating and antithrombotic effects. Since previous studies have clearly demonstrated that the activation steps take place in the liver, we examined the effect of specific induction or inhibition of cytochrome P450 subfamilies on the antiaggregating activity of clopidogrel. SKF 525-A, a global cytochrome P450 inhibitor, dramatically decreased the antiaggregating effect of clopidogrel, therefore indicating that cytochrome P450 enzymes are involved in the hepatic activation of clopidogrel. The efficacy of clopidogrel was increased in animals pretreated with 3-methylcholanthrene and (3-naphthoflavone, indicating that the cytochrome P450-1A subfamily pathway was mainly involved in the activating metabolism of clopidogrel. The use of specific antibodies directed against the various cytochrome P450 subfamilies ascertained this observation.


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