Inhibition of Heme Oxygenase-1 Partially Reverses the Arsenite-Mediated Decrease of CYP1A1, CYP1A2, CYP3A23, and CYP3A2 Catalytic Activity in Isolated Rat Hepatocytes

2011 ◽  
Vol 40 (3) ◽  
pp. 504-514 ◽  
Author(s):  
Anwar Anwar-Mohamed ◽  
Lars-Oliver Klotz ◽  
Ayman O. S. El-Kadi
1988 ◽  
Vol 252 (1) ◽  
pp. 137-142 ◽  
Author(s):  
J M Te Koppele ◽  
B Coles ◽  
B Ketterer ◽  
G J Mulder

The stereoselectivity of purified rat GSH transferases towards alpha-bromoisovaleric acid (BI) and its amide derivative alpha-bromoisovalerylurea (BIU) was investigated. GSH transferase 2-2 was the only enzyme to catalyse the conjugation of BI and was selective for the (S)-enantiomer. The conjugation of (R)- and (S)-BIU was catalysed by the isoenzymes 2-2, 3-3 and 4-4. Transferase 1-1 was less active, and no catalytic activity was observed with transferase 7-7. Isoenzymes 1-1 and 2-2 of the Alpha multigene family preferentially catalysed the conjugation of the (S)-enantiomer of BIU (and BI), whereas isoenzymes 3-3 and 4-4 of the Mu multigene family preferred (R)-BIU. The opposite stereoselectivity of conjugation of BI and BIU previously observed in isolated rat hepatocytes and the summation of activities of enzymes known to be present in hepatocytes on the basis of present data are in accord.


1979 ◽  
Vol 254 (18) ◽  
pp. 8841-8846
Author(s):  
L.J. Debeer ◽  
J. Thomas ◽  
P.J. De Schepper ◽  
G.P. Mannaerts

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