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Recombinant truncated and microsomal heme oxygenase-1 and -2: differential sensitivity to inhibitors

Recombinant truncated forms of heme oxygenase-1 and -2 (HO-1 and HO-2) were compared with their crude microsomal counterparts from brain and spleen tissue of adult male rats with respect to their inhibition by azole-based, nonporphyrin HO inhibitors. The drugs tested were an imidazole-alcohol, an im...

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Bibliographic Details
Published in:Canadian journal of physiology and pharmacology 2010-04, Vol.88 (4), p.480-486
Main Authors: Vukomanovic, Dragic, McLaughlin, Brian, Rahman, Mona N, Vlahakis, Jason Z, Roman, Gheorghe, Dercho, Ryan A, Kinobe, Robert T, Hum, Maaike, Brien, James F, Jia, Zongchao, Szarek, Walter A, Nakatsu, Kanji
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Language:English
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Summary:Recombinant truncated forms of heme oxygenase-1 and -2 (HO-1 and HO-2) were compared with their crude microsomal counterparts from brain and spleen tissue of adult male rats with respect to their inhibition by azole-based, nonporphyrin HO inhibitors. The drugs tested were an imidazole-alcohol, an imidazole-dioxolane, and a triazole-ketone. Both the recombinant and crude forms of HO-2 were similarly inhibited by the 3 drugs. The crude microsomal spleen form of HO-1 was more susceptible to inhibition than was the truncated recombinant form. This difference is attributed to the extra amino acids in the full-length enzyme. These observations may be relevant in the design of drugs as inhibitors of HO and other membrane proteins.
ISSN:0008-4212
1205-7541
DOI:10.1139/Y10-004