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

Journal Publication ResearchOnline@JCU
Vukomanovic, Dragic;McLaughlin, Brian;Rahman, Mona N.;Vlahakis, Jason Z.;Roman, Gheorghe;Dercho, Ryan A.;Kinobe, Robert;Hum, Maaike;Brien, James F.;Jia, Zongchao;Szarek, Walter A.;Nakatsu, Kanji
Robert Kinobe
Abstract

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.

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88

ISBN/ISSN

1205-7541

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4

Pages Count

7

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NRC Research Press

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DOI

10.1139/Y10-004