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.

Journal

Canadian Journal of Physiology and Pharmacology

Publication Name

Canadian Journal of Physiology and Pharmacology

Volume

88

ISBN/ISSN

1205-7541

Edition

N/A

Issue

4

Pages Count

7

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N/A

Publisher

NRC Research Press

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Publish Date

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Date

N/A

EISSN

N/A

DOI

10.1139/Y10-004