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

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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.

On a comparé l’inhibition de formes recombinantes tronquées de hème oxygénase-1 et -2 (HO-1 et HO-2) avec celle de leurs contreparties microsomales brutes, en utilisant des inhibiteurs de HO non porphyriques, à base d’azole. On a testé trois médicaments: un imidazole-alcool, un imidazole-dioxolane et un triazole-cétone. Les 3 médicaments ont inhibé de manière similaire les formes recombinantes et brutes de HO-2. La forme microsomale brute splénique de HO-1 a été plus sensible à l’inhibition que la forme recombinante tronquée. Cette différence est attribuée aux acides aminés surnuméraires dans l’enzyme complète. Ces observations pourraient être utiles pour la conception d’inhibiteurs de HO et d’autres protéines membranaires.
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Document Type: Research Article

Publication date: April 1, 2010

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