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2004•Current Protocols in ToxicologyRequires access

Human Cytochrome P450: Metabolism of Testosterone by CYP3A4 and Inhibition by Ketoconazole

Khawja A. Usmani, Jun Tang

Open publisher page 36 citations

Abstract

This unit describes methods for measuring CYP3A4 activity using testosterone as a specific substrate, and for measuring CYP3A4 inhibition using ketoconazole as a selective inhibitor of testosterone oxidation. CYP3A4 is one of the most important and most abundant drug-metabolizing CYP isoforms in human liver microsomes (∼40% of total CYP), and it has the broadest substrate specificity. It is important to determine whether CYP3A4 is involved in its metabolism.

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What this paper is about

This unit describes methods for measuring CYP3A4 activity using testosterone as a specific substrate, and for measuring CYP3A4 inhibition using ketoconazole as a selective inhibitor of testosterone oxidation. CYP3A4 is one of the most important and most abundant drug-metabolizing CYP isoforms in human liver microsomes (∼40% of total CYP), and it has the broadest substrate specificity. It is important to determine whether CYP3A4 is involved in its metabolism.

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OpenAlex reports 36 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

This unit describes methods for measuring CYP3A4 activity using testosterone as a specific substrate, and for measuring CYP3A4 inhibition using ketoconazole as a selective inhibitor of testosterone oxidation. CYP3A4 is one of the most important and most abundant drug-metabolizing CYP isoforms in human liver microsomes (∼40% of total CYP), and it has the broadest substrate specificity. It is important to determine whether CYP3A4 is involved in its metabolism.

Key concepts: Ketoconazole, CYP3A4, Cytochrome P450, Microsome, Testosterone (patch), Chemistry, Drug metabolism, Metabolism

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