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Drug Metabolism and Disposition Fast Forward
First published on February 5, 2009; DOI: 10.1124/dmd.108.025718

0090-9556/09/3705-925-931$20.00
DMD 37:925-931, 2009

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MINIREVIEW

Antibodies as a Probe in Cytochrome P450 Research

Magang Shou, and Anthony Y. H. Lu

Department of Pharmacokinetics and Drug Metabolism, Amgen Inc., Thousand Oaks, California (M.S.); and Department of Chemical Biology, College of Pharmacy, Rutgers University, Piscataway, New Jersey (A.Y.H.L.)

Cytochrome P450 (P450) is the superfamily of enzymes responsible for biotransformation of endobiotics and xenobiotics. However, their large isoform multiplicity, inducibility, diverse structure, widespread distribution, polymorphic expression, and broad overlapping substrate specificity make it difficult to measure the precise role of each individual P450 to the metabolism of drugs (or carcinogens) and hamper the understanding of the relationship between the genetic/environmental factors that regulate P450 phenotype and the responses of the individual P450s to drugs. The antibodies against P450s have been useful tools for the quantitative determination of expression level and contribution of the epitope-specific P450 to the metabolism of a drug or carcinogen substrate in tissues containing multiple P450 isoforms and for implications in pharmacogenetics and human risk assessment. In particular, the inhibitory antibodies are uniquely suited for reaction phenotyping that helps to predict human pharmacokinetics for clinical drug-drug interaction potential in drug discovery and development.


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Address correspondence to: Dr. Magang Shou, Department of Pharmacokinetics and Drug Metabolism, Amgen Inc., 30E-2-B, One Amgen Center Drive, Thousand Oaks, CA 91320. E-mail: mshou{at}amgen.com






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