Hongbing Wang, PhD
![]() | Assistant Professor |
Research
My primary research interest is in the understanding of the molecular mechanisms that govern the xenobiotic-induced regulation of metabolizing enzymes and drug transporters in human. Utilizing human primary hepatocytes as a model, specific research focus has been centered on pregnane X receptor (PXR), constitutive androstane receptor (CAR), and aryl hydrocarbon receptor (AhR), in human liver, which play critical roles in regulating drug induced expression of main phase I, phase II metabolizing/detoxification enzymes, as well as drug transporters. My research interests also involve the metabolism dependent prodrug bioactivation and transport related drug resistance. Particularly, P450 mediated biotransformation of chemotherapeutics (such as cyclophosphamide and ifosphamide) in liver and breast cancer.
Selected Publications
Faucette SR, Sueyoshi T, Smith C, Negishi M, LeCluyse EL, and Wang H. Differential regulation of hepatic CYP2B6 and CYP3A4 genes by constitutive androstane receptor but not pregnane X receptor. J. Pharmacol. Exp. Ther. 317(3):1200-9, 2006
Smith C, Graham RA, Krol WL, Silver IS, Negishi M, Wang H, and LeCluyse EL. Differential UGT1A1 induction by chrysin in primary human hepatocytes and HepG2 cells. J. Pharmacol. Exp. Ther. 315:1256-1264, 2005
Hempel N, Wang H, LeCluyse EL, McManus ME, and Negishi M. The human sulfotransferase SULT1A1 gene is regulated in a synergistic manner by Sp1 and GA binding protein. Mol. Pharmacol. 66(6): 1690-701, 2004
Wang H, Faucette SR, Moore R, Sueyoshi T, Negishi M, and LeCluyse EL. Human CAR mediates induction of CYP2B6 gene expression by phenytoin. J. Biol. Chem. 279 (28): 29295-29301, 2004
Wang H, Faucette SR, Sueyoshi T, Moore R, Ferguson S, Negishi M, and LeCluyse EL. A novel distal enhancer module regulated by PXR/CAR is essential for the maximal induction of CYP2B6 gene expression. J. Biol. Chem. 278 (16): 14146-52, 2003
Wang H, Chanas B, and Ghanayem BI. Cytochrome P450 2E1 (CYP2E1) is the only enzyme responsible for acrylonitrile metabolism to cyanide: comparative studies using CYP2E1-null and wild-type mice. Drug Metab. Dispos. 30:911-917, 2002
