| Literature DB >> 33484438 |
Yeo-Jung Kwon1, Sangyun Shin1, Young-Jin Chun2.
Abstract
Human cytochrome P450 enzymes (CYPs) play a critical role in various biological processes and human diseases. CYP1 family members, including CYP1A1, CYP1A2, and CYP1B1, are induced by aryl hydrocarbon receptors (AhRs). The binding of ligands such as polycyclic aromatic hydrocarbons activates the AhRs, which are involved in the metabolism (including oxidation) of various endogenous or exogenous substrates. The ligands that induce CYP1 expression are reported to be carcinogenic xenobiotics. Hence, CYP1 enzymes are correlated with the pathogenesis of cancers. Various endogenous substrates are involved in the metabolism of steroid hormones, eicosanoids, and other biological molecules that mediate the pathogenesis of several human diseases. Additionally, CYP1s metabolize and activate/inactivate therapeutic drugs, especially, anti-cancer agents. As the metabolism of drugs determines their therapeutic efficacy, CYP1s can determine the susceptibility of patients to some drugs. Thus, understanding the role of CYP1s in diseases and establishing novel and efficient therapeutic strategies based on CYP1s have piqued the interest of the scientific community.Entities:
Keywords: Cancer; Cytochrome P450 (CYP) 1 enzymes; Drug metabolism; Metabolic diseases; Polymorphism
Year: 2021 PMID: 33484438 DOI: 10.1007/s12272-021-01306-w
Source DB: PubMed Journal: Arch Pharm Res ISSN: 0253-6269 Impact factor: 4.946