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Before the CYP1B1 enzyme activity was characterized, CYP1A1 had been believed to be responsible for virtually all Ba P hydroxylase activity.

CYP1B1 is now known to share with CYP1A1 the PAH-inducible Ba P hydroxylase activity (21). High levels of CYP1A1 m RNA, protein, and enzyme activity are detectable following induction by PAHs; in fact, many of the inducers are in turn metabolized by CYP1A1.

It is thus possible that a “high affinity AHR” patient might develop cancer of the oral cavity or lung after only 20- or 40-pack years of smoking, whereas a “poor affinity AHR” individual might never develop cancer even after more than 100-pack years.

genes that had been developed over more than two decades.

Unlike CYP1A1, CYP1B1 often shows substantial constitutive levels.

CYP1B1 expression is high in vascular endothelial cells, breast, prostate, uterus, epithelial lining of the head and neck, various types of tumors, adrenal cortex, and many other tissues.

AHR-mediated induction of CYP1 enzymes can lead to genotoxicity, mutation, and tumor initiation (6).

When 2,3,7,8-tetrachlorodibenzodioxin (TCDD; dioxin) was realized to be at least 30,000 times more potent than PAHs as an inducer of Ba P hydroxylase, B6 and D2 mice were treated with dioxin, and the effective dose for 50% induction (ED gene, which encodes the AHR that regulates CYP1A1 induction, has amino acid differences responsible for high affinity (in B6) and poor affinity (in D2) receptor that binds dioxin or PAHs (reviewed in Refs. Dose-response curve for hepatic CYP1A1 induction by TCDD in B6 and D2 mice.

Inducible CYP1A1 activity is ubiquitous, located in virtually every tissue of the body including endothelial cells of blood vessels, epithelial cells of the skin and gastrointestinal tract, fetus, and embryo (reviewed in Ref. Of 12 mutations in and near the human ) null mutation (23).

An I462V mutation, often associated with the Msp I mutation, was reported to have increased Ba P hydroxylase activity (23); however, two independent studies showed that c DNA-expressed Ba P hydroxylase activity alleles and lung cancer in cigarette smokers) were found in other laboratories in Japan (26–28) and China (29, 30) but not in Caucasians, African Americans, or Eastern Mediterraneans (10).

It was subsequently shown that PAHs, metabolized to reactive intermediates, bind covalently to nucleic acids and proteins to form adducts (2); thus, the concept of “metabolic activation” by PAH-metabolizing enzymes was born.

Mammalian cell cultures were found to have Ba P hydroxylase (aryl hydrocarbon hydroxylase) activity that becomes highly induced within 12–24 h upon exposure to various PAHs (3).

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