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FUNCTIONAL EFFECTS OF CYP1A2, NAT1, AND NAT2 GENETIC VARIANTS IN NUCLEOTIDE EXCISION REPAIR DEFECIENT HUMAN FIBROBLASTS: IMPLICATIONS FOR TOXICOLOGICAL RISK FROM ENVIRONMENTAL ARYLAMINES Carmine S. Leggett August6,2010 Arylamine N-acetyltransferase 1 (NAT1) and 2 (NAT2) catalyze the detoxification and/or activation of aromatic and heterocyclic amine carCinogens by two pathways. This metabolism reaction can lead to the detoxification by Nacetylation, or bioactivation by a-acetylation often preceded by CYP450 hydroxylation. Human NAT2 polymorphisms are characterized by rapid, intermediate, and slow acetylator phenotypes, thus resulting in differences in the rate of arylamine metabolism and consequently cancer risk. We have constructed nucleotide excision repair-deficient human cell model expressing human CYP1A2 and human NAT1and NAT2 in order to investigate carcinogen metabolism and cancer susceptibility in human cells. In this study we introduce the utilization of SV40-transformed human fibroblasts (GM4429) to examine the functional effects of human NAT2 haplotypes, in the presence of human NAT1. Many carCinogens, such as 4aminobiphenyl, are metabolized by both NAT1 and NAT2, consequently both isozymes have toxicologically significant functions in the metabolism of

Functional effects of CYP1A2, NAT1, and NAT2 genetic variants in nucleotide excision repair-deficient human fibroblasts : implications for toxicological risk from environmental arylamines.