Abstract
Lung cancer is one of the most important causes of cancer-related mortality worldwide. Human cytochrome P450 2A13 enzyme (CYP2A13) is predominantly expressed in the respiratory tract and could catalyze various carcinogens. In this study, we quantified CYP2A13 expression in non-small cell lung cancer (NSCLC) tissues and examined the relation between CYP2A13 and clinicopathologic factors. Thirty-five paired lung cancer and normal tissues were studied for the expression of the CYP2A13 gene by using real-time PCR and Western blotting assays. We also investigated the relationship between CYP2A13 expression and clinicopathologic factors such as age, gender, histology and lymph node status in tumor tissues. SPSS (17.0) statistical software was applied for data analysis. The real-time PCR results showed that there was no significant difference in the CYP2A13 mRNA transcript levels between tumor and paired normal tissues in the 35 samples and in 12 paired squamous cell carcinomas. In adenocarcinoma, the expression of CYP2A13 mRNA in tumor tissues was 12.5% of that in adjacent tissues (P < 0.05) and it was not associated with age, gender, histology and lymph node status of the patients. The amounts of CYP2A13 proteins detected by Western blotting assays correlated well with those of the corresponding mRNAs. In conclusion, the expression of CYP2A13 was downregulated in lung adenocarcinoma. CYP2A13 may be involved in the development and progression of lung adenocarcinoma.
Highlights
Human cytochrome P450 (CYP450) enzymes are the principal enzymes involved in the metabolic activation of many compounds, such as drugs, environmental toxicants and chemical carcinogens[1]
Paired-sample t-test was used to analyze the expression levels of cytochrome P450 2A13 enzyme (CYP2A13) mRNA in the 35 breast cancer samples and paired normal tissues and no significant difference was found between them (P = 0.059)
The cytochrome P450 superfamily are the major enzymes involved in drug metabolism and bioactivation, and CYP catalyzes various environmental protoxicants and chemical procarcinogens, such as 4-aminobiphenyl, naphthalene, styrene and toluene[9,10]
Summary
Human cytochrome P450 (CYP450) enzymes are the principal enzymes involved in the metabolic activation of many compounds, such as drugs, environmental toxicants and chemical carcinogens[1]. Variations of P450 enzymes in expression or activity can contribute substantially to inter-individual differences in therapeutic efficacy or toxicant susceptibility[2]. CYP2A13 is highly effective in the metabolic activation of many respiratory-tract toxicants, especially 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK), which is a tobacco-specific carcinogen[5,6,7]. It was found that CYP2A13 is active for the metabolism of aflatoxin B1[8]. The expression of CYP2A13 may substantially influence the incidence of respiratory tumor. We measured the expressions of CYP2A13 in lung cancer and paired normal tissues and examined their relationship with clinicopathological factors
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