Archives of Pharmacal Research

  • 제25권3호
  • /
  • Pages.375-380
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  • 2002
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  • 0253-6269(pISSN)
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  • 1976-3786(eISSN)
대한약학회 (The Pharmaceutical Society of Korea)
권호 표지

No Role of Protected Region B of Human Cytochrome P4501A2 Gene (CYP1A2) As an AP-1 Response Element

  • Chung, In-Jae (College of Pharmacy, Duksung Womens University) ;
  • Jung, Ki-Hwa (College of Pharmacy, Duksung Womens University)
  • 발행 : 2002.06.01
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초록

Cytochrome P4501A2 (CYP1A2) is a member of the cytochrome P450 family of isozymes involved in the phase I drug metabolism of vertebrates. CYP1A2 is responsible for the activation of a number of aromatic amines to mutagenic and carcinogenic forms. Thus, the level of CYP1A2, which varies among different populations, may determine an individual's susceptibility to these chemicals. We have previously reported on the importance of a cis element named PRB (protected region B) in the regulation of human Cytochrome P4501A2 (CYP1A2) gene, which appeared to act as a positive regulatory element. Closer examination of the PRB sequence (-2218 to -2187 bp) revealed a putative AP-1 binding site, TGACTAA, at -2212 bp (Chung and Bresnick, 1997). To elucidate the role of AP-1 in CYP1A2 regulation, we transiently overexpressed c-Jun and c-Fos transcription factors in human hepatoma HepG2 cells, and examined their influence on the CYP1A2 promoter activity by reporter gene assays. Cotransfection of the c-Jun and the c-Fos expression vectors increased the induced transactivation by five to six fold from the CYP1A2 promoter constructs. However, deletion of the PRB element did not affect the degree of activation by the c-Jun and the c-Fos. Therefore, it is unlikely that the c-Jun and the c-Fos activate the CYP1A2 promoter through this AP-1 consensus-like sequence in the PRB region.

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참고문헌

  1. Abate, C., Baker, S. J., Lees-Miller, S. P., Anderson, C. W., Marshak, D. R., and Curran, T., Dimerization and DNA binding alter phosphorylation of Fos and Jun. Proc. Natl. Acad. Sci. USA., 90, 6766-6770 (1993) https://doi.org/10.1073/pnas.90.14.6766
  2. Adamson, R. H., Thorgeirsson, U. P, Snyderwine, E. G., Thorgeirsson, S. S., Reeves, J., Dalgard, D. W., Takayama, S., and Sugimura, T., Carcinogenicity of 2-amino-3-methylimidazo (4,5-f)quinoline in nonhuman primates: induction of tumors in three macaques. Gann,. 81,10-14(1990) https://doi.org/10.1111/j.1349-7006.1990.tb02500.x
  3. Aoyama, T., Gonzalez, F. J., and Gelboin, H.V, Mutagen activation by cDNA-expressed P(1)450, P(3)450, and P450a. Mol. Carcinogesis., 1,253-259 (1989) https://doi.org/10.1002/mc.2940010408
  4. Angel, P., and Karin, M., The role of jun, fos, and the AP-1 complex in cell-proliferation and transformation. Biochem. Biophys. Acta, 1072, 129-157 (1991)
  5. Angel, P., Hattori, K., Smeal, T., and Karin, M., The jun proto-oncogene is positively autoregulated by its product, Jun/AP1. Cell, 55, 875-885(1988) https://doi.org/10.1016/0092-8674(88)90143-2
  6. Battula, N., Sagara, J., and Gelboin, H. V., Expression of P1-450 and P3-450 DNA coding sequences as enzymatically active cytochrome P-450 in mammalian cells. Proc. Natl. Acad. Sci. USA, 84,4073-4077 (1987) https://doi.org/10.1073/pnas.84.12.4073
  7. Brasier, A. R., Tate, J. E., and Habener, J. F., Optimized use of the firefly luciferase assay as a reporter gene in mammalian cell lines. Biotechniques, 7,1116-1122 (1989)
  8. Chung, I., and Bresnick, E., 3-Methylcholanthrene-mediated induction of cytochrome P4501A2 in human hepatoma HepG2 cells as quantified by the reverse transcription-polymerase chain reaction. Arch. Biochem. Biophys., 314, 75-81 (1994) https://doi.org/10.1006/abbi.1994.1413
  9. Chung, I., and Bresnick, E., Regulation of the constitutive expression of the human CYP1A2 gene: cis-elements and their interactions with proteins. Mol. Pharmacol., . 47, 677-685(1995)
  10. Chung, I. and Bresnick, E., Identification of positive and negative regulatory elements of the human cytochrome P4501A2 (CYP1A2) gene. Arch. Biochem. Biophys., 338,220-226 (1997) https://doi.org/10.1006/abbi.1996.9815
  11. Groves, W. E., Davis, F. L., and Shells, B. H., Spectrophotomeric determination of microgram quantities of protein without nucleic acid interference. Anal. Biochem., 22, 195-210 (1968) https://doi.org/10.1016/0003-2697(68)90307-2
  12. Hai, T., and Curran, T., Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc. Natl. Acad. Sci. USA, 88, 3720-3724 (1991) https://doi.org/10.1073/pnas.88.9.3720
  13. loannides, C., and Parke, D. V., Induction of cytochrome P4501 as indicator of potential chemical carcinogenesis. Drug Metab. Rev., 25, 485-501 (1993) https://doi.org/10.3109/03602539308993983
  14. Jones, N. C., Rigby, P.W. J., and Ziff, E. B., Transacting protein factors and the regulation of eukaryotic transcription: lessons from studies on DNA tumor viruses. Genes and Development. Vol. 2. New York: Cold Spring Harbor Laboratory. (1988)
  15. Kalow, W., and Tang, B. K., Use of caffeine metabolite ratio to explore CYP1A2 and xanthine oxidase activities. Clin. Pharmacol. Ther., 50, 508-519 (1991) https://doi.org/10.1038/clpt.1991.176
  16. Lamph , W. W., Wamsley, P., Corpi, P-S., and Verma, I. M., Induction of proto-oncogene Jun/AP-1 by serum and TPA. Nature, 334, 629-631 (1988) https://doi.org/10.1038/334629a0
  17. Lee, W., Mitchell, P., and Tjian, R., Purified transcriptional factor AP-1 interacts with TPA-inducible enhancer elements. Cell, 49,741-752 (1987) https://doi.org/10.1016/0092-8674(87)90612-X
  18. Nakajima, M., Yokoi, T., Mizutani, M., Shin, S., Kadlubar, F. F, and Kamataki, T., Phenotyping of CYP1A2 in Japaneses population by analysis of caffeine urinary metabolite: absence of mutation prescribing the phenotype in the CYP1A2 gene. Cancer Epidemiol, Biomarkers Prev., 3, 413-421(1994)
  19. Nelson, D. R., Koymans, L., Kamataki, T., Stegeman, J. J., Feyereisen, R., Waxman, D., Waterman, M. R., Gotoh, O., Coon, M. J., Eastabrook, .R W, Gunsalus, I. C., and Nebert, D. W, P-450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature. Pharmacogenetics, 6,1-42 (1996) https://doi.org/10.1097/00008571-199602000-00002
  20. Quattrochi, L. C., Shih, H., and Pickwell, G. V., Induction of the Human CYP1A2 enhancer by phorbol ester. Arch. Biochem. Biophys., 350,41-48 (1998) https://doi.org/10.1006/abbi.1997.0491
  21. Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular Cloning: A Laboratory Manual. 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N. Y. (1989)
  22. Schweikl, H., Taylor, J. A., Kitareewan, T. S., Linko, P., Nagomey, D., and Goldstein, J. A., Expression of CYP1A1 and CYP1A2 genes in human liver. Pharmacogenetics, 3, 239-249 (1993) https://doi.org/10.1097/00008571-199310000-00003
  23. Sesardic, D., Boobis, A. R., Edwards, R. J., and Davies, D. S., A form of cytochrome P450 in man, orthlogous to form d in the rat, catalyses the O-deethylation of phenacetin and is inducible by cigarette smoking. Br. J. Clin. Pharmacol., 26,363-372 (1988) https://doi.org/10.1111/j.1365-2125.1988.tb03393.x
  24. Sesardic, D., Pasanen, M., Pelkonen, O., and Boobis, A. R., Differential expression and regulation of members of the cytochrome P4501A gene subfamily in human tissues. Carcinogenesis., 11, 1183-1188 (1990) https://doi.org/10.1093/carcin/11.7.1183
  25. Sonnenberg, J. L., Rauscher, F J., III, Morgan, J. I., and Curran, T., Regulation of proenkephalin by Fos and Jun. Science, 246, 1622-1625 (1989) https://doi.org/10.1126/science.2512642
  26. Suzuki, T., Okuno, H., Yoshida, T., Endo, T., Nishina, H,., and Iba., H., Difference in transcriptional regulatory function between c-fos and fra-2. Nucleic Acids Res., 19,5537-5542(1991) https://doi.org/10.1093/nar/19.20.5537
  27. Wrighton, S. A., Campanile, C., Thomas, P. E., Paines, S. L., Watkins, P. B., Parker, G., Mendex-Picon, G., Haniu, M., Shively, J. E., Levin, W., and Guzelian, P. S., Mol. Pharmacol., 29, 405-410 (1986)