Normal bronchial epithelial cell expression of glutathione transferase P1, glutathione transferase M3, and glutathione peroxidase is low in subjects with bronchogenic carcinoma

Cancer Research

Volumn 60, Issue 6, 2000, Pages 1609-1618

  Crawford, Erin L ^a   Khuder, Sadik A ^a   Durham, Samual J ^a   Frampton, Mark ^b   Utell, Mark ^b   Thilly, William G ^c   Weaver, David A ^a   Ferencak, William J ^a   Jennings, Constance A ^a   Hammersley, Jeffrey R ^a   Olson, Daniel A ^a   Willey, James C ^a  

^a MEDICAL COLLEGE OF OHIO   (United States)

^b UNIVERSITY OF ROCHESTER SCHOOL OF MEDICINE AND DENTISTRY   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; MESSENGER RNA;

ADULT; AGED; ARTICLE; BRONCHUS MUCOSA; CLINICAL ARTICLE; CONTROLLED STUDY; ENVIRONMENTAL EXPOSURE; FEMALE; GENE EXPRESSION; HEREDITY; HUMAN; HUMAN CELL; LUNG CARCINOMA; MALE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

ADOLESCENT; ADULT; AGE FACTORS; AGED; ANALYSIS OF VARIANCE; BRONCHI; CARCINOMA, BRONCHOGENIC; CELL LINE; CELLS, CULTURED; EPITHELIAL CELLS; FEMALE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE EXPRESSION REGULATION, NEOPLASTIC; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; HUMANS; LUNG NEOPLASMS; MALE; MIDDLE AGED; REPRODUCIBILITY OF RESULTS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; SEX FACTORS; SMOKING;

EID: 0034654175     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (55)

1. Church, D. F., and Pryor, W. A. Free-radical chemistry of cigarette smoke and its toxicological implications. Environ. Health Perspect., 64: 111-126, 1985.
2. Niki, E., Minamisawa, S., Oikawa, M., and Komuro, E. Membrane damage from lipid oxidation induced by free radicals and cigarette smoke. Ann. NY Acad. Sci., 686: 29-37, 1993.
3. Frampton, M. W., Samet, J. M., and Utell, M. J. Environmental factors and atmospheric pollutants. Semin. Respir. Infect., 6: 185-193, 1991.
4. Anttila, S., Luostarinen, L., Hirvonen, A., Elovaara, E., Karjalainen, A., Nurminen, T., Hayes, J. D., Vainio, H., and Ketterer, B. Pulmonary expression of glutathione S-transferase M3 in lung cancer patients: Association with GSTM1 polymorphism, smoking, and asbestos exposure. Cancer Res., 55: 3305-3309, 1995.
5. Quinlan, T., Spivack, S., and Mossman, B. T. Regulation of antioxidant enzymes in lung after oxidant injury. Environ. Health Perspect., 102: 79-87, 1994.
6. Avissar, N., Finkelstein, J. N., Horowitz, S., Willey, J. C., Coy, E., Frampton, M. W., Watkins, R. H., Khullar, P., Xu, Y., and Cohen, H. J. Extracellular glutathione peroxidase in human lung epithelial lining fluid and in lung cells. Am. J. Physiol., 270: L173-L182, 1996.
7. Borm, P. J. A., and Driscoll, K. Particles, inflammation and respiratory tract carcinogenesis. Toxicol. Lett. (Amst.), 88: 109-113, 1996.
8. Cantin, A., and Crystal, R. G. Oxidants, antioxidants and the pathogenesis of emphysema. Eur. J. Respir. Dis. Suppl., 139: 7-17, 1985.
9. Mannervik, B., and Danielson, U. H. Glutathione transferases - structure and catalytic activity. CRC Crit. Rev. Biochem., 23: 283-337, 1988.
10. Mannervik, B., Alin, P., Guthenberg, C. Jensson, H., Tahir, M. K., Warholm, M., and Jornvall, H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc. Natl. Acad. Sci. USA, 82: 7202-7206, 1985.
11. Meyer, D. J., Coles, B., Pemble, S. E., Gilmore, K. S., Fraser, G. M., and Ketterer, B. θ, a new class of glutathione transferases purified from rat and man. Biochem. J., 274: 409-414, 1991.
12. Pemble, S. E., Wardle, A. F., and Taylor, J. B. Glutathione S-transferase class κ: characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem. J., 319: 749-754, 1996.
13. Hayes, J. D., and Pulford D. J. The glulathione S-transferase supergene family: regulation of GST* and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol., 30: 445-600, 1995.
14. Anttila, S., Hirvonen, A., Vainio, H., Husgafvel-Pursiainen, K., Hayes, J. D., and Ketterer, B. Immunohistochemical localization of glutathione S-transferases in human lung. Cancer Res., 53: 5643-5648, 1993.
15. Morgenstern, R., Lundqvist, G., Hancock, V., and DePierre, J. W. Studies on the activity and activation of rat liver microsomal glutathione transferase, in particular with a substrate analogue series. J. Biol. Chem., 263: 6671-6675, 1988.
16. Strange, R. C., Matharoo, B., Faulder, G. C., Jones, P., Cotton, W., Elder, J. B., and Deakin, M. The human glutathione S-transferases: a case-control study of the incidence of the GST1 0 phenotype in patients with adenocarcinoma. Carcinogenesis (Lond.), 12: 25-28, 1991.
17. Tsuchida, S., and Sato, K. Glutathione transferases and cancer. Crit. Rev. Biochem. Mol. Biol., 27, 337-384, 1992.
18. Anderson, C., Mosialou, E., Weinander, R., and Morgenstern, R. Enzymology of microsomal glutathione S-transferase. Adv. Pharmacol., 27: 19-35, 1994.
19. Takahashi, K., Akasaka, M., Yamamoto, Y., Kohayashi, C., Mizoguchi, J., and Koyama, J. Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. J. Biochem., 108: 145-148, 1990.
20. Chu, F., Esworthy, R. S., Doroshow, J. H., Doan, K., and Liu., X. Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood, 79: 3233-3238, 1992.
21. Morgenstern, R., and DePierre, J. W. Membrane-bound glutathione transferase. Biochem. Soc. Trans., 15: 719-721, 1987.
22. Singhal, S. S., Gupta, S., Ahmad, H., Sharma, R., and Awasthi, Y. C. Characterization of a novel α-class anionic glutathione S-transferase isozyme from human liver. Arch. Biochem. Biophys., 279: 45-53, 1990.
23. Comstock, K. E., Widersten, M., Hao, X. Y., Henner, W. D., and Mannervik, B. A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes. Arch. Biochem. Biophys., 311: 487-495, 1994.
24. Kano, T., Sakai, M., and Muramatsu, M. Structure and expression of a human class π glutathione S-transferase messenger RNA. Cancer Res., 47: 5626-5630, 1987.
25. Tsuchida, S., Sekine, Y., Shineha, R., Nishihira, T., and Sato, K. Elevation of the placental glutathione S-transterase form (GST-π) in tumor tissues and the levels in sera of patients with cancer. Cancer Res., 49: 5225-5229, 1989.
26. Moscow, J. A., Fairchild, C. R., Madden, M. J., Ransom, D. T., Wieand, H. S., O'Brien, E. E., Poplack, D. G., Cossman, J., Myers, C. E., and Cowan, K. H. Expression of anionic glutathione S-transferase and P-glycoprotein genes in human tissues and tumors. Cancer Res., 49: 1422-1428, 1989.
27. Ketterer, B., Harris, J. M., Talaska, G., Meyer, D. J., Pemble, S. E., Taylor, J. B., Lang, N. P., and Kadlubar, F. F. The human glutathione S-transferase supergene family, its polymorphism, and its effects on susceptibility to lung cancer. Environ. Health Perspect., 98: 87-94, 1992.
28. Mannervik, B., Castro, V., Danielson, U. H., Platz, A., Mansson, J., and Ringbong, U. Expression of class π glutathione transferase from drug-resistant human melanoma cells. Proc. Am. Assoc. Cancer Res., 28: 19, 1987.
29. Howie, A. F., Forrester, L. M., Glancey, M. J., Schlager, J. J., Powis, G., Beckett, G. J., Hayes, J. D., and Wolf, C. R. Glutathione S-transferase and glutathione peroxidase expression in normal and tumour human tissues. Carcinogenesis (Lond.), 11: 451-458, 1990.
30. Seidegard, J., Pero, R. W., Markowitz, M. M., Roush, G., Miller, D. G., and Beattie, E. J. Isoenzyme(s) of glutathione transferase (class Mu) as a marker for the susceptibility to lung cancer: a follow up study. Carcinogenesis (Lond.), 11: 33-36, 1990.
31. Nazar-Stewart, V. Motulsky, A. G., Eaton, D. L., White, E., Hornung, S. K., Leng, Z., Stapleton, P., and Weiss, N. S. The glutathione S-transferase mu polymorphism as a marker for susceptibility to lung carcinoma. Cancer Res., 53: 2313-2318, 1993.
32. Zhong, S., Howie, A. F., Ketterer, B., Taylor, J., Hayes, J. D., Beckett, G. J., Wathen, C. G., Wolf, C. R., and Spurr, N. K. Glutathione S-transferase mu locus: use of genotyping and phenotyping assays to assess association with lung cancer susceptibility. Carcinogenesis (Lond.), 12: 1533-1537, 1991.
33. Willey, J. C., Crawford, E. L., Jackson, C. M., Weaver, D. A., Hoban, J. C., Khuder, S. A., and DeMuth, J. P. Expression measurement of many genes simultaneously by quantitative RT-PCR using standardized mixtures of competitive templates. Am. J. Respir. Cell Mol. Biol., 19: 6-17, 1998.
34. Willey, J. C., Coy, E., Brolly, C., Utell, M. J., Frampton, M. W., Hammersley, J., Thilly, W. G., Olson, D., and Cairns, K. Xenohiotic metabolism enzyme gene expression in human bronchial epithelial and alveolar macrophage cells. Am. J. Respir. Cell Mol. Biol., 14: 262-271, 1996.
35. Willey, J. C., Coy, E. L., Frampton, M. W., Torres, A., Apostolakos, M. J., Hoehn, G., Schuermann, W. H., Thilly, W. G., Olson, D. E., Hammersley, J. R., Crespi, C. L., and Utell, M. J. Quantitative RT-PCR measurement of cytochromes p450 1A1, 1B1, and 2B7, microsomal epoxide hydrolase, and NADPH oxidoreductase expression in lung cells of smokers and non-smokers. Am J. Respir. Cell Mol. Biol., 17: 114-124, 1997.
36. DeMuth, J. P., Jackson, C. M., Weaver, D. A., Crawford, E. L., Durzinsky, D. S., Durham, S. J., Zaher, A., Phillips, E. R., Khuder, S. A., and Willey, J. C. The gene expression index c-myc x E2F-1/p21 is highly predictive of malignant phenotype in human bronchial epithelial cells. Am. J. Respir. Cell Mol. Biol., 19: 18-24, 1998.
37. Chomczynski, P. A reagent for the single-step simultaneous isolation of RNA, DNA and proteins from cell and tissue samples. Anal. Biochem., 162: 156-159, 1993.
38. Apostolakos, M. J., Schuermann, W. H. T., Frampton, M. W., Utell, M. J., and Willey, J. C. Measurement of gene expression by multiplex competitive polymerase chain reaction. Anal. Biochem., 213: 277-284, 1993.
39. Gilliland, G., Perrin, S., Blanchard, K., and Bunn, H. F. Analysis of cytokine mRNA and DNA: Detection and quantification by competitive polymerase chain reaction. Proc. Natl. Acad. Sci. USA, 87: 2725-2729, 1990.
40. Celi, F. S., Zenilman, M. E., and Shuldiner, A. R. A rapid and versatile method to synthesize internal standards for competitive PCR. Nucleic Acids Res., 21: 1047, 1993.
41. Sharma, R., Haque, A. K., Awasthi, S., Singh, S. V., Piper, J. T., and Awasthi, Y. C. Differential carcinogenicity of benzo[a]pyrene in male and female CD-1 mouse lung. J. Toxicol. Environ. Health, 52: 45-62, 1997.
42. Harries, L. W., Stubbins, M. J., Forman, D., Howard, G. C., and Wolf, C. R. Identification of genetic polymorphisms at the glutathione S-transferase π locus and association with susceptibility to bladder, testicular and prostate cancer. Carcinogenesis (Lond.), 18: 641-644, 1997.
43. Ryberg, D., Skaug, V., Hewer, A., Phillips, D. H., Harries, L. W., Wolf, C. R., Ogreid, D., Ulvik, A., Vu, P., and Haugen, A. Genotypes of glutathione transferase M1 and P1 and their significance for lung DNA adduct levels and cancer risk. Carcinogenesis (Lond.), 18: 1285-1289, 1997.
44. Moscow, J. A., Townsend, A., J., Goldsmith, M. E., Whang-Peng, J., Vickers, P. J., Poisson, R., Legault-Poisson, S., Myers, C. E., and Cowan, K. H. Isolation of the human anionic glulathione S-transferase cDNA and the relation of its gene expression to estrogen-receptor content in primary breast cancer. Proc. Natl. Acad. Sci. USA, 85: 6518-6522, 1988.
45. Heuvel, J. P. V., Clark, G. C., Kohn, M. C., Tritscher, A. M., Greenlee, W. F., Lucier, G. W., and Bell, D. A. Dioxin-responsive genes: examination of dose-response relationships using quantitative reverse transcriptase-polymerase chain reaction. Cancer Res., 54: 62-68, 1994.
46. Therond, P., Gerbaud, P., Dimon, S., Anderson, W. B., Evain-Brion, D., and Raynaud, F. Antioxidant enzymes in psoriatic fibroblasts and erythrocytes. J Invest. Dermatol., 106: 1325-1328, 1996.
47. Ponte, P., Ng, S., Engel, J., Gunning, P., and Kedes, L. Evolutionary conservation in the untranslated regions of actin mRNAs: DNA sequence of a human β-actin cDNA. Nucleic Acids Res., 12: 1687-1696, 1984.
48. Sukenaga, Y., Ishida, K., Takeda, T., and Takagi, K. cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Res., 15: 7178, 1987.
49. Seidegard, J., Vorachek, W. R., Pero, R. W., and Pearson, W. R. Hereditary differences in the expression of the human glutathione transferase active on trans-stilbene oxide are due to a gene deletion. Proc. Natl. Acad. Sci. USA, 85: 7293-7297, 1988.
50. Vorachek, W. R., Pearson, W. R., and Rule, G. S. Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc. Natl. Acad. Sci. USA, 88: 4443-4447, 1991.
51. Comstock, K. E., Johnson, K. J., Rifenbery, D., and Henner, W. D. Isolation and analysis of the gene and cDNA for a human mu class glutathione S-transferase, GSTM4. J. Biol. Chem., 268: 16958-16965, 1993.
52. Takahashi, Y., Campbell, E. A., Hirata, Y., Takayama, T., and Listowsky, I. A basis for differentiating among the multiple human mu-glutathione S-transferases and molecular cloning of brain GSTM5. J. Biol. Chem., 268: 8893-8898, 1993.
53. Campbell, E., Takahashi, Y., Abramovitz, M., Peretz, M., and Listowsky, I. A distinct human testis and brain μ-class glutathione S-transferase: Molecular cloning and characterization of a form present even in individuals lacking hepatic type μ isoenzymes. J. Biol. Chem., 265: 9188-9193, 1990.
54. Pemble, S., Scroeder, K. R., Spencer, S. R., Meyer, D. J., Hallier, E., Bolt, H. M., Ketterer, B., and Taylor, J. B. Human glutathione S-transferase θ (GSTT1): cDNA cloning and the characterization of a genetic polymorphism. Biochem. J., 300: 271-276, 1994.
55. DeJong, J. L., Morgenstern, R., Jornvall, H., DePierre, J. W., and Tu, C. D. Gene expression of rat and human microsomal glutathione S-transferases. J. Biol. Chem., 263: 8430-8436, 1988.