참고문헌
- 해리슨 내과학 편찬위원회. 해리슨 내과학. 서울, 정담 출판사, pp 1317-1324, 1997
- 이은우, 김영철 역. 머크 매뉴얼. 서울, 한우리, p 702, 2667, 2002
- 윤창열, 김용진. 난경연구집성. 서울, 주민출판사, p 768, 769, 2002
- 許俊. 東醫寶鑑. 서울, 법인문화사, p 1433, 1996
- 李梴. 醫學入門. 서울, 남산당, p 212, 213, 1980
- 전국한의과대학 폐계내과학교실편저. 동의폐계내과학. 서울, 한문화사, p 87, 526, 2002
- 김영환. 분자생물학적 측면에서의 폐암의 발생. 녹십자의보, 27(3):152-157, 1999
- 임재형, 김훈, 변미권, 감철우, 박동일. 인체폐암세포의 증식 및 prostaglandin E2 생성에 미치는 청조구폐탕의 영향에 관한 연구. 동의생리병리학회지 20(4):966-972, 2006
- 조인주, 감철우, 김기탁, 박동일. 인체폐암세포에서 Bcl-2 발현저하 및 caspase 활성을 통한 청조구폐탕의 apoptosis 유발에 관한 연구. 동의생리병리학회지 21(1):93-97, 2007
- 홍수현, 박철, 홍상훈, 최병태, 이용태, 박동일, 최영현. 어성초 메탄올 추출물에 의한 A549 인체 폐암세포 사멸유도에 관한 연구. 동의생리병리학회지 20(6):1584-1592, 2006
- 박봉규, 박동일. 천금위경탕의 인체 폐암 세포 증식억제에 관한 연구. 동의생리병리학회지 18(4):1147-1153, 2004
- 이성열, 김원일, 박동일. 길경이 인체 폐암세포에 미치는 영향에 대한 실험적 연구. 동의생리병리학회지 17(4):1019-1030, 2003
- Evans, V.G. Multiple pathways to apoptosis. Cell Biol. Int 17: 461-476, 1993 https://doi.org/10.1006/cbir.1993.1087
- Arends, M.J., Morris, R.G., Wyllie, A.H. Apoptosis. The role of the endonuclease. Am. J. Pathol. 136: 593-608, 1990
- Zhan, Q., Fan, S., Bae, I., Guillouf, C., Liebermann, D.A., OConnor, P.M., Fornace, A.J. Jr. Induction of bax by genotoxic stress in human cells correlates with normal p53 status and apoptosis. Oncogene. 9: 3743-3751, 1994
- Shi. L., Nishioka, W.K., Th'ng, J., Bradbury, E.M., Litchfield, D.W., Greenberg, A.H. Premature p34cdc2 activation required for apoptosis. Science. 263: 1143-1145, 1994 https://doi.org/10.1126/science.8108732
- Chiarugi, V., Magnelli, L., Basi, G. Apoptosis and the cell cycle. Cell. Mol. Biol. Res. 40: 603-612, 1994
- Reed, J.C. Bcl-2 family proteins. Oncogene. 17: 3225-3236, 1998 https://doi.org/10.1038/sj.onc.1202591
- Miyashita, T., Reed, J.C. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell. 80: 293-299, 1995 https://doi.org/10.1016/0092-8674(95)90412-3
- El-Deiry, W.S., Harper, J.W., O'Connor, P.M., Velculescu, V.E., Canman, C.E., Jackman, J., Pietenpol, J.A., Burrell, M., Hill, D.E., Wang, Y., Wiman, K.G., Mercer, W.E., Kastan, M.B., Kohn, K.W., Elledge, S.J., Kinzler, K.W., Vogelstain, B. WAF1/CIP1 is induced in p53-mediated G1 arrest and apoptosis. Cancer Res. 54: 1169-1174, 1994
- Kluck, R.M., Bossy-Wetzel, E., Green, D.R., Newmeyer, D.D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 275: 1132-1136, 1997 https://doi.org/10.1126/science.275.5303.1132
- Nagata, S. Apoptosis by death factor. Cell. 88: 355-365, 1997 https://doi.org/10.1016/S0092-8674(00)81874-7
- Tsujimoto, Y. Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria. Genes Cells. 3: 697-707, 1998 https://doi.org/10.1046/j.1365-2443.1998.00223.x
- Cheng, J.Q., Jiang, X., Fraser, M., Li, M., Dan, H.C., Sun, M., Tsang, B.K. Role of X-linked inhibitor of apoptosis protein in chemoresistance in ovarian cancer: possible involvement of the phosphoinositide-3 kinase/Akt pathway. Drug Resist. Update. 5: 131-146, 2002 https://doi.org/10.1016/S1368-7646(02)00003-1
- Salvesen, G.S., Duckett, C.S. IAP proteins: blocking the road to death's door. Nat. Rev. Mol. Cell. Biol. 3: 401-410, 2002 https://doi.org/10.1038/nrm830
- Holcik, M., Gibson, H., Korneluk, R.G. XIAP: apoptotic brake and promising therapeutic target. Apoptosis. 6: 253-261, 2001 https://doi.org/10.1023/A:1011379307472
- LaCasse, E.C., Baird, S., Korneluk, R.G., MacKenzie, A.E. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene. 17: 3247-3259, 1998 https://doi.org/10.1038/sj.onc.1202569
- Giercksky, K.E. COX-2 inhibition and prevention of cancer. Best Pract. Res. Clin. Gastroenterol. 15: 821-833, 2001 https://doi.org/10.1053/bega.2001.0237
- Turini, M.E., DuBois, R.N. Cyclooxygenase-2: a therapeutic target. Annu. Rev. Med. 53: 35-57, 2002 https://doi.org/10.1146/annurev.med.53.082901.103952
- Chiarugi, V., Magnelli, L., Gallo, O. Cox-2, iNOS and p53 as play-makers of tumor angiogenesis. Int. J. Mol. Med. 2: 715-719, 1998
-
Surh, Y.J., Chun, K.S., Cha, H.H., Han, S.S., Keum, Y.S., Park, K.K., Lee, S.S. Molecular mechanisms underlying chemopreventive activities of anti-inflammatory phytochemicals: down-regulation of COX-2 and iNOS through suppression of NF-
$\kappa$ B activation. Mutat. Res. pp 243-268, 480-481, 2001 - Thun, M.J., Henley, S.J., Patrono, C. Nonsteroidal anti-inflammatory drugs as anticancer agents: mechanistic, pharmacologic, and clinical issues. J. Natl. Cancer Inst. 94: 252-266, 2002 https://doi.org/10.1093/jnci/94.4.252
- oole, J.C., Andrews, L.G., Tollefsbol, T.O. Activity, function, and gene regulation of the catalytic subunit of telomerase (hTERT). Gene. 269: 1-12, 2001 https://doi.org/10.1016/S0378-1119(01)00440-1
- Kyo, S., Inoue, M. Complex regulatory mechanisms of telomerase activity in normal and cancer cells: How can we apply them for cancer therapy. Oncogene. 21: 688-697, 2002 https://doi.org/10.1038/sj.onc.1205163
- Fabian, D., Koppel, J., Maddox-Hyttel, P. Apoptotic processes during mammalian preimplantation development. Theriogenology 64: 221-231, 2005 https://doi.org/10.1016/j.theriogenology.2004.11.022
- Baek, S.J., Kim, J.S., Nixon, J.B., DiAugustine, R.P., Eling, T.E. Expression of NAG-1, a transforming growth factor-beta superfamily member, by troglitazone requires the early growth response gene EGR-1. J Biol Chem. 279: 6883-6892, 2004 https://doi.org/10.1074/jbc.M305295200
- Liu, C., Rangnekar, V.M., Adamson, E., Mercola, D. Suppression of growth and transformation and induction of apoptosis by EGR-1. Cancer Gene Ther 5: 3-28, 1998
- Calogero, A., Arcella, A., de Gregorio, G., Porcellini, A., Mercola, D., Liu, C., Lombari, V., Zani, M., Giannini, G., Gagliardi, F.M., Caruso, R., Gulino, A., Frati, L., Ragona, G. The early growth response gene EGR-1 behaves as a suppressor gene that is down-regulated independent of ARF/Mdm2 but not p53 alterations in fresh human gliomas. Clin Cancer Res 7: 2788-2796, 2001
- Huang, R.P., Fan, Y., de Belle, I., Niemeyer, C., Gottardis, M.M., Mercola, D., Adamson, E.D. Decreased Egr-1 expression in human, mouse and rat mammary cells and tissues correlates with tumor formation. Int J Cancer 72: 102-109, 1997 https://doi.org/10.1002/(SICI)1097-0215(19970703)72:1<102::AID-IJC15>3.0.CO;2-L
- de Belle, I., Huang, R.P., Fan, Y., Liu, C., Mercola, D., Adamson, E.D. p53 and Egr-1 additively suppress transformed growth in HT1080 cells but Egr-1 counteracts p53-dependent apoptosis. Oncogene 18: 3633-3642, 1999 https://doi.org/10.1038/sj.onc.1202696
- Virolle, T., Adamson, E.D., Baron, V., Birle, D., Mercola, D., Mustelin, T., de Belle, I. The Egr-1 transcription factor directly activates PTEN during irradiation-induced signalling. Nat Cell Biol 3: 1124-1128, 2001 https://doi.org/10.1038/ncb1201-1124
- Huang, R.P., Liu, C., Fan, Y., Mercola, D., Adamson, E.D. Egr-1 negatively regulates human tumor cell growth via the DNA-binding domain. Cancer Res 55: 5054-5062, 1995
- Eling, T.E., Baek, S.J., Shim, M., Lee, C.H. NSAID activated gene (NAG-1), a modulator of tumorigenesis. J Biochem Mol Biol 39: 649-655, 2006 https://doi.org/10.5483/BMBRep.2006.39.6.649
-
Baek, S.J., Kim, K.S., Nixon, J.B., Wilson, L.C., Eling, T.E. Cyclooxygenase inhibitors regulate the expression of a TGF-
$\beta$ superfamily member that has proapoptotic and antitumorigenic activities. Mol Pharmacol 59: 901-908, 2001 https://doi.org/10.1124/mol.59.4.901 -
Tan, M., Wang, Y., Guan, K., Sun, Y. PTGF-
$\beta$ , a type beta transforming growth factor (TGF-$\beta$ ) superfamily member, is a p53 target gene that inhibits tumor cell growth via TGF-$\beta$ signaling pathway. Proc Natl Acad Sci USA 97: 109-114, 2000 -
Li, P.X., Wong, J., Ayed, A., Ngo, D., Brade, A.M., Arrowsmith, C., Austin, R.C., Klamut, H.J. Placental transforming growth factor-
$\beta$ is a downstream mediator of the growth arrest and apoptotic response of tumor cells to DNA damage and p53 overexpression. J Biol Chem 275: 20127-20135, 2000 https://doi.org/10.1074/jbc.M909580199 - Baek, S.J., Wilson, L.C., Eling, T.E. Resveratrol enhances the expression of non-steroidal anti-inflammatory drug-activated gene (NAG-1) by increasing the expression of p53. Carcinogenesis 23: 425-434, 2002 https://doi.org/10.1093/carcin/23.3.425
- Koff, A., Giordano, A., Desai, D., Yamashita, K., Harper, J.W., Elledge, S., Nishimoto, T., Morgan, D.O., Franza, B.R., Roberts, J.M. Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle. Science 257: 1689-1694, 1992 https://doi.org/10.1126/science.1388288
- Zeng, Y.X., el-Deiry, W.S. Regulation of p21WAF1/CIP1 expression by p53-independent pathways. Oncogene 12: 1557-1564, 1996
- Morgan, D.O. Principles of CDK regulation. Nature 374: 131-134, 1995
- Harper, J.W., Adami, G.R., Wei, N., Keyomarsi, K., Elledge, S.J. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75: 805-816, 1993 https://doi.org/10.1016/0092-8674(93)90499-G
- Xiong, Y., Hannon, G., Zhang, H., Casso, D., Kobayashi, R., Beach, D. p21 is a universal inhibitor of cyclin kinases. Nature 366: 701-704, 1993 https://doi.org/10.1038/366701a0
- Vainio, H. Is COX-2 inhibition a panacea for cancer prevention? Int J Cancer 94: 613-614, 2001 https://doi.org/10.1002/ijc.1518
- Dempke, W., Rie, C., Grothey, A., Schmoll, H.J. Cyclooxygenase-2: a novel target for cancer chemotherapy? J Cancer Res Clin Oncol 127: 411-417, 2001 https://doi.org/10.1007/s004320000225
- Sawaoka, H., Tsuji, S., Tsujii, M., Gunawan, E.S., Sasaki, Y., Kawano, S., Hori, M. Cyclooxygenase inhibitors suppress angiogenesis and reduce tumor growth in vivo. Lab Invest 79: 1469-1477, 1999
-
Yamamoto, Y., Gaynor, R.B. Therapeutic potential of inhibition of the NF-
${\kappa}B$ pathway in the treatment of inflammation and cancer. J Clin Invest 107: 135-142, 2001 https://doi.org/10.1172/JCI11914 - Cerni, C. Telomeres, telomerase, and myc. An update. Mutat Res 462: 31-47, 2000 https://doi.org/10.1016/S1383-5742(99)00091-5