메뉴 건너뛰기




Volumn 64, Issue 7, 2012, Pages 1070-1077

Cochinchina momordica seed extract induces apoptosis and cell cycle arrest in human gastric cancer cells via PARP and p53 signal pathways

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS INDUCING FACTOR; CASPASE 3; CASPASE 8; CASPASE 9; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; MOMORDICA COCHINCHINENSIS SEED EXTRACT; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PLANT EXTRACT; PROTEIN BAX; PROTEIN BCL 2; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 84867757377     PISSN: 01635581     EISSN: 15327914     Source Type: Journal    
DOI: 10.1080/01635581.2012.712737     Document Type: Article
Times cited : (28)

References (32)
  • 1
    • 1542289820 scopus 로고    scopus 로고
    • Fatty acid and carotenoid composition of gac (Momordica cochinchinensis Spreng) fruit
    • Ishida, B K, Turner, C, Chapman, M H, and, McKeon, T A. 2004. Fatty acid and carotenoid composition of gac (Momordica cochinchinensis Spreng) fruit. J Agric Food Chem, 2: 274-279.
    • (2004) J Agric Food Chem , vol.2 , pp. 274-279
    • Ishida, B.K.1    Turner, C.2    Chapman, M.H.3    McKeon, T.A.4
  • 2
    • 0015009992 scopus 로고
    • Pharmacological studies on the saponin isolated from the seed of Momordica cochinchinensis Sprenger
    • Kubota, K, Sato, M, Murakami, T, and, Yamagishi, T. 1971. Pharmacological studies on the saponin isolated from the seed of Momordica cochinchinensis Sprenger. Yakugaku Zasshi, 91: 174-179.
    • (1971) Yakugaku Zasshi , vol.91 , pp. 174-179
    • Kubota, K.1    Sato, M.2    Murakami, T.3    Yamagishi, T.4
  • 3
    • 0024368497 scopus 로고
    • Purification and properties of a new ribosome-inactivating protein with RNA glycosidase activity suitable for immunotoxin preparation from the seeds of Momordica cochinchinensis (abstr)
    • Bolognesi, A, Barbieri, L, Carnicelli, D, Abbondanza, A, Cenini, P. 1989. Purification and properties of a new ribosome-inactivating protein with RNA glycosidase activity suitable for immunotoxin preparation from the seeds of Momordica cochinchinensis (abstr). Biochim Biophys Acta, 993: 287-292.
    • (1989) Biochim Biophys Acta , vol.993 , pp. 287-292
    • Bolognesi, A.1    Barbieri, L.2    Carnicelli, D.3    Abbondanza, A.4    Cenini, P.5
  • 4
    • 0004542594 scopus 로고
    • The structure of a new triterpene, momordic acids, obtained from momordica cochinchinensis sprenger
    • Murakami, T, Nagasawa, H, Itokawa, H, Tachi, Y, and, Tanaka, K. 1966. The structure of a new triterpene, momordic acids, obtained from momordica cochinchinensis sprenger. Tetrahedron Letters, 42: 5137-5140.
    • (1966) Tetrahedron Letters , vol.42 , pp. 5137-5140
    • Murakami, T.1    Nagasawa, H.2    Itokawa, H.3    Tachi, Y.4    Tanaka, K.5
  • 5
    • 77956411439 scopus 로고    scopus 로고
    • Enhancement of gastric ulcer healing and angiogenesis by Cochinchina momordica seed extract in rats
    • Jung Mook, Kang, Nayoung, Kim, Bongcheol, Kim, Joo-Hyon, Kim, Bong-Yong, Lee. 2010. Enhancement of gastric ulcer healing and angiogenesis by Cochinchina momordica seed extract in rats. J Korean Med Sci, 25: 875-881.
    • (2010) J Korean Med Sci , vol.25 , pp. 875-881
    • Jung Mook, K.1    Nayoung, K.2    Bongcheol, K.3    Joo-Hyon, K.4    Bong-Yong, L.5
  • 6
    • 75749090846 scopus 로고    scopus 로고
    • Effect of the extract made from Cochinchina momordica seeds on the humoral immune responses of mice to a commercial foot-and-mouth disease vaccine (serotypes O and Asia 1)
    • Sakwiwatkul, K, Li, R L, Song, X M, and, Hu, S H. 2010. Effect of the extract made from Cochinchina momordica seeds on the humoral immune responses of mice to a commercial foot-and-mouth disease vaccine (serotypes O and Asia 1). Microbiol Immunol, 54: 31-37.
    • (2010) Microbiol Immunol , vol.54 , pp. 31-37
    • Sakwiwatkul, K.1    Li, R.L.2    Song, X.M.3    Hu, S.H.4
  • 7
    • 70350333139 scopus 로고    scopus 로고
    • Enhancement of immune responses to Newcastle disease vaccine by a supplement of extract of Momordica cochinchinensis (Lour.) Spreng seeds
    • Xiao, C, Bao, G, and, Hu, S. 2009. Enhancement of immune responses to Newcastle disease vaccine by a supplement of extract of Momordica cochinchinensis (Lour.) Spreng seeds. Poultry Science, 88: 2293-2297.
    • (2009) Poultry Science , vol.88 , pp. 2293-2297
    • Xiao, C.1    Bao, G.2    Hu, S.3
  • 8
    • 33646546660 scopus 로고    scopus 로고
    • Potent antitumor activity of 10-methoxy-9-nitrocamptothecin
    • Luo, P, He, Q, He, X, Hu, Y, Lu, W. 2006. Potent antitumor activity of 10-methoxy-9-nitrocamptothecin. Mol Cancer Ther, 5: 962-968.
    • (2006) Mol Cancer Ther , vol.5 , pp. 962-968
    • Luo, P.1    He, Q.2    He, X.3    Hu, Y.4    Lu, W.5
  • 9
    • 33746377985 scopus 로고    scopus 로고
    • SH-7, a new synthesized shikonin derivative, exerting its potent antitumor activities as a topoisomerase inhibitor
    • Yang, F, Chen, Y, Duan, W, Zhang, C, Zhu, H. 2006. SH-7, a new synthesized shikonin derivative, exerting its potent antitumor activities as a topoisomerase inhibitor. Int J Cancer, 119: 1184-1193.
    • (2006) Int J Cancer , vol.119 , pp. 1184-1193
    • Yang, F.1    Chen, Y.2    Duan, W.3    Zhang, C.4    Zhu, H.5
  • 10
  • 11
    • 71049139405 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase inhibitors in cancer treatment: A clinical perspective
    • Sandhu, S K, Yap, T A, and, de Bono, J S. 2010. Poly (ADP-ribose) polymerase inhibitors in cancer treatment: a clinical perspective. Eur J Cancer, 46: 9-20.
    • (2010) Eur J Cancer , vol.46 , pp. 9-20
    • Sandhu, S.K.1    Yap, T.A.2    De Bono, J.S.3
  • 12
    • 33846064669 scopus 로고    scopus 로고
    • Protective effects of the PARP-1 inhibitor PJ34 in hypoxic-reoxygenated cardiomyoblasts
    • Fiorillo, C, Ponziani, V, Giannini, L, Cecchi, C, Celli, A. 2006. Protective effects of the PARP-1 inhibitor PJ34 in hypoxic-reoxygenated cardiomyoblasts. Cell Mol Life Sci, 63: 3061-3071.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 3061-3071
    • Fiorillo, C.1    Ponziani, V.2    Giannini, L.3    Cecchi, C.4    Celli, A.5
  • 13
    • 77954295382 scopus 로고    scopus 로고
    • The two faces of tumor suppressor p53-revisited
    • Smith, M L, and, Kumar, M A. 2010. The two faces of tumor suppressor p53-revisited. Mol Cell Pharmacol, 2: 117-119.
    • (2010) Mol Cell Pharmacol , vol.2 , pp. 117-119
    • Smith, M.L.1    Kumar, M.A.2
  • 14
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: A comprehensive update of caspase substrates
    • Fischer, U, Janicke, R U, and, Schulze-Osthoff, K. 2003. Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ, 10: 76-100.
    • (2003) Cell Death Differ , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 15
    • 3042853095 scopus 로고    scopus 로고
    • Echinocystic acid induces apoptosis in HL-60 cells through mitochondria-mediated death pathway
    • Tong, X, Lin, S, Fujii, M, and, Hou, D X. 2004. Echinocystic acid induces apoptosis in HL-60 cells through mitochondria-mediated death pathway. Cancer Lett, 212: 21-32.
    • (2004) Cancer Lett , vol.212 , pp. 21-32
    • Tong, X.1    Lin, S.2    Fujii, M.3    Hou, D.X.4
  • 16
    • 0242522206 scopus 로고    scopus 로고
    • Regulation of apoptosis by Bcl-2 family proteins
    • Burlacu, A. 2003. Regulation of apoptosis by Bcl-2 family proteins. J Cell Mol.Med, 7: 249-257.
    • (2003) J Cell Mol.Med , vol.7 , pp. 249-257
    • Burlacu, A.1
  • 17
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Nijhawan, L P, Budihardjo, D, Srinivasula, I, Ahmad, S M, Alnemri, M. 1997. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell, 91: 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Nijhawan, L.P.1    Budihardjo, D.2    Srinivasula, I.3    Ahmad, S.M.4    Alnemri, M.5
  • 18
    • 0031980222 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of T lymphocyte apoptosis
    • Penninger, J M, and, Kroemer, G. 1996. Molecular and cellular mechanisms of T lymphocyte apoptosis. Adv Immunol, 68: 51-144.
    • (1996) Adv Immunol , vol.68 , pp. 51-144
    • Penninger, J.M.1    Kroemer, G.2
  • 19
    • 0033106243 scopus 로고    scopus 로고
    • A tailless Fas-FADD death-effector domain chimera is sufficient to execute fas function in T Cells but not B cells of MRL-lpr/lpr mice
    • Kabra, N H, Cado, D, and, Winoto, A. 1999. A tailless Fas-FADD death-effector domain chimera is sufficient to execute fas function in T Cells but not B cells of MRL-lpr/lpr mice. J Immunol, 162: 2766-2774.
    • (1999) J Immunol , vol.162 , pp. 2766-2774
    • Kabra, N.H.1    Cado, D.2    Winoto, A.3
  • 20
    • 0035837040 scopus 로고    scopus 로고
    • Hepatitis C virus core protein enhances FADD-mediated apoptosis and suppresses TRADD signaling of tumor necrosis factor receptor
    • Zhu, N, Ware, C F, and, Lai, M M. 2001. Hepatitis C virus core protein enhances FADD-mediated apoptosis and suppresses TRADD signaling of tumor necrosis factor receptor. Virology, 283: 178-187.
    • (2001) Virology , vol.283 , pp. 178-187
    • Zhu, N.1    Ware, C.F.2    Lai, M.M.3
  • 22
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel, F C, Hellbardt, S, Behrmann, I, Germer, M, Pawlita, M. 1995. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. Embo J, 14: 5579-5588.
    • (1995) Embo J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5
  • 23
    • 44449174535 scopus 로고    scopus 로고
    • A PARP-1/JNK1 cascade participates in the synergistic apoptotic effect of TNFalpha and all-trans retinoic acid in APL cells
    • Mathieu, J, Flexor, M, Lanotte, M, and, Besancon, F. 2008. A PARP-1/JNK1 cascade participates in the synergistic apoptotic effect of TNFalpha and all-trans retinoic acid in APL cells. Oncogene, 27: 3361-3370.
    • (2008) Oncogene , vol.27 , pp. 3361-3370
    • Mathieu, J.1    Flexor, M.2    Lanotte, M.3    Besancon, F.4
  • 24
    • 36549082920 scopus 로고    scopus 로고
    • Poly(ADP-ribose) makes a date with death
    • Heeres, J T, and, Hergenrother, P J. 2007. Poly(ADP-ribose) makes a date with death. Curr Opin Chem Biol, 11: 644-653.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 644-653
    • Heeres, J.T.1    Hergenrother, P.J.2
  • 25
    • 36249022077 scopus 로고    scopus 로고
    • Nuclear translocation of p65 NF-kappaB is sufficient for VCAM-1, but not ICAM-1, expression in TNF-stimulated smooth muscle cells: Differential requirement for PARP-1 expression and interaction
    • Zerfaoui, M, Suzuki, Y, Naura, A S, Hans, C P, Nichols, C. 2008. Nuclear translocation of p65 NF-kappaB is sufficient for VCAM-1, but not ICAM-1, expression in TNF-stimulated smooth muscle cells: differential requirement for PARP-1 expression and interaction. Cell Signal, 20: 186-194.
    • (2008) Cell Signal , vol.20 , pp. 186-194
    • Zerfaoui, M.1    Suzuki, Y.2    Naura, A.S.3    Hans, C.P.4    Nichols, C.5
  • 26
    • 18344377030 scopus 로고    scopus 로고
    • The p53 pathway: Positive and negative feedback loops
    • Harris, S L, and, Levine, A J. 2005. The p53 pathway: positive and negative feedback loops. Oncogene, 24: 2899-2908.
    • (2005) Oncogene , vol.24 , pp. 2899-2908
    • Harris, S.L.1    Levine, A.J.2
  • 27
    • 0037380884 scopus 로고    scopus 로고
    • Bax plays a pivotal role in thapsigargin-induced apoptosis of human colon cancer HCT116 cells by controlling Smac/Diablo and Omi/HtrA2 release from mitochondria
    • Yamaguchi, H, Bhalla, K, and, Wang, H G. 2003. Bax plays a pivotal role in thapsigargin-induced apoptosis of human colon cancer HCT116 cells by controlling Smac/Diablo and Omi/HtrA2 release from mitochondria. Cancer Research, 63: 1483-1489.
    • (2003) Cancer Research , vol.63 , pp. 1483-1489
    • Yamaguchi, H.1    Bhalla, K.2    Wang, H.G.3
  • 28
    • 0027109075 scopus 로고
    • Guardian of the genome
    • p53
    • Lane, D P. 1992. guardian of the genome. Nature, 358 (6381): 15-16. p53
    • (1992) Nature , vol.358 , Issue.6381 , pp. 15-16
    • Lane, D.P.1
  • 29
    • 59249101220 scopus 로고    scopus 로고
    • Anti-tumor effects of telomelysin for head and neck squamous cell carcinoma
    • Fujita, K, Kimura, M, Kondo, N, Sakakbara, A, Sano, D. 2008. Anti-tumor effects of telomelysin for head and neck squamous cell carcinoma. Oncology Reports, 20: 1363-1368.
    • (2008) Oncology Reports , vol.20 , pp. 1363-1368
    • Fujita, K.1    Kimura, M.2    Kondo, N.3    Sakakbara, A.4    Sano, D.5
  • 30
    • 58849101367 scopus 로고    scopus 로고
    • Polymeric tubulysin-peptide nanoparticles with potent antitumor activity
    • Schluep, T, Gunawan, P, Ma, L, Jensen, G S, Duringer, J. 2009. Polymeric tubulysin-peptide nanoparticles with potent antitumor activity. Clin Cancer Res, 15: 181-189.
    • (2009) Clin Cancer Res , vol.15 , pp. 181-189
    • Schluep, T.1    Gunawan, P.2    Ma, L.3    Jensen, G.S.4    Duringer, J.5
  • 31
    • 1542344934 scopus 로고    scopus 로고
    • Bax-induced cytochrome c release from mitochondria depend sonalpha-helices-5 and-6
    • Heimlich, G, McKinnon, A D, Bernardo, K, Brdiczka, D, Reed, J C. 2004. Bax-induced cytochrome c release from mitochondria depend sonalpha-helices-5 and-6. Biochem J, 378: 247-255.
    • (2004) Biochem J , vol.378 , pp. 247-255
    • Heimlich, G.1    McKinnon, A.D.2    Bernardo, K.3    Brdiczka, D.4    Reed, J.C.5
  • 32
    • 0036479115 scopus 로고    scopus 로고
    • Transcriptional repression of the anti-apoptotic survivin gene by wild type p53
    • Hoffman, W H, Biade, S, Zilfou, J T, Chen, J, and, Murphy, M. 2002. Transcriptional repression of the anti-apoptotic survivin gene by wild type p53. J Biol Chem, 277: 3247-3257.
    • (2002) J Biol Chem , vol.277 , pp. 3247-3257
    • Hoffman, W.H.1    Biade, S.2    Zilfou, J.T.3    Chen, J.4    Murphy, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.