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Volumn 1171, Issue , 2009, Pages 501-508

Ginkgolide B induces apoptosis via activation of JNK and p21-activated protein kinase 2 in mouse embryonic stem cells

Author keywords

Apoptosis; Ginkgolide B; JNK; PAK2

Indexed keywords

ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; ANTISENSE OLIGONUCLEOTIDE; CASPASE 3; CASPASE 3 INHIBITOR; GINKGOLIDE B; P21 ACTIVATED KINASE 2; STRESS ACTIVATED PROTEIN KINASE;

EID: 69149098568     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2009.04691.x     Document Type: Conference Paper
Times cited : (8)

References (34)
  • 1
    • 0041825261 scopus 로고    scopus 로고
    • Pharmacological studies supporting the therapeutic use of Ginkgo biloba extract for Alzheimer's disease
    • Ahlemeyer, B. J. Krieglstein. 2003. Pharmacological studies supporting the therapeutic use of Ginkgo biloba extract for Alzheimer's disease. Pharmacopsychiatry 36 (Suppl 1 S8 14.
    • (2003) Pharmacopsychiatry , vol.36 , Issue.SUPPL. 1
    • Ahlemeyer, B.1    Krieglstein, J.2
  • 2
    • 0042169046 scopus 로고    scopus 로고
    • Ginkgo biloba extracts and cancer: A research area in its infancy
    • DeFeudis, F.V., V. Papadopoulos K. Drieu. 2003. Ginkgo biloba extracts and cancer: a research area in its infancy. Fundam. Clin. Pharmacol. 17 : 405 417.
    • (2003) Fundam. Clin. Pharmacol. , vol.17 , pp. 405-417
    • Defeudis, F.V.1    Papadopoulos, V.2    Drieu, K.3
  • 3
    • 4344600436 scopus 로고    scopus 로고
    • Ginkgolide B inhibits the neurotoxicity of prions or amyloid-beta1-42
    • Bate, C., M. Salmona A. Williams. 2004. Ginkgolide B inhibits the neurotoxicity of prions or amyloid-beta1-42. J. Neuroinflammation 1 : 4.
    • (2004) J. Neuroinflammation , vol.1 , pp. 4
    • Bate, C.1    Salmona, M.2    Williams, A.3
  • 4
    • 0037126035 scopus 로고    scopus 로고
    • Inhibition of amyloid-beta aggregation and caspase-3 activation by the Ginkgo biloba extract EGb761
    • Luo, Y. et al. 2002. Inhibition of amyloid-beta aggregation and caspase-3 activation by the Ginkgo biloba extract EGb761. Proc. Natl. Acad. Sci. USA 99 : 12197 12202.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12197-12202
    • Luo, Y.1
  • 5
    • 15244358528 scopus 로고    scopus 로고
    • Ginkgo biloba extract (EGb 761) induces apoptosis by the activation of caspase-3 in oral cavity cancer cells
    • Kim, K.S. et al. 2005. Ginkgo biloba extract (EGb 761) induces apoptosis by the activation of caspase-3 in oral cavity cancer cells. Oral Oncol. 41 : 383 389.
    • (2005) Oral Oncol. , vol.41 , pp. 383-389
    • Kim, K.S.1
  • 6
    • 27744566105 scopus 로고    scopus 로고
    • Ginkgolides induce apoptosis and decrease cell numbers in mouse blastocysts
    • Chan, W.H. 2005. Ginkgolides induce apoptosis and decrease cell numbers in mouse blastocysts. Biochem. Biophys. Res. Commun. 338 : 1263 1267.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1263-1267
    • Chan, W.H.1
  • 7
    • 33750002736 scopus 로고    scopus 로고
    • Ginkgolide B induces apoptosis and developmental injury in mouse embryonic stem cells and blastocysts
    • Chan, W.H. 2006. Ginkgolide B induces apoptosis and developmental injury in mouse embryonic stem cells and blastocysts. Hum. Reprod. 21 : 2985 2995.
    • (2006) Hum. Reprod. , vol.21 , pp. 2985-2995
    • Chan, W.H.1
  • 8
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J.F., A.H. Wyllie A.R. Currie. 1972. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26 : 239 257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 9
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie, A.H. 1980. Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284 : 555 556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 10
    • 0030759279 scopus 로고    scopus 로고
    • Kinase cascades regulating entry into apoptosis
    • Anderson, P. 1997. Kinase cascades regulating entry into apoptosis. Microbiol. Mol. Biol. Rev. 61 : 33 46.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 33-46
    • Anderson, P.1
  • 11
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia, Z. et al. 1995. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270 : 1326 1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1
  • 12
    • 0347537940 scopus 로고    scopus 로고
    • Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis
    • Verheij, M. et al. 1996. Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis. Nature 380 : 75 79.
    • (1996) Nature , vol.380 , pp. 75-79
    • Verheij, M.1
  • 13
    • 0030614914 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase-mediated activation of interleukin-1beta converting enzyme/CED-3-like protease during anticancer drug-induced apoptosis
    • Seimiya, H. et al. 1997. c-Jun NH2-terminal kinase-mediated activation of interleukin-1beta converting enzyme/CED-3-like protease during anticancer drug-induced apoptosis. J. Biol. Chem. 272 : 4631 4636.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4631-4636
    • Seimiya, H.1
  • 14
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel, T. G.M. Bokoch. 1997. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276 : 1571 1574.
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 15
    • 0031443641 scopus 로고    scopus 로고
    • Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis
    • Lee, N. et al. 1997. Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis. Proc. Natl. Acad. Sci. USA 94 : 13642 13647.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13642-13647
    • Lee, N.1
  • 16
    • 0032531273 scopus 로고    scopus 로고
    • Proteolytic cleavage and activation of PAK2 during UV irradiation-induced apoptosis in A431 cells
    • Tang, T.K. et al. 1998. Proteolytic cleavage and activation of PAK2 during UV irradiation-induced apoptosis in A431 cells. J. Cell Biochem. 70 : 442 454.
    • (1998) J. Cell Biochem. , vol.70 , pp. 442-454
    • Tang, T.K.1
  • 17
    • 0032931817 scopus 로고    scopus 로고
    • PAK2 is cleaved and activated during hyperosmotic shock-induced apoptosis via a caspase-dependent mechanism: Evidence for the involvement of oxidative stress
    • Chan, W.H., J.S. Yu S.D. Yang. 1999. PAK2 is cleaved and activated during hyperosmotic shock-induced apoptosis via a caspase-dependent mechanism: evidence for the involvement of oxidative stress. J. Cell Physiol. 178 : 397 408.
    • (1999) J. Cell Physiol. , vol.178 , pp. 397-408
    • Chan, W.H.1    Yu, J.S.2    Yang, S.D.3
  • 18
    • 0034306285 scopus 로고    scopus 로고
    • Apoptotic signalling cascade in photosensitized human epidermal carcinoma A431 cells: Involvement of singlet oxygen, c-Jun N-terminal kinase, caspase-3 and p21-activated kinase 2
    • Chan, W.H., J.S. Yu S.D. Yang. 2000. Apoptotic signalling cascade in photosensitized human epidermal carcinoma A431 cells: involvement of singlet oxygen, c-Jun N-terminal kinase, caspase-3 and p21-activated kinase 2. Biochem. J. 351 : 221 232.
    • (2000) Biochem. J. , vol.351 , pp. 221-232
    • Chan, W.H.1    Yu, J.S.2    Yang, S.D.3
  • 19
    • 33847078455 scopus 로고    scopus 로고
    • Apoptotic signaling in methylglyoxal-treated human osteoblasts involves oxidative stress, c-Jun N-terminal kinase, caspase-3, and p21-activated kinase 2
    • Chan, W.H., H.J. Wu N.H. Shiao. 2007. Apoptotic signaling in methylglyoxal-treated human osteoblasts involves oxidative stress, c-Jun N-terminal kinase, caspase-3, and p21-activated kinase 2. J. Cell Biochem. 100 : 1056 1069.
    • (2007) J. Cell Biochem. , vol.100 , pp. 1056-1069
    • Chan, W.H.1    Wu, H.J.2    Shiao, N.H.3
  • 20
    • 34249782842 scopus 로고    scopus 로고
    • Citrinin induces apoptosis via a mitochondria-dependent pathway and inhibition of survival signals in embryonic stem cells, and causes developmental injury in blastocysts
    • Chan, W.H. 2007. Citrinin induces apoptosis via a mitochondria-dependent pathway and inhibition of survival signals in embryonic stem cells, and causes developmental injury in blastocysts. Biochem. J. 404 : 317 326.
    • (2007) Biochem. J. , vol.404 , pp. 317-326
    • Chan, W.H.1
  • 21
    • 0141529729 scopus 로고    scopus 로고
    • Curcumin inhibits UV irradiation-induced oxidative stress and apoptotic biochemical changes in human epidermoid carcinoma A431 cells
    • Chan, W.H., C.C. Wu J.S. Yu. 2003. Curcumin inhibits UV irradiation-induced oxidative stress and apoptotic biochemical changes in human epidermoid carcinoma A431 cells. J. Cell. Biochem. 90 : 327 338.
    • (2003) J. Cell. Biochem. , vol.90 , pp. 327-338
    • Chan, W.H.1    Wu, C.C.2    Yu, J.S.3
  • 22
    • 0037362431 scopus 로고    scopus 로고
    • Subcellular localization of Photofrin determines the death phenotype of human epidermoid carcinoma A431 cells triggered by photodynamic therapy: When plasma membranes are the main targets
    • Hsieh, Y.J. et al. 2003. Subcellular localization of Photofrin determines the death phenotype of human epidermoid carcinoma A431 cells triggered by photodynamic therapy: when plasma membranes are the main targets. J. Cell Physiol. 194 : 363 375.
    • (2003) J. Cell Physiol. , vol.194 , pp. 363-375
    • Hsieh, Y.J.1
  • 23
    • 15044365453 scopus 로고    scopus 로고
    • Anti-apoptotic effects of curcumin on photosensitized human epidermal carcinoma A431 cells
    • Chan, W.H. H.J. Wu. 2004. Anti-apoptotic effects of curcumin on photosensitized human epidermal carcinoma A431 cells. J. Cell Biochem. 92 : 200 212.
    • (2004) J. Cell Biochem. , vol.92 , pp. 200-212
    • Chan, W.H.1    Wu, H.J.2
  • 24
    • 21344462243 scopus 로고    scopus 로고
    • Curcumin prevents methylglyoxal-induced oxidative stress and apoptosis in mouse embryonic stem cells and blastocysts
    • Hsuuw, Y.D. et al. 2005. Curcumin prevents methylglyoxal-induced oxidative stress and apoptosis in mouse embryonic stem cells and blastocysts. J. Cell. Physiol. 205 : 379 386.
    • (2005) J. Cell. Physiol. , vol.205 , pp. 379-386
    • Hsuuw, Y.D.1
  • 25
    • 0029670910 scopus 로고    scopus 로고
    • CPP32/apopain is a key interleukin 1 beta converting enzyme-like protease involved in Fas-mediated apoptosis
    • Schlegel, J. et al. 1996. CPP32/apopain is a key interleukin 1 beta converting enzyme-like protease involved in Fas-mediated apoptosis. J. Biol. Chem. 271 : 1841 1844.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1841-1844
    • Schlegel, J.1
  • 26
    • 0029894283 scopus 로고    scopus 로고
    • Activation of the CPP32 apoptotic protease by distinct signaling pathways with differential sensitivity to Bcl-xL
    • Erhardt, P. G.M. Cooper. 1996. Activation of the CPP32 apoptotic protease by distinct signaling pathways with differential sensitivity to Bcl-xL. J. Biol. Chem. 271 : 17601 17604.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17601-17604
    • Erhardt, P.1    Cooper, G.M.2
  • 27
    • 0035923665 scopus 로고    scopus 로고
    • SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase
    • Bennett, B.L. et al. 2001. SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase. Proc. Natl. Acad. Sci. USA 98 : 13681 13686.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13681-13686
    • Bennett, B.L.1
  • 28
    • 0029829898 scopus 로고    scopus 로고
    • Cleavage arrest of early frog embryos by the G protein-activated protein kinase PAK I
    • Rooney, R.D. et al. 1996. Cleavage arrest of early frog embryos by the G protein-activated protein kinase PAK I. J. Biol. Chem. 271 : 21498 21504.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21498-21504
    • Rooney, R.D.1
  • 29
    • 0030880187 scopus 로고    scopus 로고
    • A member of the Ste20/PAK family of protein kinases is involved in both arrest of Xenopus oocytes at G2/prophase of the first meiotic cell cycle and in prevention of apoptosis
    • Faure, S. et al. 1997. A member of the Ste20/PAK family of protein kinases is involved in both arrest of Xenopus oocytes at G2/prophase of the first meiotic cell cycle and in prevention of apoptosis. EMBO J. 16 : 5550 5561.
    • (1997) EMBO J. , vol.16 , pp. 5550-5561
    • Faure, S.1
  • 30
    • 0033524507 scopus 로고    scopus 로고
    • Control of G2/M transition in Xenopus by a member of the p21-activated kinase (PAK) family: A link between protein kinase a and PAK signaling pathways?
    • Faure, S. et al. 1999. Control of G2/M transition in Xenopus by a member of the p21-activated kinase (PAK) family: a link between protein kinase A and PAK signaling pathways? J. Biol. Chem. 274 : 3573 3579.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3573-3579
    • Faure, S.1
  • 31
    • 0034723369 scopus 로고    scopus 로고
    • Regulation of Xenopus p21-activated kinase (X-PAK2) by Cdc42 and maturation-promoting factor controls Xenopus oocyte maturation
    • Cau, J. et al. 2000. Regulation of Xenopus p21-activated kinase (X-PAK2) by Cdc42 and maturation-promoting factor controls Xenopus oocyte maturation. J. Biol. Chem. 275 : 2367 2375.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2367-2375
    • Cau, J.1
  • 32
    • 24944467331 scopus 로고    scopus 로고
    • Anti-phosphopeptide antibody, P-STM as a novel tool for detecting mitotic phosphoproteins: Identification of lamins a and C as two major targets
    • Tsai, I.C. et al. 2005. Anti-phosphopeptide antibody, P-STM as a novel tool for detecting mitotic phosphoproteins: identification of lamins A and C as two major targets. J. Cell Biochem. 94 : 967 981.
    • (2005) J. Cell Biochem. , vol.94 , pp. 967-981
    • Tsai, I.C.1
  • 33
    • 0031830188 scopus 로고    scopus 로고
    • Heat shock stress induces cleavage and activation of PAK2 in apoptotic cells
    • Chan, W.H., J.S. Yu S.D. Yang. 1998. Heat shock stress induces cleavage and activation of PAK2 in apoptotic cells. J. Protein Chem. 17 : 485 494.
    • (1998) J. Protein Chem. , vol.17 , pp. 485-494
    • Chan, W.H.1    Yu, J.S.2    Yang, S.D.3
  • 34
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso, O.A. et al. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81 : 1137 1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1


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