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Volumn 43, Issue 1, 2004, Pages 53-59

Catalpol inhibits apoptosis in hydrogen peroxide-induced PC12 cells by preventing cytochrome c release and inactivating of caspase cascade

Author keywords

Apoptosis; Caspase; Catalpol; Cytochrome c; Hydrogen peroxide; PC12 cells

Indexed keywords

CASPASE 3; CATALPOL; CYTOCHROME C; HYDROGEN PEROXIDE; INTERLEUKIN 1BETA CONVERTING ENZYME; PROTEIN BAX; PROTEIN BCL 2;

EID: 1242337383     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2003.10.017     Document Type: Article
Times cited : (97)

References (26)
  • 1
    • 0036179645 scopus 로고    scopus 로고
    • Death receptors couple to both cell proliferation and apoptosis
    • Budd R.C. Death receptors couple to both cell proliferation and apoptosis. J. Clin. Invest. 109:2002;437-441.
    • (2002) J. Clin. Invest. , vol.109 , pp. 437-441
    • Budd, R.C.1
  • 3
    • 0033805296 scopus 로고    scopus 로고
    • Triggering and modulation of apoptosis by oxidative stress
    • Chandra J., Samali A., Orrenius S. Triggering and modulation of apoptosis by oxidative stress. Free Radic. Biol. Med. 29:2000;323-333.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 323-333
    • Chandra, J.1    Samali, A.2    Orrenius, S.3
  • 4
    • 0033162401 scopus 로고    scopus 로고
    • Involvement of p53 and HSP70 proteins in attenuation of UVC-induced apoptosis by thermal stress in hepatocellular carcinoma cells
    • Chen Y.C., Lin-Shiau S.Y., Lin J.K. Involvement of p53 and HSP70 proteins in attenuation of UVC-induced apoptosis by thermal stress in hepatocellular carcinoma cells. Photochem. Photobiol. 70:1996;78-86.
    • (1996) Photochem. Photobiol. , vol.70 , pp. 78-86
    • Chen, Y.C.1    Lin-Shiau, S.Y.2    Lin, J.K.3
  • 5
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen G.M. Caspases: the executioners of apoptosis. J. Biochem. 326:1997;1-16.
    • (1997) J. Biochem. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 6
    • 0033179760 scopus 로고    scopus 로고
    • Bcl-2 family members and the mitochondria in apoptosis
    • Gross A., McDonnell J.M., Korsmeyer S.J. Bcl-2 family members and the mitochondria in apoptosis. Genes Dev. 13:1999;1899-1911.
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 7
    • 0028792111 scopus 로고
    • Lipid peroxidation and antioxidants as biomarkers of tissue damage
    • Gutteridege J.M.C. Lipid peroxidation and antioxidants as biomarkers of tissue damage. Clin. Chem. 41:1995;1819-1828.
    • (1995) Clin. Chem. , vol.41 , pp. 1819-1828
    • Gutteridege, J.M.C.1
  • 8
    • 0030797727 scopus 로고    scopus 로고
    • Bax deletion further orders the cell death pathway in cerebellar granule cells and suggests a caspase-independent pathway to cell death
    • Knudson C.M., Creedon D.J., Deshmukh M., Korsmeyer S.J., Johnson E.M. Jr. Bax deletion further orders the cell death pathway in cerebellar granule cells and suggests a caspase-independent pathway to cell death. J. Cell Biol. 139:1997;205-217.
    • (1997) J. Cell Biol. , vol.139 , pp. 205-217
    • Knudson, C.M.1    Creedon, D.J.2    Deshmukh, M.3    Korsmeyer, S.J.4    Johnson Jr., E.M.5
  • 9
    • 0030986669 scopus 로고    scopus 로고
    • Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis
    • Kruman I., Bruce-Keller A., Bredesen D., Waeg G., Mattson M. Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis. J. Neurosci. 17:1997;5089-5100.
    • (1997) J. Neurosci. , vol.17 , pp. 5089-5100
    • Kruman, I.1    Bruce-Keller, A.2    Bredesen, D.3    Waeg, G.4    Mattson, M.5
  • 10
    • 0032746896 scopus 로고    scopus 로고
    • Roles of P53, c-Myc, Bcl-2, Bax and caspase in glutamate-induced neuronal apoptosis and the possible neuroprotective mechanism of basic fibroblast growth factor
    • Liu X., Zhu X.Z. Roles of P53, c-Myc, Bcl-2, Bax and caspase in glutamate-induced neuronal apoptosis and the possible neuroprotective mechanism of basic fibroblast growth factor. Mol. Brain Res. 70:1999;201-206.
    • (1999) Mol. Brain Res. , vol.70 , pp. 201-206
    • Liu, X.1    Zhu, X.Z.2
  • 12
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survivals: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survivals: application to proliferation and cytotoxicity assays. J. Immunol. Meth. 65:1983;55-63.
    • (1983) J. Immunol. Meth. , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 13
    • 0031775603 scopus 로고    scopus 로고
    • Caspases medicate 6-hydroxydopamone-induced apoptosis but not necrosis in PC12 cells
    • Ochu E.E., Rothwell N.J., Walterls C.M. Caspases medicate 6-hydroxydopamone-induced apoptosis but not necrosis in PC12 cells. J. Neurochem. 70:1998;2637-2640.
    • (1998) J. Neurochem. , vol.70 , pp. 2637-2640
    • Ochu, E.E.1    Rothwell, N.J.2    Walterls, C.M.3
  • 14
    • 0035426195 scopus 로고    scopus 로고
    • Ca (2+)-calmodulin antagonist chlorpromazine and poly(ADP-ribose) polymerase modulators 4-aminobenzamide and nicotinamide influence hepatic expression of BCL-XL and P53 and protect against acetaminophen-induced programmed and unprogrammed cell death in mice
    • Ray S.D., Balasubramanian G., Bagchi D., Reddy C.S. Ca (2+)-calmodulin antagonist chlorpromazine and poly(ADP-ribose) polymerase modulators 4-aminobenzamide and nicotinamide influence hepatic expression of BCL-XL and P53 and protect against acetaminophen-induced programmed and unprogrammed cell death in mice. Free Radic. Biol. Med. 31:2001;277-291.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 277-291
    • Ray, S.D.1    Balasubramanian, G.2    Bagchi, D.3    Reddy, C.S.4
  • 15
    • 0029131043 scopus 로고
    • The activation and translation of extracellular signal-regulated kinases (ERK-1 and ERK-2) appear not to be required for elongation of neurites in PC12D cells
    • Sano M., Kohno M., Iwanaga M. The activation and translation of extracellular signal-regulated kinases (ERK-1 and ERK-2) appear not to be required for elongation of neurites in PC12D cells. Brain Res. 688:1995;213-218.
    • (1995) Brain Res. , vol.688 , pp. 213-218
    • Sano, M.1    Kohno, M.2    Iwanaga, M.3
  • 16
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Solange D., Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10:2000;369-377.
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Solange, D.1    Martinou, J.C.2
  • 18
    • 0037192790 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein
    • Sun X.M., Bratton S.B., Butterworth M., MacFarlane M., Cohen G.M. Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein. J. Biol. Chem. 277:2002;11345-11351.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11345-11351
    • Sun, X.M.1    Bratton, S.B.2    Butterworth, M.3    MacFarlane, M.4    Cohen, G.M.5
  • 19
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic reticulum specific apoptosis and cytotoxicity by amyloid-β
    • Toshiyuki N., Hong Z., Nobuhiro M., En L., Jin X., Bruce A.Y., Junying Y. Caspase-12 mediates endoplasmic reticulum specific apoptosis and cytotoxicity by amyloid-β Nature. 403:2000;98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Toshiyuki, N.1    Hong, Z.2    Nobuhiro, M.3    En, L.4    Jin, X.5    Bruce, A.Y.6    Junying, Y.7
  • 20
    • 0022546957 scopus 로고
    • Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma
    • Tsujimoto Y., Croce C.M. Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc. Natl Acad. Sci. USA. 83:1986;5214-5218.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 22
    • 0028913385 scopus 로고
    • Comparison of three in vitro cytotoxicity assays for estimating surfactant ocular irritation
    • Vian L., Vincent J., Maurin J., Fabre I., Giroux J., Cano J.P. Comparison of three in vitro cytotoxicity assays for estimating surfactant ocular irritation. Toxicol. in vitro. 9:1995;185-190.
    • (1995) Toxicol. in Vitro , vol.9 , pp. 185-190
    • Vian, L.1    Vincent, J.2    Maurin, J.3    Fabre, I.4    Giroux, J.5    Cano, J.P.6
  • 24
    • 0032736984 scopus 로고    scopus 로고
    • Ischemic preconditioning protects the mouse liver by inhibition of apoptosis through a caspase-dependents pathway
    • Yaday S.S., Sindram D., Perry D.K., Clavien P.A. Ischemic preconditioning protects the mouse liver by inhibition of apoptosis through a caspase-dependents pathway. Hepatology. 30:1999;1223-1231.
    • (1999) Hepatology , vol.30 , pp. 1223-1231
    • Yaday, S.S.1    Sindram, D.2    Perry, D.K.3    Clavien, P.A.4
  • 25
    • 0030014491 scopus 로고    scopus 로고
    • Neuritogenic effect of natural iridoid compounds on PC12h cells and its possible relation to signaling protein kinases
    • Yamazaki M., Chiba K., Mohri T. Neuritogenic effect of natural iridoid compounds on PC12h cells and its possible relation to signaling protein kinases. Biol. Pharm. Bull. 19:1996;791-795.
    • (1996) Biol. Pharm. Bull. , vol.19 , pp. 791-795
    • Yamazaki, M.1    Chiba, K.2    Mohri, T.3
  • 26
    • 0032007312 scopus 로고    scopus 로고
    • Chemopreventive isothiocyanates induce apoptosis and caspase-3-like protease activity
    • Yu R., Mandlekar S., Harvey K.J., Ucker D.S., Kong T.A.N. Chemopreventive isothiocyanates induce apoptosis and caspase-3-like protease activity. Cancer Res. 58:2000;402-408.
    • (2000) Cancer Res. , vol.58 , pp. 402-408
    • Yu, R.1    Mandlekar, S.2    Harvey, K.J.3    Ucker, D.S.4    Kong, T.A.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.