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Volumn 36, Issue 4, 2004, Pages 429-444

HSP25 overexpression attenuates oxidative stress-induced apoptosis: Roles of ERK1/2 signaling and manganese superoxide dismutase

Author keywords

Free radicals; HSP25; MnSOD; Oxidative stress; PKC; Resistance to apoptosis; Tyrosine kinase phosphorylation

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ANTISENSE OLIGODEOXYNUCLEOTIDE; DNA FRAGMENT; HEAT SHOCK PROTEIN 25; HYDROGEN PEROXIDE; JANUS KINASE; MANGANESE SUPEROXIDE DISMUTASE; MITOGEN ACTIVATED PROTEIN KINASE 1; PLATELET DERIVED GROWTH FACTOR BETA RECEPTOR; PROTEIN KINASE C DELTA; PROTEIN SH2;

EID: 1242306195     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2003.11.009     Document Type: Article
Times cited : (37)

References (50)
  • 1
    • 0031961844 scopus 로고    scopus 로고
    • Overexpression of HSP25 reduces the level of TNF-α-induced oxidative DNA damage biomarker, 8-hydroxy-2′-deoxyguanosine in L929 cells
    • Park Y.M., Han M.Y., Blackburn R.V., Lee Y.S. Overexpression of HSP25 reduces the level of TNF-α-induced oxidative DNA damage biomarker, 8-hydroxy-2′-deoxyguanosine in L929 cells. J. Cell. Physiol. 174:1997;27-34.
    • (1997) J. Cell. Physiol. , vol.174 , pp. 27-34
    • Park, Y.M.1    Han, M.Y.2    Blackburn, R.V.3    Lee, Y.S.4
  • 2
    • 0027293201 scopus 로고
    • Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wild type or deletion mutants of the Drosophila 27-kD heat shock protein
    • Mehlen P., Briolay J., Smith L., Diaz-Latoud C., Fabre N., Pauli D., Arrigo A.P. Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wild type or deletion mutants of the Drosophila 27-kD heat shock protein. Eur. J. Biochem. 215:1995;277-284.
    • (1995) Eur. J. Biochem. , vol.215 , pp. 277-284
    • Mehlen, P.1    Briolay, J.2    Smith, L.3    Diaz-Latoud, C.4    Fabre, N.5    Pauli, D.6    Arrigo, A.P.7
  • 3
    • 0034054731 scopus 로고    scopus 로고
    • Role of small heat shock protein HSP25 in radioresistance and glutathione-redox cycle
    • Baek S.H., Min J.N., Park E.M., Han M.Y., Lee Y.S., Lee Y., Park Y.M. Role of small heat shock protein HSP25 in radioresistance and glutathione-redox cycle. J. Cell. Physiol. 183:2000;100-107.
    • (2000) J. Cell. Physiol. , vol.183 , pp. 100-107
    • Baek, S.H.1    Min, J.N.2    Park, E.M.3    Han, M.Y.4    Lee, Y.S.5    Lee, Y.6    Park, Y.M.7
  • 4
    • 0029823749 scopus 로고    scopus 로고
    • Modification of growth and tumorigenicity in epidermal cell lines by DNA-mediated gene transfer of M(r) 27,000 heat shock protein (hsp27)
    • Kindas-Mugge I., Herbacek I., Jantschitsch C., Micksche M., Trautinger F. Modification of growth and tumorigenicity in epidermal cell lines by DNA-mediated gene transfer of M(r) 27,000 heat shock protein (hsp27). Cell Growth Differ. 7:1996;1167-1174.
    • (1996) Cell Growth Differ. , vol.7 , pp. 1167-1174
    • Kindas-Mugge, I.1    Herbacek, I.2    Jantschitsch, C.3    Micksche, M.4    Trautinger, F.5
  • 5
    • 0033818673 scopus 로고    scopus 로고
    • HSP25-induced radioresistance is associated with reduction of apoptotic death: Involvement of Bcl-2 or cell cycle
    • Park S.H., Cho H.N., Lee S.J., Kim T.H., Park Y.M., Lee Y.J., Cho C.K., Yoo S.Y., Lee Y.S. HSP25-induced radioresistance is associated with reduction of apoptotic death: involvement of Bcl-2 or cell cycle. Radiat. Res. 154:2000;421-428.
    • (2000) Radiat. Res. , vol.154 , pp. 421-428
    • Park, S.H.1    Cho, H.N.2    Lee, S.J.3    Kim, T.H.4    Park, Y.M.5    Lee, Y.J.6    Cho, C.K.7    Yoo, S.Y.8    Lee, Y.S.9
  • 6
    • 0036312641 scopus 로고    scopus 로고
    • Downregulation of ERK2 is essential for the inhibition of radiation-induced cell death in HSP25-overepxressed L929 cells
    • Cho H.N., Lee Y.J., Cho C.K., Lee S.J., Lee Y.S. Downregulation of ERK2 is essential for the inhibition of radiation-induced cell death in HSP25-overepxressed L929 cells. Cell Death Differ. 9:2003;448-456.
    • (2003) Cell Death Differ. , vol.9 , pp. 448-456
    • Cho, H.N.1    Lee, Y.J.2    Cho, C.K.3    Lee, S.J.4    Lee, Y.S.5
  • 7
    • 0027049804 scopus 로고
    • The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases
    • Devary Y., Gottlieb R.A., Smeal T., Karin M. The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases. Cell. 71:1992;1081-1091.
    • (1992) Cell , vol.71 , pp. 1081-1091
    • Devary, Y.1    Gottlieb, R.A.2    Smeal, T.3    Karin, M.4
  • 8
    • 0029039139 scopus 로고
    • - in vascular smooth muscle cells
    • - in vascular smooth muscle cells. Circ. Res. 77:1995;29-36.
    • (1995) Circ. Res. , vol.77 , pp. 29-36
    • Baas, A.S.1    Berk, B.C.2
  • 10
    • 0030886770 scopus 로고    scopus 로고
    • Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats
    • Aikawa R., Komuro I., Yamazaki T., Zou Y., Kudoh S., Tanaka M., Shiojima I., Hiroi Y., Yazaki Y. Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats. J. Clin. Invest. 100:1997;1813-1821.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1813-1821
    • Aikawa, R.1    Komuro, I.2    Yamazaki, T.3    Zou, Y.4    Kudoh, S.5    Tanaka, M.6    Shiojima, I.7    Hiroi, Y.8    Yazaki, Y.9
  • 12
    • 0028358806 scopus 로고
    • Diversity in function and regulation of MAP kinase pathways
    • Blumer K.J., Johnson G.L. Diversity in function and regulation of MAP kinase pathways. Trends Biochem. Sci. 19:1994;236-240.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 236-240
    • Blumer, K.J.1    Johnson, G.L.2
  • 13
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger R., Krebs E.G. The MAPK signaling cascade. FASEB J. 9:1995;726-735.
    • (1995) FASEB J. , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 14
    • 0029789967 scopus 로고    scopus 로고
    • Protein kinase C activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf
    • Ueda Y., Hirai S., Osada S., Suzuki A., Mizuno K., Ohno S. Protein kinase C activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf. J. Biol. Chem. 271:1996;23512-23519.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23512-23519
    • Ueda, Y.1    Hirai, S.2    Osada, S.3    Suzuki, A.4    Mizuno, K.5    Ohno, S.6
  • 15
    • 0141611211 scopus 로고
    • Evidence that pp42, a major tyrosine kinase target protein, is a mitogen-activated serine/threonine protein kinase
    • Rossomando A.J., Payne D.M., Weber M.J., Sturgill T.W. Evidence that pp42, a major tyrosine kinase target protein, is a mitogen-activated serine/threonine protein kinase. Proc. Natl. Acad. Sci. USA. 86:1989;6940-6943.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6940-6943
    • Rossomando, A.J.1    Payne, D.M.2    Weber, M.J.3    Sturgill, T.W.4
  • 16
    • 0032498995 scopus 로고    scopus 로고
    • Signal transduction. Taking the Rap
    • Marshall C.J. Signal transduction. Taking the Rap. Nature. 392:1998;553-554.
    • (1998) Nature , vol.392 , pp. 553-554
    • Marshall, C.J.1
  • 17
    • 0032861127 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase signalling in neurons
    • Grewal S.S., York R.D., Stork P.J. Extracellular signal-regulated kinase signalling in neurons. Curr. Opin. Neurobiol. 9:1999;544-553.
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 544-553
    • Grewal, S.S.1    York, R.D.2    Stork, P.J.3
  • 18
    • 0031028381 scopus 로고    scopus 로고
    • Cell cycle arrest mediated by the MEK/mitogen-activated protein kinase pathway
    • Pumiglia K.M., Decker S.J. Cell cycle arrest mediated by the MEK/mitogen-activated protein kinase pathway. Proc. Natl. Acad. Sci. USA. 94:1997;448-452.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 448-452
    • Pumiglia, K.M.1    Decker, S.J.2
  • 20
    • 0032574692 scopus 로고    scopus 로고
    • Macrophages resistant to endogenously generated nitric oxide-mediated apoptosis are hypersensitive to exogenously added nitric oxide donors: Dichotomous apoptotic response independent of caspase 3 inhibitor PD098059
    • Mohr S., McCormick T.S., Lapetina E.G. Macrophages resistant to endogenously generated nitric oxide-mediated apoptosis are hypersensitive to exogenously added nitric oxide donors: dichotomous apoptotic response independent of caspase 3 inhibitor PD098059. Proc. Natl. Acad. Sci. USA. 95:1998;5045-5050.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5045-5050
    • Mohr, S.1    McCormick, T.S.2    Lapetina, E.G.3
  • 21
    • 0032578510 scopus 로고    scopus 로고
    • Inhibition of the p44/42 MAP kinase pathway protects hippocampal neurons in a cell-culture model of seizure activity
    • Murray B., Alessandrini A., Cole A.J., Yee A.G., Furshpan E.J. Inhibition of the p44/42 MAP kinase pathway protects hippocampal neurons in a cell-culture model of seizure activity. Proc. Natl. Acad Sci USA. 95:1998;11975-11980.
    • (1998) Proc. Natl. Acad Sci USA , vol.95 , pp. 11975-11980
    • Murray, B.1    Alessandrini, A.2    Cole, A.J.3    Yee, A.G.4    Furshpan, E.J.5
  • 22
    • 0035136052 scopus 로고    scopus 로고
    • Hydrogen peroxide induces apoptosis of chondrocytes: Involvement of calcium ion and extracellular signal-regulated protein kinase
    • Asada S., Fukuda K., Nishisaka F., Matusukawa M., Hamanisi C. Hydrogen peroxide induces apoptosis of chondrocytes: involvement of calcium ion and extracellular signal-regulated protein kinase. Inflamm. Res. 50:2001;19-23.
    • (2001) Inflamm. Res. , vol.50 , pp. 19-23
    • Asada, S.1    Fukuda, K.2    Nishisaka, F.3    Matusukawa, M.4    Hamanisi, C.5
  • 23
    • 0034671751 scopus 로고    scopus 로고
    • Requirement for ERK activation in cisplatin-induced apoptosis
    • Wang X., Martindale J.L., Holbrook N.J. Requirement for ERK activation in cisplatin-induced apoptosis. J. Biol. Chem. 275:2000;39435-39443.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39435-39443
    • Wang, X.1    Martindale, J.L.2    Holbrook, N.J.3
  • 25
    • 1242278248 scopus 로고    scopus 로고
    • The trail to superoxide dismutase
    • Fridovich I. The trail to superoxide dismutase. Protein Sci. 64:1998;97-112.
    • (1998) Protein Sci. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 29
    • 0035132058 scopus 로고    scopus 로고
    • Overexpression of heat-shock protein 25 augments radiation-induced cell-cycle arrest in murine L929 cells
    • Cho H.N., Lee S.J., Park S.H., Lee Y., Cho C.K., Lee Y.S. Overexpression of heat-shock protein 25 augments radiation-induced cell-cycle arrest in murine L929 cells. Int. J. Radiat. Biol. 77:2001;225-233.
    • (2001) Int. J. Radiat. Biol. , vol.77 , pp. 225-233
    • Cho, H.N.1    Lee, S.J.2    Park, S.H.3    Lee, Y.4    Cho, C.K.5    Lee, Y.S.6
  • 30
    • 0345129995 scopus 로고    scopus 로고
    • Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element
    • Soh J.W., Lee E.H., Prywes R., Weinstein I.B. Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element. Mol. Cell. Biol. 19:1999;1313-1324.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1313-1324
    • Soh, J.W.1    Lee, E.H.2    Prywes, R.3    Weinstein, I.B.4
  • 31
    • 0027170176 scopus 로고
    • RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblasts
    • Cook S.J., Rubinfeld B., Albert I., McCormick F. RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblasts. EMBO. J. 12:1993;3475-3485.
    • (1993) EMBO. J. , vol.12 , pp. 3475-3485
    • Cook, S.J.1    Rubinfeld, B.2    Albert, I.3    McCormick, F.4
  • 32
    • 0028239101 scopus 로고
    • Inhibition of v-raf-dependent c-fos expression and transformation by a kinase-defective mutant of the mitogen-activated protein kinase ERK2
    • Kortenjann M., Thomae O., Shaw P.E. Inhibition of v-raf-dependent c-fos expression and transformation by a kinase-defective mutant of the mitogen-activated protein kinase ERK2. Mol. Cell. Biol. 14:1994;4815-4824.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4815-4824
    • Kortenjann, M.1    Thomae, O.2    Shaw, P.E.3
  • 33
    • 0034652599 scopus 로고    scopus 로고
    • Dominant-negative Jun N-terminal protein kinase (JNK1) inhibits metabolic oxidative stress during glucose deprivation in a human breast carcinoma cell line
    • Lee Y.J., Galoforo S.S., Sim J.E., Ridnour L.A., Choi J., Forman H.J., Corry P.M., Spitz D.R. Dominant-negative Jun N-terminal protein kinase (JNK1) inhibits metabolic oxidative stress during glucose deprivation in a human breast carcinoma cell line. Free. Radic. Biol. Med. 28:2000;575-584.
    • (2000) Free. Radic. Biol. Med. , vol.28 , pp. 575-584
    • Lee, Y.J.1    Galoforo, S.S.2    Sim, J.E.3    Ridnour, L.A.4    Choi, J.5    Forman, H.J.6    Corry, P.M.7    Spitz, D.R.8
  • 34
    • 0028905076 scopus 로고
    • Transcription factor ATF2 regulation by the JNK signal transduction pathway
    • Gupta S., Campbell D., Derijard B., Davis R.J. Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science. 267:1995;389-393.
    • (1995) Science , vol.267 , pp. 389-393
    • Gupta, S.1    Campbell, D.2    Derijard, B.3    Davis, R.J.4
  • 35
    • 0035972152 scopus 로고    scopus 로고
    • Generation of fusion genes carrying drug resistance, green fluorescent protein, and herpes simplex virus thymidine kinase genes in a single cistron
    • Oh S.C., Nam S.-Y., Kwon H.-C., Kim C.-M., Seo J.-S., Lee J.-E., Sung R.-H., Jang Y.-J., Chung Y.-H., Chung H.-Y. Generation of fusion genes carrying drug resistance, green fluorescent protein, and herpes simplex virus thymidine kinase genes in a single cistron. Mol. Cells. 11:2001;192-197.
    • (2001) Mol. Cells , vol.11 , pp. 192-197
    • Oh, S.C.1    Nam, S.-Y.2    Kwon, H.-C.3    Kim, C.-M.4    Seo, J.-S.5    Lee, J.-E.6    Sung, R.-H.7    Jang, Y.-J.8    Chung, Y.-H.9    Chung, H.-Y.10
  • 36
    • 0029862497 scopus 로고    scopus 로고
    • A stable human-derived packaging cell line for production of high titer retrovirus/vesicular stomatitis virus G pseudotypes
    • Ory D.S., Neugeboren B.A., Mulligan R.C. A stable human-derived packaging cell line for production of high titer retrovirus/vesicular stomatitis virus G pseudotypes. Proc. Natl. Acad. Sci. USA. 93:1996;11400-11406.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11400-11406
    • Ory, D.S.1    Neugeboren, B.A.2    Mulligan, R.C.3
  • 39
  • 40
    • 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., Yu J.S., Yang S.D. 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. 351:2000;221-232.
    • (2000) Biochem. J. , vol.351 , pp. 221-232
    • Chan, W.H.1    Yu, J.S.2    Yang, S.D.3
  • 41
    • 0032869695 scopus 로고    scopus 로고
    • Novel aspects of Ras proteins biology: Regulation and implications
    • Perez-Sala D., Rebollo A. Novel aspects of Ras proteins biology: regulation and implications. Cell Death Differ. 6:1999;722-728.
    • (1999) Cell Death Differ. , vol.6 , pp. 722-728
    • Perez-Sala, D.1    Rebollo, A.2
  • 43
    • 0032849088 scopus 로고    scopus 로고
    • New insights into the regulation of protein kinase C and novel phorbol ester receptors
    • Ron D., Kazanietz M.G. New insights into the regulation of protein kinase C and novel phorbol ester receptors. FASEB J. 13:1999;1658-1676.
    • (1999) FASEB J. , vol.13 , pp. 1658-1676
    • Ron, D.1    Kazanietz, M.G.2
  • 44
    • 0030976892 scopus 로고    scopus 로고
    • Association between v-Src and protein kinase C δ in v-Src-transformed fibroblasts
    • Zang Q., Lu Z., Curto M., Barile M., Shalloway D., Foster D.A. Association between v-Src and protein kinase C δ in v-Src-transformed fibroblasts. J. Biol. Chem. 272:1997;13275-13280.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13275-13280
    • Zang, Q.1    Lu, Z.2    Curto, M.3    Barile, M.4    Shalloway, D.5    Foster, D.A.6
  • 46
    • 0034806972 scopus 로고    scopus 로고
    • Enhanced ROS production in oncogenically transformed cells potentiates c-Jun N-terminal kinase and p38 mitogen-activated protein kinase activation and sensitization to genotoxic stress
    • Benhar M., Dalyot I., Engelberg D., Levitzki A. Enhanced ROS production in oncogenically transformed cells potentiates c-Jun N-terminal kinase and p38 mitogen-activated protein kinase activation and sensitization to genotoxic stress. Mol. Cell. Biol. 21:2001;6913-6926.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6913-6926
    • Benhar, M.1    Dalyot, I.2    Engelberg, D.3    Levitzki, A.4
  • 47
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • Adler V., Yin Z., Tew K.D., Ronai Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene. 18:1999;6104-6111.
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 48
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • Rhee S.G. Redox signaling: hydrogen peroxide as intracellular messenger. Exp. Mol. Med. 31:1999;53-59.
    • (1999) Exp. Mol. Med. , vol.31 , pp. 53-59
    • Rhee, S.G.1
  • 49
    • 0029020434 scopus 로고
    • Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts. Possible mechanisms for its accumulation
    • Akashi M., Hachiya M., Paquette R.L., Osawa Y., Shimizu S., Suzuki G. Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts. Possible mechanisms for its accumulation. J. Biol. Chem. 270:1995;15864-15869.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15864-15869
    • Akashi, M.1    Hachiya, M.2    Paquette, R.L.3    Osawa, Y.4    Shimizu, S.5    Suzuki, G.6
  • 50
    • 0028369815 scopus 로고
    • Lung manganese superoxide dismutase increases during cytokine-mediated protection against pulmonary oxygen toxicity in rats
    • Lewis-Molock Y., Suzuki K., Tanaguchi N., Nguyen D.H., Mason R.J., White C.W. Lung manganese superoxide dismutase increases during cytokine-mediated protection against pulmonary oxygen toxicity in rats. Am. J. Respir. Cell. Mol. Biol. 10:1994;133-141.
    • (1994) Am. J. Respir. Cell. Mol. Biol. , vol.10 , pp. 133-141
    • Lewis-Molock, Y.1    Suzuki, K.2    Tanaguchi, N.3    Nguyen, D.H.4    Mason, R.J.5    White, C.W.6


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