메뉴 건너뛰기




Volumn 39, Issue 3, 2004, Pages 423-432

Proteasome inhibition increases HuR level, restores heat-inducible HSP72 expression and thermotolerance in WI-38 senescent human fibroblasts

Author keywords

Aging; Heat shock; HSP72; HSP72 mRNA; Human fibroblast; HuR; MG132; mRNA stability; Proteasome; Thermotolerance

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; HEAT SHOCK PROTEIN 72; HUR PROTEIN; MESSENGER RNA; PROTEASOME; RNA BINDING PROTEIN;

EID: 1342265394     PISSN: 05315565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exger.2003.12.004     Document Type: Article
Times cited : (20)

References (51)
  • 1
    • 0029806382 scopus 로고    scopus 로고
    • Activation of heat-shock transcription factor 1 by hypertonic shock in 3T3 cells
    • Alfieri R.R., Petronini P.G., Urbani S., Borghetti A.F. Activation of heat-shock transcription factor 1 by hypertonic shock in 3T3 cells. Biochem. J. 319:1996;601-606.
    • (1996) Biochem. J. , vol.319 , pp. 601-606
    • Alfieri, R.R.1    Petronini, P.G.2    Urbani, S.3    Borghetti, A.F.4
  • 3
    • 0035879116 scopus 로고    scopus 로고
    • Heat-induce proteasomic degradation of HSF1 in serum-starved human fibroblasts aging in vitro
    • Bonelli M.A., Alfieri R.R., Poli M., Petronini P.G., Borghetti A.F. Heat-induce proteasomic degradation of HSF1 in serum-starved human fibroblasts aging in vitro. Exp. Cell Res. 267:2001;165-172.
    • (2001) Exp. Cell Res. , vol.267 , pp. 165-172
    • Bonelli, M.A.1    Alfieri, R.R.2    Poli, M.3    Petronini, P.G.4    Borghetti, A.F.5
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford R.H. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, R.H.1
  • 5
    • 0038120902 scopus 로고    scopus 로고
    • Cellular senescence in human keratinocytes: Unchanged proteolytic capacity and increased protein load
    • Brégégère F., Soraka Y., Bismuth J., Friguet B., Milner Y. Cellular senescence in human keratinocytes: unchanged proteolytic capacity and increased protein load. Exp. Gerontol. 38:2003;619-629.
    • (2003) Exp. Gerontol. , vol.38 , pp. 619-629
    • Brégégère, F.1    Soraka, Y.2    Bismuth, J.3    Friguet, B.4    Milner, Y.5
  • 7
    • 0037082124 scopus 로고    scopus 로고
    • Age-dependent declines in proteasome activity in the heart
    • Bulteau A.L., Szweda L.I., Friguet B. Age-dependent declines in proteasome activity in the heart. Arch. Biochem. Biophys. 397:2002;298-304.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 298-304
    • Bulteau, A.L.1    Szweda, L.I.2    Friguet, B.3
  • 8
    • 0033785045 scopus 로고    scopus 로고
    • Age-related alterations of proteasome structure and function in aging epidermis
    • Bulteau A.L., Petropoulos I., Friguet B. Age-related alterations of proteasome structure and function in aging epidermis. Exp. Gerontol. 35:2000;767-777.
    • (2000) Exp. Gerontol. , vol.35 , pp. 767-777
    • Bulteau, A.L.1    Petropoulos, I.2    Friguet, B.3
  • 9
    • 0019551730 scopus 로고
    • Western blotting: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to humidified nitrocellulose and radiographic detection with antibody and radioiodinated protein a
    • Burnette W.N. Western blotting: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to humidified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:1981;195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 10
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush K.T., Goldberg A.L., Nigam S.K. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J. Biol. Chem. 272:1997;9086-9092.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 11
    • 0042346327 scopus 로고    scopus 로고
    • Central role of the proteasome in senescence and survival of human fibroblasts: Induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation
    • Chondrogianni N., Stratford F.L.L., Trougakos I.P., Friguet B., Rivett A.J., Gonos E.S. Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation. J. Biol. Chem. 278:2003;28026-28037.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28026-28037
    • Chondrogianni, N.1    Stratford, F.L.L.2    Trougakos, I.P.3    Friguet, B.4    Rivett, A.J.5    Gonos, E.S.6
  • 13
    • 0032526427 scopus 로고    scopus 로고
    • Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs
    • Fan X.C., Steitz J.A. Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs. EMBO J. 17:1998;3448-3460.
    • (1998) EMBO J. , vol.17 , pp. 3448-3460
    • Fan, X.C.1    Steitz, J.A.2
  • 15
    • 0034850959 scopus 로고    scopus 로고
    • Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock
    • Gallouzi I.-E., Brennan C.M., Steitz J.A. Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock. RNA. 7:2001;1348-1361.
    • (2001) RNA , vol.7 , pp. 1348-1361
    • Gallouzi, I.-E.1    Brennan, C.M.2    Steitz, J.A.3
  • 16
    • 0034571026 scopus 로고    scopus 로고
    • Oxidative stress, aging and the proteasomal system
    • Grune T. Oxidative stress, aging and the proteasomal system. Biogerontology. 1:2000;31-40.
    • (2000) Biogerontology , vol.1 , pp. 31-40
    • Grune, T.1
  • 18
    • 50549218525 scopus 로고
    • The limited in vitro lifespan of human diploid cell strains
    • Hayflich L. The limited in vitro lifespan of human diploid cell strains. Exp. Cell Res. 37:1965;614-636.
    • (1965) Exp. Cell Res. , vol.37 , pp. 614-636
    • Hayflich, L.1
  • 19
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperons, and proteotoxicity
    • Hightower L.E. Heat shock, stress proteins, chaperons, and proteotoxicity. Cell. 66:1991;191-197.
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 20
    • 0000097632 scopus 로고
    • Conserved features of eukaryotic HSP70 genes revealed by comparison with the nucleotide sequence of human HSP70
    • Hunt C., Morimoto R.I. Conserved features of eukaryotic HSP70 genes revealed by comparison with the nucleotide sequence of human HSP70. Proc. Natl Acad. Sci. USA. 82:1985;6455-6459.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 6455-6459
    • Hunt, C.1    Morimoto, R.I.2
  • 21
    • 0033534750 scopus 로고    scopus 로고
    • Proteasome inhibitors MG132 and lactacystin hyperphosporylate HSF1 and induce hsp70 and hsp27 expression
    • Kim D., Kim S.H., Li G.C. Proteasome inhibitors MG132 and lactacystin hyperphosporylate HSF1 and induce hsp70 and hsp27 expression. Biochem, Biophys. Res. Commun. 254:1999;264-268.
    • (1999) Biochem, Biophys. Res. Commun. , vol.254 , pp. 264-268
    • Kim, D.1    Kim, S.H.2    Li, G.C.3
  • 22
    • 0036084783 scopus 로고    scopus 로고
    • Heat shock proteins: Modifying factors in physiological stress responses and acquired thermotolerance
    • Kregel K.C. Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J. Appl. Physiol. 92:2002;2177-2186.
    • (2002) J. Appl. Physiol. , vol.92 , pp. 2177-2186
    • Kregel, K.C.1
  • 23
    • 0033574789 scopus 로고    scopus 로고
    • Control of mRNA decay by heat shock-ubiquitin-proteasome pathway
    • Laroia G., Cuesta R., Brewer G., Schneider R.J. Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science. 284:1999;499-502.
    • (1999) Science , vol.284 , pp. 499-502
    • Laroia, G.1    Cuesta, R.2    Brewer, G.3    Schneider, R.J.4
  • 24
    • 0002858113 scopus 로고    scopus 로고
    • Proteasome inhibitors cause induction of heat shock proteins and trehalose, which confers thermotolerance in Saccharomices cerevisiae
    • Lee D.H., Goldberg A.L. Proteasome inhibitors cause induction of heat shock proteins and trehalose, which confers thermotolerance in Saccharomices cerevisiae. Mol. Cell Biol. 18:1998;30-38.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 30-38
    • Lee, D.H.1    Goldberg, A.L.2
  • 25
    • 0020130877 scopus 로고
    • Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster ovary cells
    • Li G.C., Werb Z. Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster ovary cells. Proc. Natl Acad. Sci. USA. 79:1982;3218-3222.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 3218-3222
    • Li, G.C.1    Werb, Z.2
  • 26
    • 0022555843 scopus 로고
    • The heat shock response
    • Lindquist S. The heat shock response. Annu. Rev. Biochem. 55:1986;1151-1191.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 27
    • 0000931391 scopus 로고    scopus 로고
    • Attenuated heat shock transcriptional response in aging: Molecular mechanism and implication in the biology of aging
    • U. Feige, R.I. Morimoto, I. Yahara, & B. Polla. Basel: Birkhauser Verlag
    • Liu A.Y.-C., Lee K., Manalo D., Huang L.E. Attenuated heat shock transcriptional response in aging: Molecular mechanism and implication in the biology of aging. Feige U., Morimoto R.I., Yahara I., Polla B. Stress-Inducible Cellular Responses. 1996;394-408 Birkhauser Verlag, Basel.
    • (1996) Stress-Inducible Cellular Responses , pp. 394-408
    • Liu, A.Y.-C.1    Lee, K.2    Manalo, D.3    Huang, L.E.4
  • 28
    • 0026699672 scopus 로고
    • Reduction in heat shock gene expression correlates with increased thermosensitivity in senescent human fibroblasts
    • Luce M.C., Cristofalo V.J. Reduction in heat shock gene expression correlates with increased thermosensitivity in senescent human fibroblasts. Exp. Cell Res. 202:1992;9-16.
    • (1992) Exp. Cell Res. , vol.202 , pp. 9-16
    • Luce, M.C.1    Cristofalo, V.J.2
  • 31
    • 1342294159 scopus 로고    scopus 로고
    • Stability of the nuclear protein turnover during cellular senescence of human fibroblasts
    • Merker K., Ullrich O., Schmidt H., Sitte N., Grune T. Stability of the nuclear protein turnover during cellular senescence of human fibroblasts. FASEB. J. 17:2003;1963-1965.
    • (2003) FASEB. J. , vol.17 , pp. 1963-1965
    • Merker, K.1    Ullrich, O.2    Schmidt, H.3    Sitte, N.4    Grune, T.5
  • 34
    • 0027526648 scopus 로고
    • Different HSP70 expression and cell survival during adaptive responses of 3T3 and transformed 3T3 cells to osmotic stress
    • Petronini P.G., Alfieri R., De Angelis E.M., Campanini C., Borghetti A.F., Wheeler K.P. Different HSP70 expression and cell survival during adaptive responses of 3T3 and transformed 3T3 cells to osmotic stress. Br. J. Cancer. 67:1993;493-499.
    • (1993) Br. J. Cancer , vol.67 , pp. 493-499
    • Petronini, P.G.1    Alfieri, R.2    De Angelis, E.M.3    Campanini, C.4    Borghetti, A.F.5    Wheeler, K.P.6
  • 36
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:1994;761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 37
    • 0034713329 scopus 로고    scopus 로고
    • Is beta-galactosidase staining a marker of senescence in vitro and in vivo?
    • Severino J., Allen R.G., Balin S., Balin A., Cristofalo V.J. Is beta-galactosidase staining a marker of senescence in vitro and in vivo? Exp. Cell Res. 257:2000;162-171.
    • (2000) Exp. Cell Res. , vol.257 , pp. 162-171
    • Severino, J.1    Allen, R.G.2    Balin, S.3    Balin, A.4    Cristofalo, V.J.5
  • 38
    • 0034117954 scopus 로고    scopus 로고
    • Protein oxidation and degradation during proliferative senescence of human MRC-5 fibroblasts
    • Sitte N., Merker K., von Zglinicki T., Grune T. Protein oxidation and degradation during proliferative senescence of human MRC-5 fibroblasts. Free Radic. Biol. Med. 28:2000;701-708.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 701-708
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Grune, T.4
  • 39
    • 0033673408 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part I-effects of proliferative senescence
    • Sitte N., Merker K., von Zglinicki T., Grune T., Davies K.J. Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part I-effects of proliferative senescence. FASEB J. 14:2000;2495-2502.
    • (2000) FASEB J. , vol.14 , pp. 2495-2502
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Grune, T.4    Davies, K.J.5
  • 40
    • 0033674181 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part II-aging of nondividing cells
    • Sitte N., Merker K., von Zglinicki T., Davies K.J., Grune T. Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part II-aging of nondividing cells. FASEB J. 14:2000;2503-2510.
    • (2000) FASEB J. , vol.14 , pp. 2503-2510
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Davies, K.J.4    Grune, T.5
  • 41
    • 0034571008 scopus 로고    scopus 로고
    • Molecular chaperones and the aging process
    • Söti C., Csermely P. Molecular chaperones and the aging process. Biogerontology. 1:2000;225-233.
    • (2000) Biogerontology , vol.1 , pp. 225-233
    • Söti, C.1    Csermely, P.2
  • 43
    • 0142186172 scopus 로고    scopus 로고
    • Aging and molecular chaperones
    • Söti C., Csermely P. Aging and molecular chaperones. Exp. Gerontol. 38:2003;m1037-m1040.
    • (2003) Exp. Gerontol. , vol.38
    • Söti, C.1    Csermely, P.2
  • 44
    • 0042330311 scopus 로고    scopus 로고
    • Apoptosis, necrosis and cellular senescence: Chaperone occupancy as a potential switch
    • Söti C., Subbarao Sreedhart A., Csermely P. Apoptosis, necrosis and cellular senescence: chaperone occupancy as a potential switch. Aging Cell. 2:2003;39-45.
    • (2003) Aging Cell , vol.2 , pp. 39-45
    • Söti, C.1    Subbarao Sreedhart, A.2    Csermely, P.3
  • 45
    • 0034782105 scopus 로고    scopus 로고
    • The proteasome and its function in the ageing process
    • Stolzing A., Grune T. The proteasome and its function in the ageing process. Clin. Exp. Dermatol. 26:2001;566-572.
    • (2001) Clin. Exp. Dermatol. , vol.26 , pp. 566-572
    • Stolzing, A.1    Grune, T.2
  • 46
    • 0142011160 scopus 로고    scopus 로고
    • Metabolic stabilization of MAP kinase phosphatase-2 in senescence of human fibroblasts
    • Torres C., Francis M.K., Lorenzini A., Tresini M., Cristofalo V.J. Metabolic stabilization of MAP kinase phosphatase-2 in senescence of human fibroblasts. Exp. Cell Res. 290:2003;195-206.
    • (2003) Exp. Cell Res. , vol.290 , pp. 195-206
    • Torres, C.1    Francis, M.K.2    Lorenzini, A.3    Tresini, M.4    Cristofalo, V.J.5
  • 47
    • 0036774482 scopus 로고    scopus 로고
    • Matrix-mediated cellular rejuvenation
    • Volloch V., Kaplan D. Matrix-mediated cellular rejuvenation. Matrix Biol. 21:2003;533-543.
    • (2003) Matrix Biol. , vol.21 , pp. 533-543
    • Volloch, V.1    Kaplan, D.2
  • 48
    • 0032434207 scopus 로고    scopus 로고
    • Reduced thermotolerance in aged cells results from a loss of an hsp72-mediated control of JNK signaling pathway
    • Volloch V., Mosser D.D., Massie B., Sherman M.Y. Reduced thermotolerance in aged cells results from a loss of an hsp72-mediated control of JNK signaling pathway. Cell Stress Chaperones. 3:1998;265-271.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 265-271
    • Volloch, V.1    Mosser, D.D.2    Massie, B.3    Sherman, M.Y.4
  • 50
    • 0034908634 scopus 로고    scopus 로고
    • Loss of HuR is linked to reduced expression of proliferative genes during replicative senescence
    • Wang W., Yang X., Cristofalo V.J., Holbrook N.J., Gorospe M. Loss of HuR is linked to reduced expression of proliferative genes during replicative senescence. Mol. Cell Biol. 21:2001;5889-5898.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 5889-5898
    • Wang, W.1    Yang, X.2    Cristofalo, V.J.3    Holbrook, N.J.4    Gorospe, M.5
  • 51
    • 0029780370 scopus 로고    scopus 로고
    • Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells
    • Zhou M., Wu X., Ginsberg H.N. Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells. J. Biol. Chem. 271:1996;24769-24775.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24769-24775
    • Zhou, M.1    Wu, X.2    Ginsberg, H.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.