메뉴 건너뛰기




Volumn 123, Issue 4, 2012, Pages 635-644

Age-related differences in the dynamics of hippocampal proteasome recovery

Author keywords

hippocampus; immunoproteasome; neurodegen eration; POMP; proteasome; ubiquitin

Indexed keywords

BRAIN PROTEIN; PROTEASOME; PROTEASOME MATURATION PROTEIN; UNCLASSIFIED DRUG;

EID: 84867580630     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2012.07932.x     Document Type: Article
Times cited : (6)

References (41)
  • 1
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N. F., Sampat R. M., and, Kopito R. R., (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 2
    • 0034641694 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian protein interacting with 20S proteasome precursors
    • Burri L., Höckendorff J., Boehm U., Klamp T., Dohmen R. J., and, Lévy F., (2000) Identification and characterization of a mammalian protein interacting with 20S proteasome precursors. Proc. Natl Acad. Sci. USA 97, 10348-10353.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10348-10353
    • Burri, L.1    Höckendorff, J.2    Boehm, U.3    Klamp, T.4    Dohmen, R.J.5    Lévy, F.6
  • 4
    • 28744438867 scopus 로고    scopus 로고
    • Ump1 extends yeast lifespan and enhances viability during oxidative stress: Central role for the proteasome?
    • Chen Q., Torpe J., Domen J. R., Li F., and, Séller J. N., (2006) Ump1 extends yeast lifespan and enhances viability during oxidative stress: central role for the proteasome? Free Radic. Biol. Med. 40, 120-126.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 120-126
    • Chen, Q.1    Torpe, J.2    Domen, J.R.3    Li, F.4    Séller, J.N.5
  • 5
    • 27944510125 scopus 로고    scopus 로고
    • Proteasome dysfunction in mammalian aging: Steps and factors involved
    • Chondrogianni N., and, Gonos E. S., (2005) Proteasome dysfunction in mammalian aging: steps and factors involved. Exp. Gerontol. 40, 931-938.
    • (2005) Exp. Gerontol. , vol.40 , pp. 931-938
    • Chondrogianni, N.1    Gonos, E.S.2
  • 6
    • 34250661684 scopus 로고    scopus 로고
    • Overexpression of hUMP1/POMP proteasome accessory protein enhances proteasome-mediated antioxidant defence
    • Chondrogianni N., and, Gonos E. S., (2007) Overexpression of hUMP1/POMP proteasome accessory protein enhances proteasome-mediated antioxidant defence. Exp. Gerontol. 42, 899-903.
    • (2007) Exp. Gerontol. , vol.42 , pp. 899-903
    • Chondrogianni, N.1    Gonos, E.S.2
  • 7
    • 17144414925 scopus 로고    scopus 로고
    • Overexpression of proteasome β5 subunit increases the amount of assembled proteasome and confers ameliorated response to oxidative stress and higher survival rates
    • Chondrogianni N., Tzavelas C., Pemberton A. J., Nezis I. P., Rivett A. J., and, Gonos E. S., (2005) Overexpression of proteasome β5 subunit increases the amount of assembled proteasome and confers ameliorated response to oxidative stress and higher survival rates. J. Biol. Chem. 280, 11840-11850.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11840-11850
    • Chondrogianni, N.1    Tzavelas, C.2    Pemberton, A.J.3    Nezis, I.P.4    Rivett, A.J.5    Gonos, E.S.6
  • 8
    • 84855328686 scopus 로고    scopus 로고
    • SiRNA silencing of proteasome maturation protein (POMP) activates the unfolded protein response and constitutes a model for KLICK genodermatosis
    • doi: 10.1371/journal.pone.0029471
    • Dahlqvist J., Törmä H., Badhai J., and, Dahl N., (2012) siRNA silencing of proteasome maturation protein (POMP) activates the unfolded protein response and constitutes a model for KLICK genodermatosis. PLoS ONE 7, e29471. doi: 10.1371/journal.pone.0029471.
    • (2012) PLoS ONE , vol.7
    • Dahlqvist, J.1    Törmä, H.2    Badhai, J.3    Dahl, N.4
  • 9
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G., Standaert R. F., Lane W. S., Choi S., Corey E. J., and, Schreiber S. L., (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 11
    • 36749025650 scopus 로고    scopus 로고
    • The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum
    • Fricke B., Heink S., Steffen J., Kloetzel P. M., and, Krüger E., (2007) The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum. EMBO Rep. 8, 1170-1175.
    • (2007) EMBO Rep. , vol.8 , pp. 1170-1175
    • Fricke, B.1    Heink, S.2    Steffen, J.3    Kloetzel, P.M.4    Krüger, E.5
  • 12
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska M., Rock K. L., and, Goldberg A. L., (1993) Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365, 264-267.
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 13
    • 35248841938 scopus 로고    scopus 로고
    • Molecular and cellular characterization of the age-related neuroinflammatory processes occurring in normal rat hippocampus: Potential relation with the loss of somatostatin GABAergic neurons
    • Gavilan M. P., Revilla E., Pintado C., et al,. (2007) Molecular and cellular characterization of the age-related neuroinflammatory processes occurring in normal rat hippocampus: potential relation with the loss of somatostatin GABAergic neurons. J. Neurochem. 103, 984-996.
    • (2007) J. Neurochem. , vol.103 , pp. 984-996
    • Gavilan, M.P.1    Revilla, E.2    Pintado, C.3
  • 15
    • 74049104138 scopus 로고    scopus 로고
    • Dysfunction of the unfolded protein response increases neurodegeneration in aged rat hippocampus following proteasome inhibition
    • Gavilán M. P., Pintado C., Gavilán E., Jiménez S., Ríos R. M., Vitorica J., Castaño A., and, Ruano D., (2009b) Dysfunction of the unfolded protein response increases neurodegeneration in aged rat hippocampus following proteasome inhibition. Aging Cell 8, 654-665.
    • (2009) Aging Cell , vol.8 , pp. 654-665
    • Gavilán, M.P.1    Pintado, C.2    Gavilán, E.3    Jiménez, S.4    Ríos, R.M.5    Vitorica, J.6    Castaño, A.7    Ruano, D.8
  • 16
    • 0033854415 scopus 로고    scopus 로고
    • Identification of proteassemblin, a mammalian homologue of the yeast protein, Ump1p, that is required for normal proteasome assembly
    • Griffin T. A., Slack J. P., McCluskey T. S., Monaco J. J., and, Colbert R. A., (2000) Identification of proteassemblin, a mammalian homologue of the yeast protein, Ump1p, that is required for normal proteasome assembly. Mol. Cell Biol. Res. Commun. 3, 212-217.
    • (2000) Mol. Cell Biol. Res. Commun. , vol.3 , pp. 212-217
    • Griffin, T.A.1    Slack, J.P.2    McCluskey, T.S.3    Monaco, J.J.4    Colbert, R.A.5
  • 17
    • 21544475903 scopus 로고    scopus 로고
    • IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response
    • Heink S., Ludwig D., Kloetzel P. M., and, Krüger E., (2005) IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc. Natl Acad. Sci. USA 102, 9241-9246.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.M.3    Krüger, E.4
  • 20
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser M., (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 22
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston J. A., Ward C. L., and, Kopito R. P., (1998) Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143, 1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.P.3
  • 24
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., and, Frydman J., (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454, 1088-1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 25
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • Keller J. N., Huang F. F., and, Markesbery W. R., (2000) Decreased levels of proteasome activity and proteasome expression in aging spinal cord. Neuroscience 98, 149-156.
    • (2000) Neuroscience , vol.98 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 26
    • 0036546011 scopus 로고    scopus 로고
    • The proteasome in brain aging
    • Keller J. N., Gee J., and, Ding Q., (2002) The proteasome in brain aging. Ageing Res. Rev. 1, 279-293.
    • (2002) Ageing Res. Rev. , vol.1 , pp. 279-293
    • Keller, J.N.1    Gee, J.2    Ding, Q.3
  • 27
    • 0035290730 scopus 로고    scopus 로고
    • Antigen processing by the proteasome
    • Kloetzel P. M., (2001) Antigen processing by the proteasome. Nat. Rev. Mol. Cell Biol. 2, 179-187.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 179-187
    • Kloetzel, P.M.1
  • 28
    • 34548651757 scopus 로고    scopus 로고
    • PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress
    • Kondratyev M., Avezov E., Shenkman M., Groisman B., and, Lederkremer G. Z., (2007) PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress. Exp. Cell Res. 313, 3395-3407.
    • (2007) Exp. Cell Res. , vol.313 , pp. 3395-3407
    • Kondratyev, M.1    Avezov, E.2    Shenkman, M.3    Groisman, B.4    Lederkremer, G.Z.5
  • 29
    • 77953483260 scopus 로고    scopus 로고
    • Age-related neuroinflammatory changes negatively impact on neuronal function
    • Lynch M. A., (2010) Age-related neuroinflammatory changes negatively impact on neuronal function. Front. Aging Neurosci. 1, 6.
    • (2010) Front. Aging Neurosci. , vol.1 , pp. 6
    • Lynch, M.A.1
  • 30
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes
    • Meiners S., Heyken D., Weller A., Ludwig A., Stangl K., Kloetzel P. M., and, Krüger E., (2003) Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes. J. Biol. Chem. 278, 21517-21525.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Ludwig, A.4    Stangl, K.5    Kloetzel, P.M.6    Krüger, E.7
  • 31
    • 67349217063 scopus 로고    scopus 로고
    • ER and aging-protein folding and the ER stress response
    • Naidoo N., (2009) ER and aging-protein folding and the ER stress response. Ageing Res. Rev. 8, 150-159.
    • (2009) Ageing Res. Rev. , vol.8 , pp. 150-159
    • Naidoo, N.1
  • 33
    • 84860499027 scopus 로고    scopus 로고
    • LPS-induced neuroinflammation leads to the accumulation of ubiquitinated proteins and increases susceptibility to neurodegeneration induced by proteasome inhibition in rat hippocampus
    • Pintado C., Gavilán M. P., Gavilán E., García-Cuervo L., Gutiérrez A., Vitorica J., Castaño A., Ríos R. M., and, Ruano D., (2012) LPS-induced neuroinflammation leads to the accumulation of ubiquitinated proteins and increases susceptibility to neurodegeneration induced by proteasome inhibition in rat hippocampus. J. Neuroinflammation 9, 87.
    • (2012) J. Neuroinflammation , vol.9 , pp. 87
    • Pintado, C.1    Gavilán, M.P.2    Gavilán, E.3    García-Cuervo, L.4    Gutiérrez, A.5    Vitorica, J.6    Castaño, A.7    Ríos, R.M.8    Ruano, D.9
  • 34
    • 15244361487 scopus 로고    scopus 로고
    • Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins
    • Powell S. R., Wang P., Divald A., Teichberg S., Haridas V., McCloskey T. W., Davies K. J., and, Katzeff H., (2005) Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins. Free Radic. Biol. Med. 38, 1093-1101.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1093-1101
    • Powell, S.R.1    Wang, P.2    Divald, A.3    Teichberg, S.4    Haridas, V.5    McCloskey, T.W.6    Davies, K.J.7    Katzeff, H.8
  • 35
    • 77950366349 scopus 로고    scopus 로고
    • Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells
    • Radhakrishnan S. K., Lee C. S., Young P., Beskow A., Chan J. Y., and, Deshaies R. J., (2010) Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells. Mol. Cell 38, 17-28.
    • (2010) Mol. Cell , vol.38 , pp. 17-28
    • Radhakrishnan, S.K.1    Lee, C.S.2    Young, P.3    Beskow, A.4    Chan, J.Y.5    Deshaies, R.J.6
  • 36
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M., and, Hill C. P., (2005) Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15, 27-33.
    • (2005) Trends Cell Biol. , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 37
    • 0035070697 scopus 로고    scopus 로고
    • Regulation of proteasome complexes by gamma-interferon and phosphorylation
    • Rivett A. J., Bose S., Brooks P., and, Broadfoot K. I., (2001) Regulation of proteasome complexes by gamma-interferon and phosphorylation. Biochimie 83, 363-366.
    • (2001) Biochimie , vol.83 , pp. 363-366
    • Rivett, A.J.1    Bose, S.2    Brooks, P.3    Broadfoot, K.I.4
  • 38
    • 77955596988 scopus 로고    scopus 로고
    • Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress
    • Seifert U., Bialy L. P., Ebstein F., et al,. (2010) Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress. Cell 142, 613-624.
    • (2010) Cell , vol.142 , pp. 613-624
    • Seifert, U.1    Bialy, L.P.2    Ebstein, F.3
  • 40
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier T. C., (2001) Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. 36, 1539-1550.
    • (2001) Exp. Gerontol. , vol.36 , pp. 1539-1550
    • Squier, T.C.1
  • 41
    • 0034604384 scopus 로고    scopus 로고
    • Characterisation of the newly identified human Ump1 homologue POMP and analysis of LMP7 (β5i) incorporation into 20 S proteasomes
    • Witt E., Zantopf D., Schmidt M., Kraft R., Kloetzel P. M., and, Krüger E., (2000) Characterisation of the newly identified human Ump1 homologue POMP and analysis of LMP7 (β5i) incorporation into 20 S proteasomes. J. Mol. Biol. 301, 1-9.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1-9
    • Witt, E.1    Zantopf, D.2    Schmidt, M.3    Kraft, R.4    Kloetzel, P.M.5    Krüger, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.