메뉴 건너뛰기




Volumn 124, Issue 5, 2003, Pages 575-579

Do developmentally-related changes in constitutive proteolysis affect aberrant protein accumulation and generation of the aged phenotype?

Author keywords

Aberrant protein; Constitutive proteolysis; Phenotype

Indexed keywords

POLYPEPTIDE; PROTEIN;

EID: 0038740639     PISSN: 00476374     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0047-6374(03)00005-8     Document Type: Review
Times cited : (9)

References (45)
  • 1
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Rota D.A., Davies K.J.A. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 4:2002;674-680.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 674-680
    • Rota, D.A.1    Davies, K.J.A.2
  • 2
    • 0037021453 scopus 로고    scopus 로고
    • Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
    • Bota D.A., Van Remmen H., Davies K.J.A. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Letts. 532:2002;103-106.
    • (2002) FEBS Letts. , vol.532 , pp. 103-106
    • Bota, D.A.1    Van Remmen, H.2    Davies, K.J.A.3
  • 3
    • 0035824663 scopus 로고    scopus 로고
    • Proteasomal inhibition in glyoxal-treated fibroblasts and resistance of glycated glucose-6-phosphate dehydrogenase to 20S proteasome degradation in vitro
    • Bulteau A.-L., Verbeke P., Petropoulos L., Chaffotle A.-F., Friguet B. Proteasomal inhibition in glyoxal-treated fibroblasts and resistance of glycated glucose-6-phosphate dehydrogenase to 20S proteasome degradation in vitro. J. Biol. Chem. 276:2001;45 662-45 668.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45662-45668
    • Bulteau, A.-L.1    Verbeke, P.2    Petropoulos, L.3    Chaffotle, A.-F.4    Friguet, B.5
  • 5
    • 0035451913 scopus 로고    scopus 로고
    • Proteasomes and proteasome inhibition in the central nervous system
    • Ding Q., Keller J.N. Proteasomes and proteasome inhibition in the central nervous system. Free Rad. Biol. Med. 31:2001;574-584.
    • (2001) Free Rad. Biol. Med. , vol.31 , pp. 574-584
    • Ding, Q.1    Keller, J.N.2
  • 7
    • 0035179456 scopus 로고    scopus 로고
    • Mutant protein in Huntington disease is resistant to proteolysis in affected brain
    • Dyer R.B., McMurray C.T. Mutant protein in Huntington disease is resistant to proteolysis in affected brain. Nat. Genet. 29:2001;270-278.
    • (2001) Nat. Genet. , vol.29 , pp. 270-278
    • Dyer, R.B.1    McMurray, C.T.2
  • 8
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosomal biogenesis
    • Findley D., Bartlet B., Varshavsky A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosomal biogenesis. Nature. 338:1989;394-401.
    • (1989) Nature , vol.338 , pp. 394-401
    • Findley, D.1    Bartlet, B.2    Varshavsky, A.3
  • 9
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • Fisk H.A., Yaffe M.P. A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145:1999;1199-1208.
    • (1999) J. Cell Biol. , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 10
    • 0030977793 scopus 로고    scopus 로고
    • Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxynonenal cross-linked protein
    • Friguet B., Szweda L.I. Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxynonenal cross-linked protein. FEBS Letts. 405:1997;21-25.
    • (1997) FEBS Letts. , vol.405 , pp. 21-25
    • Friguet, B.1    Szweda, L.I.2
  • 12
    • 0034571026 scopus 로고    scopus 로고
    • Oxidative stress, aging and the proteasomal system
    • Grune T. Oxidative stress, aging and the proteasomal system. Biogerom. 1:2000;31-40.
    • (2000) Biogerom. , vol.1 , pp. 31-40
    • Grune, T.1
  • 14
    • 0033926856 scopus 로고    scopus 로고
    • Increased methyl esterification of altered aspartyl residues in erythrocyte membranes in response to oxidative stress
    • Ingrosso A., D'Angelo S., Di Carlo E. Increased methyl esterification of altered aspartyl residues in erythrocyte membranes in response to oxidative stress. Eur. J. Biochem. 267:2000;4397-4405.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4397-4405
    • Ingrosso, A.1    D'Angelo, S.2    Di Carlo, E.3
  • 15
    • 0033972037 scopus 로고    scopus 로고
    • Possible involvement of proteasome inhibition in aging implications oxidative stress
    • Keller J.N., Hanni K.B., Markesbery W.R. Possible involvement of proteasome inhibition in aging implications oxidative stress. Mech. Ageing Dev. 113:2000;1302-1306.
    • (2000) Mech. Ageing Dev. , vol.113 , pp. 1302-1306
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 16
    • 0030995490 scopus 로고    scopus 로고
    • Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth and fatal seizures in mice
    • Kim E., Lowensen J.D., MacLaren D.C., Clarke S., Young S.G. Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth and fatal seizures in mice. Proc. Natl. Acad. Sci. USA. 94:1997;6132-6137.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6132-6137
    • Kim, E.1    Lowensen, J.D.2    MacLaren, D.C.3    Clarke, S.4    Young, S.G.5
  • 18
    • 0034891783 scopus 로고    scopus 로고
    • Oxidative modification of proteins during aging
    • Levine R.L., Stadtman E.R. Oxidative modification of proteins during aging. Exp. Geront. 36:2001;1495-1502.
    • (2001) Exp. Geront. , vol.36 , pp. 1495-1502
    • Levine, R.L.1    Stadtman, E.R.2
  • 19
    • 0034885731 scopus 로고    scopus 로고
    • Age-dependent deamidation of asparagine residues in proteins
    • Lindner H., Helliger W. Age-dependent deamidation of asparagine residues in proteins. Exp. Geront. 36:2001;1551-1563.
    • (2001) Exp. Geront. , vol.36 , pp. 1551-1563
    • Lindner, H.1    Helliger, W.2
  • 20
    • 0029123058 scopus 로고
    • Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress
    • Lithgow G.J., White T.M., Melov S., Johnson T.E. Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress. Proc. Natl. Acad. Sci. USA. 92:1995;7540-7544.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7540-7544
    • Lithgow, G.J.1    White, T.M.2    Melov, S.3    Johnson, T.E.4
  • 21
    • 0034575085 scopus 로고    scopus 로고
    • Longevity amid aging: Beneficial effects of exposure to mild stress
    • Minois N. Longevity amid aging: beneficial effects of exposure to mild stress. Biogeront. 1:2000;15-29.
    • (2000) Biogeront. , vol.1 , pp. 15-29
    • Minois, N.1
  • 22
    • 0034881368 scopus 로고    scopus 로고
    • Role of increased basal expression of heat shock protein 72 in colonic epithelial c2BBE adenocarcinoma cells
    • Musch M.W., Kaplan B., Chang E.B. Role of increased basal expression of heat shock protein 72 in colonic epithelial c2BBE adenocarcinoma cells. Cell Growth Diff. 12:2001;419-426.
    • (2001) Cell Growth Diff. , vol.12 , pp. 419-426
    • Musch, M.W.1    Kaplan, B.2    Chang, E.B.3
  • 23
    • 0034122917 scopus 로고    scopus 로고
    • Increase in oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells
    • Petropoulos I., Concordi M., Wang X., Hoenel B., Bregegere F., Milner Y., Friguet B. Increase in oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells. J. Geront. 55:2000;B220-B227.
    • (2000) J. Geront. , vol.55
    • Petropoulos, I.1    Concordi, M.2    Wang, X.3    Hoenel, B.4    Bregegere, F.5    Milner, Y.6    Friguet, B.7
  • 24
    • 17744372861 scopus 로고    scopus 로고
    • Roles of heat shock transcription factors in regulation of the heat shock response and beyond
    • Pirkkala L., Nykanen P., Sistonen L. Roles of heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J. 15:2001;1118-1131.
    • (2001) FASEB J. , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 25
    • 0035090477 scopus 로고    scopus 로고
    • Exercise, heat shock proteins, and myocardial protection from I-R injury
    • Powers S.K., Locke M., Demirel H.A. Exercise, heat shock proteins, and myocardial protection from I-R injury. Med. Sci. Sports Exercise. 33:2001;386-392.
    • (2001) Med. Sci. Sports Exercise , vol.33 , pp. 386-392
    • Powers, S.K.1    Locke, M.2    Demirel, H.A.3
  • 28
    • 0036132470 scopus 로고    scopus 로고
    • Protein turnover plays a key role in aging
    • Ryaazanov A.G., Nefsky B.S. Protein turnover plays a key role in aging. Mech. Ageing Dev. 123:2002;207-213.
    • (2002) Mech. Ageing Dev. , vol.123 , pp. 207-213
    • Ryaazanov, A.G.1    Nefsky, B.S.2
  • 30
    • 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 Rad. Biol. Med. 28:2000;70l-708.
    • (2000) Free Rad. Biol. Med. , vol.28
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Grune, T.4
  • 31
    • 0034571008 scopus 로고    scopus 로고
    • Molecular chaperones and the aging process
    • Soti C., Csermely P. Molecular chaperones and the aging process. Biogeront. 1:2000;225-233.
    • (2000) Biogeront. , vol.1 , pp. 225-233
    • Soti, C.1    Csermely, P.2
  • 32
    • 0033883489 scopus 로고    scopus 로고
    • Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos
    • Sutovsky P., Moren R.D., Ramalho-Santos J., Dominko T., Simerly C., Schatten G. Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos. Biol. Reprod. 63:2000;582-590.
    • (2000) Biol. Reprod. , vol.63 , pp. 582-590
    • Sutovsky, P.1    Moren, R.D.2    Ramalho-Santos, J.3    Dominko, T.4    Simerly, C.5    Schatten, G.6
  • 34
    • 0027321526 scopus 로고
    • Inhibitory effect of nonenzymic glycation on ubiquitination and ubiquitin-mediated degradation of lysozyme
    • Takizawa N., Takada K., Ohkawa K. Inhibitory effect of nonenzymic glycation on ubiquitination and ubiquitin-mediated degradation of lysozyme. Biochem. Biophys. Res. Commun. 192:1993;700-706.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 700-706
    • Takizawa, N.1    Takada, K.2    Ohkawa, K.3
  • 35
    • 0036132431 scopus 로고    scopus 로고
    • Caloric restriction and lifespan: A role for protein turnover
    • Tavernarakis N., Driscoll M. Caloric restriction and lifespan: a role for protein turnover. Mech. Ageing Dev. 123:2002;215-219.
    • (2002) Mech. Ageing Dev. , vol.123 , pp. 215-219
    • Tavernarakis, N.1    Driscoll, M.2
  • 36
    • 0035824651 scopus 로고    scopus 로고
    • Sensitivity of mammalian cells expressing mutant ubiquitin to protein damaging agents
    • Tsirigotis M., Zhang M., Chui R.K., Wouters B.G., Gray D.A. Sensitivity of mammalian cells expressing mutant ubiquitin to protein damaging agents. J. Biol. Chem. 276:2001;46 073-46 078.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46073-46078
    • Tsirigotis, M.1    Zhang, M.2    Chui, R.K.3    Wouters, B.G.4    Gray, D.A.5
  • 38
    • 0033793043 scopus 로고    scopus 로고
    • Modulating cellular aging in vitro: Hormetic effects of repeated mild heat stress on protein oxidation and glycation
    • Verbeke P., Clark B.F.C., Rattan S.I.S. Modulating cellular aging in vitro: hormetic effects of repeated mild heat stress on protein oxidation and glycation. Exp. Geront. 35:2000;787-794.
    • (2000) Exp. Geront. , vol.35 , pp. 787-794
    • Verbeke, P.1    Clark, B.F.C.2    Rattan, S.I.S.3
  • 39
    • 0035894209 scopus 로고    scopus 로고
    • Reduced levels of oxidized and glycated proteins in human fibroblasts exposed to repeated mild heat shock during serial passaging in vitro
    • Verbeke P., Clark B.F.C., Rattan S.I.S. Reduced levels of oxidized and glycated proteins in human fibroblasts exposed to repeated mild heat shock during serial passaging in vitro. Free Rad. Biol. Med. 31:2001;1593-1602.
    • (2001) Free Rad. Biol. Med. , vol.31 , pp. 1593-1602
    • Verbeke, P.1    Clark, B.F.C.2    Rattan, S.I.S.3
  • 42
    • 0027367968 scopus 로고
    • A human mitochondrial ATP-dependent protease that is highly homologous to bacterial LON protease
    • Wang N., Gottesman S., Willingham M.C., et al. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial LON protease. Proc. Natl. Acad. Sci. USA. 90:1993;11 247-11 251.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11247-11251
    • Wang, N.1    Gottesman, S.2    Willingham, M.C.3
  • 44
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of hunting tin is independent of polyglutamine aggregation
    • Zhou H., Li S.-H., Li X.-J. Chaperone suppression of cellular toxicity of hunting tin is independent of polyglutamine aggregation. J. Biol. Chem. 276:2001;48 417-48 424.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.-H.2    Li, X.-J.3
  • 45
    • 0036033355 scopus 로고    scopus 로고
    • Epidermal growth factor up-regulates the transcription of mouse Lon homologue ATP-dependent protease through extracellular signal regulated protein kinase- and phosphoinositol-3-kinase-dependent pathways
    • Zhu Y., Wang M., Lin H., Huang C., Shi X., Luo J. Epidermal growth factor up-regulates the transcription of mouse Lon homologue ATP-dependent protease through extracellular signal regulated protein kinase- and phosphoinositol-3-kinase-dependent pathways. Exp. Cell Res. 280:2002;97-106.
    • (2002) Exp. Cell Res. , vol.280 , pp. 97-106
    • Zhu, Y.1    Wang, M.2    Lin, H.3    Huang, C.4    Shi, X.5    Luo, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.