메뉴 건너뛰기




Volumn 27, Issue 5-6, 2006, Pages 444-454

Autophagy as a cell-repair mechanism: Activation of chaperone-mediated autophagy during oxidative stress

Author keywords

Aging; Autophagy; Chaperone mediated autophagy; Chaperones; Lysosomes; Oxidative stress; Protein aggregation

Indexed keywords

CHAPERONE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN; PROTEIN;

EID: 33749185898     PISSN: 00982997     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mam.2006.08.007     Document Type: Review
Times cited : (127)

References (35)
  • 1
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes F., and Dice J.F. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J. Cell Sci. 114 (2001) 2491-2499
    • (2001) J. Cell Sci. , vol.114 , pp. 2491-2499
    • Agarraberes, F.1    Dice, J.F.2
  • 2
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • Agarraberes F., Terlecky S., and Dice J. An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J. Cell Biol. 137 (1997) 825-834
    • (1997) J. Cell Biol. , vol.137 , pp. 825-834
    • Agarraberes, F.1    Terlecky, S.2    Dice, J.3
  • 3
    • 0036710928 scopus 로고    scopus 로고
    • Lipofuscin: mechanisms of age-related accumulation and influence on cell function
    • Brunk U.T., and Terman A. Lipofuscin: mechanisms of age-related accumulation and influence on cell function. Free Radic. Biol. Med. 33 (2002) 611-619
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 611-619
    • Brunk, U.T.1    Terman, A.2
  • 4
    • 0024975155 scopus 로고
    • A role for a 70 kDa heat shock protein in lysosomal degradation of intracellular protein
    • Chiang H., Terlecky S., Plant C., and Dice J. A role for a 70 kDa heat shock protein in lysosomal degradation of intracellular protein. Science 246 (1989) 382-385
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.1    Terlecky, S.2    Plant, C.3    Dice, J.4
  • 5
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: in sickness and in health
    • Cuervo A. Autophagy: in sickness and in health. Trends Cell Biol. 14 (2004) 70-77
    • (2004) Trends Cell Biol. , vol.14 , pp. 70-77
    • Cuervo, A.1
  • 6
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo A., and Dice J. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273 (1996) 501-503
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.1    Dice, J.2
  • 7
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of lamp2a levels in the lysosomal membrane
    • Cuervo A., and Dice J. Regulation of lamp2a levels in the lysosomal membrane. Traffic 1 (2000) 570-583
    • (2000) Traffic , vol.1 , pp. 570-583
    • Cuervo, A.1    Dice, J.2
  • 8
    • 0034510572 scopus 로고    scopus 로고
    • Unique properties of lamp2a compared to other lamp2 isoforms
    • Cuervo A., and Dice J. Unique properties of lamp2a compared to other lamp2 isoforms. J. Cell Sci. 113 (2000) 4441-4450
    • (2000) J. Cell Sci. , vol.113 , pp. 4441-4450
    • Cuervo, A.1    Dice, J.2
  • 9
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo A.M., and Dice J.F. Age-related decline in chaperone-mediated autophagy. J. Biol. Chem. 275 (2000) 31505-31513
    • (2000) J. Biol. Chem. , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 10
    • 0031041902 scopus 로고    scopus 로고
    • A lysosomal population responsible for the hsc73-mediated degradation of cytosolic proteins in lysosomes
    • Cuervo A., Dice J., and Knecht E. A lysosomal population responsible for the hsc73-mediated degradation of cytosolic proteins in lysosomes. J. Biol. Chem. 272 (1997) 5606-5615
    • (1997) J. Biol. Chem. , vol.272 , pp. 5606-5615
    • Cuervo, A.1    Dice, J.2    Knecht, E.3
  • 11
    • 0032938776 scopus 로고    scopus 로고
    • Direct lysosomal uptake of alpha2-microglobulin contributes to chemically induced nephropathy
    • Cuervo A., Hildebrand H., Bomhard E., and Dice J. Direct lysosomal uptake of alpha2-microglobulin contributes to chemically induced nephropathy. Kidney Int. 55 (1999) 529-545
    • (1999) Kidney Int. , vol.55 , pp. 529-545
    • Cuervo, A.1    Hildebrand, H.2    Bomhard, E.3    Dice, J.4
  • 12
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • Cuervo A., Knecht E., Terlecky S., and Dice J. Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am. J. Physiol. 269 (1995) C1200-C1208
    • (1995) Am. J. Physiol. , vol.269
    • Cuervo, A.1    Knecht, E.2    Terlecky, S.3    Dice, J.4
  • 13
    • 0037413688 scopus 로고    scopus 로고
    • Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor
    • Cuervo A., Mann L., Bonten E., d'Azzo A., and Dice J. Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor. EMBO J. 22 (2003) 12-19
    • (2003) EMBO J. , vol.22 , pp. 12-19
    • Cuervo, A.1    Mann, L.2    Bonten, E.3    d'Azzo, A.4    Dice, J.5
  • 14
    • 0020405985 scopus 로고
    • Altered degradation of proteins microinjected into senescent human fibroblasts
    • Dice J. Altered degradation of proteins microinjected into senescent human fibroblasts. J. Biol. Chem. 257 (1982) 14624-14627
    • (1982) J. Biol. Chem. , vol.257 , pp. 14624-14627
    • Dice, J.1
  • 15
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice J. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem. Sci. 15 (1990) 305-309
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 305-309
    • Dice, J.1
  • 16
    • 21844440290 scopus 로고    scopus 로고
    • Ketone bodies stimulate chaperone-mediated autophagy
    • Finn P.F., and Dice J.F. Ketone bodies stimulate chaperone-mediated autophagy. J. Biol. Chem. 280 (2005) 25864-25870
    • (2005) J. Biol. Chem. , vol.280 , pp. 25864-25870
    • Finn, P.F.1    Dice, J.F.2
  • 17
    • 3543041226 scopus 로고    scopus 로고
    • Molecular wear and tear leads to terminal marking and the unstable isoforms of aging
    • Gracy R., Talent J., and Zvaigzne A. Molecular wear and tear leads to terminal marking and the unstable isoforms of aging. J. Exp. Zool. 282 (1998) 18-27
    • (1998) J. Exp. Zool. , vol.282 , pp. 18-27
    • Gracy, R.1    Talent, J.2    Zvaigzne, A.3
  • 18
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T., Merker K., Sandig G., and Davies K.J. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem. Biophys. Res. Commun. 305 (2003) 709-718
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 19
    • 0015046403 scopus 로고
    • Lysosomes, membranes and aging
    • Hochshild R. Lysosomes, membranes and aging. Exp. Gerontol. 6 (1970) 153-166
    • (1970) Exp. Gerontol. , vol.6 , pp. 153-166
    • Hochshild, R.1
  • 20
    • 33748374920 scopus 로고    scopus 로고
    • Kaushik, S., Massey, A.C., Cuervo, A.M., 2006. Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy. EMBO J. [E-pub ahead of printing].
  • 22
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • Kiffin R., Christian C., Knecht E., and Cuervo A. Activation of chaperone-mediated autophagy during oxidative stress. Mol. Biol. Cell 15 (2004) 4829-4840
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.4
  • 23
    • 4344673498 scopus 로고    scopus 로고
    • Mechanisms of chaperone-mediated autophagy
    • Majeski A., and Dice J. Mechanisms of chaperone-mediated autophagy. Int. J. Biochem. Cell Biol. 36 (2004) 2435-2444
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2435-2444
    • Majeski, A.1    Dice, J.2
  • 26
    • 27644493346 scopus 로고    scopus 로고
    • The pleiotropic role of autophagy: from protein metabolism to bactericide
    • Mizushima N. The pleiotropic role of autophagy: from protein metabolism to bactericide. Cell Death Diff. 12 (2005) 1535-1541
    • (2005) Cell Death Diff. , vol.12 , pp. 1535-1541
    • Mizushima, N.1
  • 27
    • 0018826889 scopus 로고
    • Ultrastructural study of granular cell ameloblastoma
    • Noda M., and Suzuki A. Ultrastructural study of granular cell ameloblastoma. Acta Pathol. Japonica 30 (1980) 145-156
    • (1980) Acta Pathol. Japonica , vol.30 , pp. 145-156
    • Noda, M.1    Suzuki, A.2
  • 28
  • 29
    • 0034282931 scopus 로고    scopus 로고
    • Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state
    • Salvador N., Aguado C., Horst M., and Knecht E. Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J. Biol. Chem. 275 (2000) 27447-27456
    • (2000) J. Biol. Chem. , vol.275 , pp. 27447-27456
    • Salvador, N.1    Aguado, C.2    Horst, M.3    Knecht, E.4
  • 30
    • 0034798361 scopus 로고    scopus 로고
    • Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells
    • Shringarpure R., Grune T., and Davies K. Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells. Cell Mol. Life Sci. 58 (2001) 1442-1450
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1442-1450
    • Shringarpure, R.1    Grune, T.2    Davies, K.3
  • 33
    • 0035607509 scopus 로고    scopus 로고
    • The influence of oxidation of membrane thiol groups on lysosomal proton permeability
    • Wan F., Wang Y.N., et al. The influence of oxidation of membrane thiol groups on lysosomal proton permeability. Biochem. J. 360 (2001) 355-362
    • (2001) Biochem. J. , vol.360 , pp. 355-362
    • Wan, F.1    Wang, Y.N.2
  • 34
    • 0025801067 scopus 로고
    • Proteins containing peptide sequences related to KFERQ are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats
    • Wing S., Chiang H.L., Goldberg A.L., and Dice J.F. Proteins containing peptide sequences related to KFERQ are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats. Biochem. J. 275 (1991) 165-169
    • (1991) Biochem. J. , vol.275 , pp. 165-169
    • Wing, S.1    Chiang, H.L.2    Goldberg, A.L.3    Dice, J.F.4
  • 35
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: molecular machinery for self-eating
    • Yorimitsu T., and Klionsky D. Autophagy: molecular machinery for self-eating. Cell Death Diff. 12 Suppl 2 (2005) 1542-1552
    • (2005) Cell Death Diff. , vol.12 , Issue.SUPPL. 2 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.