메뉴 건너뛰기




Volumn 25, Issue 3, 2000, Pages 95-98

Clusterin is a secreted mammalian chaperone

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CLUSTERIN; GLYCOPROTEIN; HEAT SHOCK PROTEIN;

EID: 0034161616     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(99)01534-0     Document Type: Short Survey
Times cited : (334)

References (41)
  • 1
    • 0020601062 scopus 로고
    • Purification and characterization of a cell-aggregating factor (clusterin), the major glycoprotein in ram rete testis fluid
    • Blaschuk O.et al. Purification and characterization of a cell-aggregating factor (clusterin), the major glycoprotein in ram rete testis fluid. J. Biol. Chem. 258:1983;7714-7720.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7714-7720
    • Blaschuk, O.1
  • 2
    • 0026600180 scopus 로고
    • Clusterin: The intriguing guises of a widely expressed glycoprotein
    • Jenne D.E., Tschopp J. Clusterin: the intriguing guises of a widely expressed glycoprotein. Trends Biochem. Sci. 17:1992;154-159.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 154-159
    • Jenne, D.E.1    Tschopp, J.2
  • 3
    • 0025301469 scopus 로고
    • Apolipoprotein J: Structure and tissue distribution
    • de Silva H.V.et al. Apolipoprotein J: structure and tissue distribution. Biochemistry. 29:1990;5380-5389.
    • (1990) Biochemistry , vol.29 , pp. 5380-5389
    • De Silva, H.V.1
  • 4
    • 0026356891 scopus 로고
    • Predicting coiled-coils from protein sequences
    • Lupas A. Predicting coiled-coils from protein sequences. Science. 252:1991;1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1
  • 5
    • 0028321386 scopus 로고
    • Clusterin expression in differentiating smooth muscle cells
    • Thomas-Salgar S., Millis A.J.T. Clusterin expression in differentiating smooth muscle cells. J. Biol. Chem. 269:1994;17879-17885.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17879-17885
    • Thomas-Salgar, S.1    Millis, A.J.T.2
  • 6
    • 0022627063 scopus 로고
    • Androgen-repressed messages in the rat ventral prostate
    • Montpetit M.L.et al. Androgen-repressed messages in the rat ventral prostate. Prostate. 8:1986;25-36.
    • (1986) Prostate , vol.8 , pp. 25-36
    • Montpetit, M.L.1
  • 7
    • 0026569141 scopus 로고
    • Apolipoprotein J: A membrane policeman?
    • Jordan-Starck T.C.et al. Apolipoprotein J: a membrane policeman? Curr. Opin. Lipidol. 3:1992;75-85.
    • (1992) Curr. Opin. Lipidol. , vol.3 , pp. 75-85
    • Jordan-Starck, T.C.1
  • 8
    • 0026768786 scopus 로고
    • Hepatic apolipoprotein J is secreted as a lipoprotein
    • Burkey B.F.et al. Hepatic apolipoprotein J is secreted as a lipoprotein. J. Lipid Res. 33:1992;1517-1526.
    • (1992) J. Lipid Res. , vol.33 , pp. 1517-1526
    • Burkey, B.F.1
  • 9
    • 0032055127 scopus 로고    scopus 로고
    • Apolipoprotein J (clusterin) induces cholesterol export from macrophage-foam cells: A potential anti-atherogenic function
    • Gelissen I.C.et al. Apolipoprotein J (clusterin) induces cholesterol export from macrophage-foam cells: a potential anti-atherogenic function. Biochem. J. 331:1998;231-237.
    • (1998) Biochem. J. , vol.331 , pp. 231-237
    • Gelissen, I.C.1
  • 10
    • 0033602717 scopus 로고    scopus 로고
    • A re-examination of the role of clusterin as a complement regulator
    • Hochgrebe T.T.et al. A re-examination of the role of clusterin as a complement regulator. Exp. Cell Res. 249:1999;13-21.
    • (1999) Exp. Cell Res. , vol.249 , pp. 13-21
    • Hochgrebe, T.T.1
  • 11
    • 0025910082 scopus 로고
    • Clusterin (complement lysis inhibitor) forms a high density lipoprotein complex with apolipoprotein A-I in human plasma
    • Jenne D.E.et al. Clusterin (complement lysis inhibitor) forms a high density lipoprotein complex with apolipoprotein A-I in human plasma. J. Biol. Chem. 266:1991;11030-11036.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11030-11036
    • Jenne, D.E.1
  • 12
    • 0027186334 scopus 로고
    • The cerebrospinal-fluid soluble form of Alzheimers amyloid-beta is complexed to SP-40,40 (apolipoprotein-J), an inhibitor of the complement membrane-attack complex
    • Ghiso J.et al. The cerebrospinal-fluid soluble form of Alzheimers amyloid-beta is complexed to SP-40,40 (apolipoprotein-J), an inhibitor of the complement membrane-attack complex. Biochem. J. 293:1993;27-30.
    • (1993) Biochem. J. , vol.293 , pp. 27-30
    • Ghiso, J.1
  • 13
    • 0027164921 scopus 로고
    • Clusterin, the human apolipoprotein and complement inhibitor, binds to complement C7, C8β, and the β domain of C9
    • Tschopp J.et al. Clusterin, the human apolipoprotein and complement inhibitor, binds to complement C7, C8β, and the β domain of C9. J. Immunol. 151:1993;2159-2165.
    • (1993) J. Immunol. , vol.151 , pp. 2159-2165
    • Tschopp, J.1
  • 14
    • 0033548566 scopus 로고    scopus 로고
    • Clusterin has chaperone-like activity similar to that of small heat-shock proteins
    • Humphreys D.et al. Clusterin has chaperone-like activity similar to that of small heat-shock proteins. J. Biol. Chem. 274:1999;6875-6881.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6875-6881
    • Humphreys, D.1
  • 15
    • 0029018581 scopus 로고
    • Identification of glycoprotein 330 as an endocytic receptor for apolipoprotein J/clusterin
    • Kounnas M.Z.et al. Identification of glycoprotein 330 as an endocytic receptor for apolipoprotein J/clusterin. J. Biol. Chem. 270:1995;13070-13075.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13070-13075
    • Kounnas, M.Z.1
  • 16
    • 0030753654 scopus 로고    scopus 로고
    • Interaction of apolipoprotein J-amyloid beta-peptide complex with low density lipoprotein receptor-related protein-2 megalin - A mechanism to prevent pathological accumulation of amyloid beta-peptide
    • Hammad S.M.et al. Interaction of apolipoprotein J-amyloid beta-peptide complex with low density lipoprotein receptor-related protein-2 megalin - a mechanism to prevent pathological accumulation of amyloid beta-peptide. J. Biol. Chem. 272:1997;18644-18649.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18644-18649
    • Hammad, S.M.1
  • 17
    • 0032492680 scopus 로고    scopus 로고
    • Characterization of the heparin-binding properties of human clusterin
    • Pankhurst G.J.et al. Characterization of the heparin-binding properties of human clusterin. Biochemistry. 37:1998;4823-4830.
    • (1998) Biochemistry , vol.37 , pp. 4823-4830
    • Pankhurst, G.J.1
  • 18
    • 0026739326 scopus 로고
    • Clusterin binds by a multivalent mechanism to the Fc and Fab regions of IgG
    • Wilson M.R., Easterbrook-Smith S.B. Clusterin binds by a multivalent mechanism to the Fc and Fab regions of IgG. Biochim. Biophys. Acta. 1159:1992;319-326.
    • (1992) Biochim. Biophys. Acta , vol.1159 , pp. 319-326
    • Wilson, M.R.1    Easterbrook-Smith, S.B.2
  • 19
    • 0028107410 scopus 로고
    • Apolipoprotein-J is associated with paraoxonase in human plasma
    • Kelso G.J.et al. Apolipoprotein-J is associated with paraoxonase in human plasma. Biochemistry. 33:1994;832-839.
    • (1994) Biochemistry , vol.33 , pp. 832-839
    • Kelso, G.J.1
  • 20
    • 0033532581 scopus 로고    scopus 로고
    • Clusterin prevents aggregation of neuropeptide 106-126 in vitro
    • McHattie S., Edington N. Clusterin prevents aggregation of neuropeptide 106-126 in vitro. Biochem. Biophys. Res. Commun. 259:1999;336-340.
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 336-340
    • McHattie, S.1    Edington, N.2
  • 21
    • 0030067110 scopus 로고    scopus 로고
    • Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function
    • Akesson P.et al. Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function. J. Biol. Chem. 271:1996;1081-1088.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1081-1088
    • Akesson, P.1
  • 22
    • 0029845259 scopus 로고    scopus 로고
    • Clusterin, a putative complement regulator, binds to the cell surface of Staphylococcus aureus isolates
    • Partridge S.R.et al. Clusterin, a putative complement regulator, binds to the cell surface of Staphylococcus aureus isolates. Infect. Immunol. 64:1996;4324-4329.
    • (1996) Infect. Immunol. , vol.64 , pp. 4324-4329
    • Partridge, S.R.1
  • 23
    • 0030026569 scopus 로고    scopus 로고
    • Interaction of transforming growth factor beta receptors with apolipoprotein J/clusterin
    • Reddy K.B.et al. Interaction of transforming growth factor beta receptors with apolipoprotein J/clusterin. Biochemistry. 35:1996;309-314.
    • (1996) Biochemistry , vol.35 , pp. 309-314
    • Reddy, K.B.1
  • 24
    • 0030664673 scopus 로고    scopus 로고
    • Stress-induced transcription of the clusterin/ApoJ gene
    • Michel D.et al. Stress-induced transcription of the clusterin/ApoJ gene. Biochem. J. 328:1997;45-50.
    • (1997) Biochem. J. , vol.328 , pp. 45-50
    • Michel, D.1
  • 26
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veigner L.et al. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273:1998;11032-11037.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11032-11037
    • Veigner, L.1
  • 27
    • 0033602929 scopus 로고    scopus 로고
    • Clusterin in the male reproductive system: Localization and possible function
    • Bailey R., Griswold M.D. Clusterin in the male reproductive system: localization and possible function. Mol. Cell Endocrinol. 151:1999;17-23.
    • (1999) Mol. Cell Endocrinol. , vol.151 , pp. 17-23
    • Bailey, R.1    Griswold, M.D.2
  • 28
    • 0028988412 scopus 로고
    • Interaction of alpha-crystallin with spin-labelled peptides
    • Farahbakhsh Z.T.et al. Interaction of alpha-crystallin with spin-labelled peptides. Biochemistry. 43:1995;509-516.
    • (1995) Biochemistry , vol.43 , pp. 509-516
    • Farahbakhsh, Z.T.1
  • 29
    • 0029061350 scopus 로고
    • Prevention of cell death induced by tumor necrosis factor alpha in LNCaP cells by overexpression of sulfated glycoprotein-2 (clusterin)
    • Sensibar J.A.et al. Prevention of cell death induced by tumor necrosis factor alpha in LNCaP cells by overexpression of sulfated glycoprotein-2 (clusterin). Cancer Res. 55:1995;2431-2437.
    • (1995) Cancer Res. , vol.55 , pp. 2431-2437
    • Sensibar, J.A.1
  • 30
    • 0030660559 scopus 로고    scopus 로고
    • Effects of clusterin overexpression on TNFα- And TGFβ-mediated death of L929 cells
    • Humphreys D.et al. Effects of clusterin overexpression on TNFα- and TGFβ-mediated death of L929 cells. Biochemistry. 36:1997;15233-15243.
    • (1997) Biochemistry , vol.36 , pp. 15233-15243
    • Humphreys, D.1
  • 31
    • 0028210028 scopus 로고
    • Human clusterin gene expression is confined to surviving cells during in vitro programmed cell death
    • French L.E.et al. Human clusterin gene expression is confined to surviving cells during in vitro programmed cell death. J. Clin. Invest. 93:1994;877-884.
    • (1994) J. Clin. Invest. , vol.93 , pp. 877-884
    • French, L.E.1
  • 32
    • 0032979467 scopus 로고    scopus 로고
    • Clusterin gene expression mediates resistance to apoptotic cell death induced by heat shock and oxidative stress
    • Viard I.et al. Clusterin gene expression mediates resistance to apoptotic cell death induced by heat shock and oxidative stress. J. Invest. Dermatol. 112:1999;290-296.
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 290-296
    • Viard, I.1
  • 33
    • 0031748528 scopus 로고    scopus 로고
    • Clusterin protects against oxidative stress in vitro through aggregative and nonaggregative properties
    • Schwochau G.B.et al. Clusterin protects against oxidative stress in vitro through aggregative and nonaggregative properties. Kidney Int. 53:1998;1647-1653.
    • (1998) Kidney Int. , vol.53 , pp. 1647-1653
    • Schwochau, G.B.1
  • 34
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:1988;10881-10890.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 35
    • 0031561418 scopus 로고    scopus 로고
    • Functional elements in molecular chaperone αb-crystallin: Identification of binding sites in αb-crystallin
    • Sharma K.K.et al. Functional elements in molecular chaperone αB-crystallin: identification of binding sites in αB-crystallin. Biochem. Biophys. Res. Commun. 239:1997;217-222.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 217-222
    • Sharma, K.K.1
  • 36
    • 0032546801 scopus 로고    scopus 로고
    • Identification of 1,1′-bi(4-anilino)naphthalene-5,5′-disulfonic acid binding sequences in αb-crystallin
    • Sharma K.K.et al. Identification of 1,1′-bi(4-anilino)naphthalene-5,5′-disulfonic acid binding sequences in αB-crystallin. J. Biol. Chem. 273:1998;15474-15478.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15474-15478
    • Sharma, K.K.1
  • 37
    • 0029871768 scopus 로고    scopus 로고
    • Transforming growth factor β (TGF β)-induced nuclear localization of apolipoprotein J/clusterin in epithelial cells
    • Reddy K.B.et al. Transforming growth factor β (TGF β)-induced nuclear localization of apolipoprotein J/clusterin in epithelial cells. Biochemistry. 35:1996;6157-6163.
    • (1996) Biochemistry , vol.35 , pp. 6157-6163
    • Reddy, K.B.1
  • 38
    • 0344848800 scopus 로고    scopus 로고
    • Isolation of Ku70-binding proteins (KUBs)
    • Yang C.R.et al. Isolation of Ku70-binding proteins (KUBs). Nucleic Acids Res. 27:1999;2165-2174.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2165-2174
    • Yang, C.R.1
  • 39
    • 0033548184 scopus 로고    scopus 로고
    • Multiple involvement of clusterin in chicken ovarian follicle development - binding to two oocyte-specific members of the low density lipoprotein receptor gene family
    • Mahon M.G.et al. Multiple involvement of clusterin in chicken ovarian follicle development - binding to two oocyte-specific members of the low density lipoprotein receptor gene family. J. Biol. Chem. 274:1999;4036-4044.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4036-4044
    • Mahon, M.G.1
  • 40
    • 0027321292 scopus 로고
    • A seed protein induced by heat treatment in soybean
    • Kagawa H.et al. A seed protein induced by heat treatment in soybean. Food Chem. 48:1993;159-163.
    • (1993) Food Chem. , vol.48 , pp. 159-163
    • Kagawa, H.1
  • 41
    • 0031064365 scopus 로고    scopus 로고
    • Secretory heat-shock protein of the thermotolerant yeast Hansenula polymorpha. Identification and comparative characteristics
    • Tsiomenko A.B.et al. Secretory heat-shock protein of the thermotolerant yeast Hansenula polymorpha. Identification and comparative characteristics. Biochemistry (Moscow). 62:1997;123-128.
    • (1997) Biochemistry (Moscow) , vol.62 , pp. 123-128
    • Tsiomenko, A.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.