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Volumn 39, Issue 6, 2008, Pages 571-578

Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions

Author keywords

Actin; Hsc70; Hsp70; Mesoangioblast cells

Indexed keywords

F ACTIN; HEAT SHOCK PROTEIN 70;

EID: 56349090843     PISSN: 15672379     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10735-008-9197-7     Document Type: Article
Times cited : (10)

References (39)
  • 1
    • 1642407667 scopus 로고    scopus 로고
    • Unique gene expression signatures of independently-derived human embryonic stem cell lines
    • 10.1093/hmg/ddh068
    • MJ Abeyta AT Clark RT Rodriguez 2004 Unique gene expression signatures of independently-derived human embryonic stem cell lines Hum Mol Genet 13 601 608 10.1093/hmg/ddh068
    • (2004) Hum Mol Genet , vol.13 , pp. 601-608
    • Abeyta, M.J.1    Clark, A.T.2    Rodriguez, R.T.3
  • 2
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
    • 10.1016/S0962-8924(96)10056-8
    • P Ahsen 1997 Molecular chaperones: towards a characterization of the heat-shock protein 70 family Trends Cell Biol 7 129 133 10.1016/S0962-8924(96) 10056-8
    • (1997) Trends Cell Biol , vol.7 , pp. 129-133
    • Ahsen, P.1
  • 3
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • 10.1038/74697
    • A Asea SK Kraeft EA Kurt-Jones 2000 HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine Nat Med 6 435 442 10.1038/74697
    • (2000) Nat Med , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3
  • 4
    • 0029315783 scopus 로고
    • Presence of the stress-inducible form of hsp-70 (hsp-72) in normal rat colon
    • 10.1097/00024382-199506000-00003
    • SC Beck CN Paidas ML Mooney 1995 Presence of the stress-inducible form of hsp-70 (hsp-72) in normal rat colon Shock 3 398 402 10.1097/00024382-199506000- 00003
    • (1995) Shock , vol.3 , pp. 398-402
    • Beck, S.C.1    Paidas, C.N.2    Mooney, M.L.3
  • 5
    • 11144355188 scopus 로고    scopus 로고
    • Gene expression in human embryonic stem cell lines: Unique molecular signature
    • 10.1182/blood-2003-09-3314
    • B Bhattacharya T Miura R Brandenberger 2004 Gene expression in human embryonic stem cell lines: unique molecular signature Blood 103 2956 2964 10.1182/blood-2003-09-3314
    • (2004) Blood , vol.103 , pp. 2956-2964
    • Bhattacharya, B.1    Miura, T.2    Brandenberger, R.3
  • 6
    • 0028328366 scopus 로고
    • Transient increase in vimentin phosphorylation and vimentin-HSC70 association in 9L rat brain tumor cells experiencing heat-shock
    • 10.1002/jcb.240540111
    • TJ Cheng YK Lai 1994 Transient increase in vimentin phosphorylation and vimentin-HSC70 association in 9L rat brain tumor cells experiencing heat-shock J Cell Biochem 54 100 109 10.1002/jcb.240540111
    • (1994) J Cell Biochem , vol.54 , pp. 100-109
    • Cheng, T.J.1    Lai, Y.K.2
  • 7
    • 0031692606 scopus 로고    scopus 로고
    • Constitutive expression of heat shock proteins Hsp90, Hsc70, Hsp70 and Hsp60 in neural and non-neural tissues of the rat during postnatal development
    • doi:10.1379/1466-1268(1998)003<0188:CEOHSP>2.3.CO;2
    • D'Souza SM, Brown IR (1998) Constitutive expression of heat shock proteins Hsp90, Hsc70, Hsp70 and Hsp60 in neural and non-neural tissues of the rat during postnatal development. Cell Stress Chaperones 3:188-199. doi:10.1379/1466-1268(1998)003<0188:CEOHSP>2.3.CO;2
    • (1998) Cell Stress Chaperones , vol.3 , pp. 188-199
    • D'Souza, S.M.1    Brown, I.R.2
  • 8
    • 33745200953 scopus 로고    scopus 로고
    • Stress response in mesoangioblast stem cells
    • 10.1038/sj.cdd.4401794
    • F Geraci G Turturici D Galli 2006 Stress response in mesoangioblast stem cells Cell Death Differ 13 1057 1063 10.1038/sj.cdd.4401794
    • (2006) Cell Death Differ , vol.13 , pp. 1057-1063
    • Geraci, F.1    Turturici, G.2    Galli, D.3
  • 9
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • 10.1016/0092-8674(95)90444-1
    • BS Glick 1995 Can Hsp70 proteins act as force-generating motors? Cell 80 11 14 10.1016/0092-8674(95)90444-1
    • (1995) Cell , vol.80 , pp. 11-14
    • Glick, B.S.1
  • 10
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance
    • 10.1016/S0006-8993(01)02774-3
    • I Guzhova K Kislyakova O Moskaliova 2001 In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance Brain Res 914 66 73 10.1016/S0006-8993(01)02774-3
    • (2001) Brain Res , vol.914 , pp. 66-73
    • Guzhova, I.1    Kislyakova, K.2    Moskaliova, O.3
  • 11
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • 10.1038/381571a0
    • FU Hartl 1996 Molecular chaperones in cellular protein folding Nature 381 571 579 10.1038/381571a0
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 12
    • 0024541931 scopus 로고
    • Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins
    • 10.1002/jcp.1041380206
    • LE Hightower PT Guidon Jr 1989 Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins J Cell Physiol 138 257 266 10.1002/jcp.1041380206
    • (1989) J Cell Physiol , vol.138 , pp. 257-266
    • Hightower, L.E.1    Guidon Jr., P.T.2
  • 13
    • 33646010643 scopus 로고    scopus 로고
    • Chaperones in preventing protein denaturation in living cells and protecting against cellular stress
    • 10.1007/3-540-29717-0_1
    • HH Kampinga 2006 Chaperones in preventing protein denaturation in living cells and protecting against cellular stress Handb Exp Pharmacol 172 1 42 10.1007/3-540-29717-0_1
    • (2006) Handb Exp Pharmacol , vol.172 , pp. 1-42
    • Kampinga, H.H.1
  • 14
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology
    • 10.1016/S0163-7258(98)00028-X
    • JG Kiang GC Tsokos 1998 Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology Pharmacol Ther 80 183 201 10.1016/S0163-7258(98) 00028-X
    • (1998) Pharmacol Ther , vol.80 , pp. 183-201
    • Kiang, J.G.1    Tsokos, G.C.2
  • 15
    • 0035145955 scopus 로고    scopus 로고
    • Mutation of amino acids 566-572 (KKKVLDK) inhibits nuclear accumulation of heat shock protein 72 after heat shock
    • 10.1006/jmcc.2000.1274
    • AA Knowlton 2001 Mutation of amino acids 566-572 (KKKVLDK) inhibits nuclear accumulation of heat shock protein 72 after heat shock J Mol Cell Cardiol 33 49 55 10.1006/jmcc.2000.1274
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 49-55
    • Knowlton, A.A.1
  • 16
    • 0032837150 scopus 로고    scopus 로고
    • Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein
    • doi:10.1379/1466-1268(1999)004<0139:ULOHEW>2.3.CO;2
    • Kurucz I, Tombor B, Prechl J, et al (1999) Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein. Cell Stress Chaperones 4:139-152. doi:10.1379/1466-1268(1999)004<0139:ULOHEW>2.3.CO;2
    • (1999) Cell Stress Chaperones , vol.4 , pp. 139-152
    • Kurucz, I.1    Tombor, B.2    Prechl, J.3
  • 17
    • 0346728756 scopus 로고    scopus 로고
    • Indomethacin and ibuprofen induce Hsc70 nuclear localization and activation of the heat shock response in HeLa cells
    • 10.1016/j.bbrc.2003.12.018
    • L Lagunas CM Bradbury A Laszlo 2004 Indomethacin and ibuprofen induce Hsc70 nuclear localization and activation of the heat shock response in HeLa cells Biochem Biophys Res Commun 313 863 870 10.1016/j.bbrc.2003.12.018
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 863-870
    • Lagunas, L.1    Bradbury, C.M.2    Laszlo, A.3
  • 18
    • 0021471730 scopus 로고
    • A major heat-shock protein defined by a monoclonal antibody
    • NB La Thangue 1984 A major heat-shock protein defined by a monoclonal antibody EMBO J 3 1871 1879
    • (1984) EMBO J , vol.3 , pp. 1871-1879
    • La Thangue, N.B.1
  • 19
    • 20744436655 scopus 로고    scopus 로고
    • Exosome-dependent trafficking of HSP70: A novel secretory pathway for cellular stress proteins
    • 10.1074/jbc.M502017200
    • GI Lancaster MA Febbraio 2005 Exosome-dependent trafficking of HSP70: a novel secretory pathway for cellular stress proteins J Biol Chem 280 23349 23355 10.1074/jbc.M502017200
    • (2005) J Biol Chem , vol.280 , pp. 23349-23355
    • Lancaster, G.I.1    Febbraio, M.A.2
  • 20
    • 0025917038 scopus 로고
    • Isolation of hsp70-binding proteins from bovine muscle
    • 10.1016/0006-291X(91)91771-4
    • BA Margulis M Welsh 1991 Isolation of hsp70-binding proteins from bovine muscle Biochem Biophys Res Commun 178 1 7 10.1016/0006-291X(91)91771-4
    • (1991) Biochem Biophys Res Commun , vol.178 , pp. 1-7
    • Margulis, B.A.1    Welsh, M.2
  • 21
    • 0025822789 scopus 로고
    • Analysis of protein binding to heat shock protein 70 in pancreatic islet cells exposed to elevated temperatures or interleukin 1 beta
    • BA Margulis M Welsh 1991 Analysis of protein binding to heat shock protein 70 in pancreatic islet cells exposed to elevated temperatures or interleukin 1 beta J Biol Chem 266 9295 9298
    • (1991) J Biol Chem , vol.266 , pp. 9295-9298
    • Margulis, B.A.1    Welsh, M.2
  • 22
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • 10.1007/s00018-004-4464-6
    • MP Mayer B Bukau 2005 Hsp70 chaperones: cellular functions and molecular mechanism Cell Mol Life Sci 62 670 684 10.1007/s00018-004-4464-6
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 23
    • 0032213716 scopus 로고    scopus 로고
    • Comparison of seven quantitative assays to assess lymphocytic cell death during HIV infection: Measurement of induced apoptosis in anti-Fas treated Jurkat cells and spontaneous apoptosis in peripheral blood mononuclear cells from children infected with HIV
    • TW McClowskey S Chavan Lakshmi Tamma 1998 Comparison of seven quantitative assays to assess lymphocytic cell death during HIV infection: measurement of induced apoptosis in anti-Fas treated Jurkat cells and spontaneous apoptosis in peripheral blood mononuclear cells from children infected with HIV AIDS Res Hum Retroviruses 14 1413 1422
    • (1998) AIDS Res Hum Retroviruses , vol.14 , pp. 1413-1422
    • McClowskey, T.W.1    Chavan, S.2    Lakshmi, T.3
  • 24
    • 0024587611 scopus 로고
    • Cell cycle-dependent association of HSP70 with specific cellular proteins
    • 10.1083/jcb.108.2.413
    • KL Milarski WJ Welch RI Morimoto 1989 Cell cycle-dependent association of HSP70 with specific cellular proteins J Cell Biol 108 413 423 10.1083/jcb.108.2.413
    • (1989) J Cell Biol , vol.108 , pp. 413-423
    • Milarski, K.L.1    Welch, W.J.2    Morimoto, R.I.3
  • 25
    • 0036333788 scopus 로고    scopus 로고
    • The meso-angioblast: A multipotent, self-renewing cell that originates from the dorsal aorta and differentiates into most mesodermal tissues
    • MG Minasi M Riminucci L De Angelis 2002 The meso-angioblast: a multipotent, self-renewing cell that originates from the dorsal aorta and differentiates into most mesodermal tissues Development 129 2773 2783
    • (2002) Development , vol.129 , pp. 2773-2783
    • Minasi, M.G.1    Riminucci, M.2    De Angelis, L.3
  • 26
    • 0028867215 scopus 로고
    • Analysis by confocal microscopy of the behaviour of heat shock protein 70 within the nucleus and of a nuclear matrix polypeptide during prolonged heat shock response in HeLa cells
    • 10.1006/excr.1995.1379
    • LM Neri BM Riederer RA Marugg 1995 Analysis by confocal microscopy of the behaviour of heat shock protein 70 within the nucleus and of a nuclear matrix polypeptide during prolonged heat shock response in HeLa cells Exp Cell Res 221 301 310 10.1006/excr.1995.1379
    • (1995) Exp Cell Res , vol.221 , pp. 301-310
    • Neri, L.M.1    Riederer, B.M.2    Marugg, R.A.3
  • 27
    • 0035834122 scopus 로고    scopus 로고
    • Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection
    • 10.1073/pnas.201112398
    • EA Nollen FA Salomons JF Brunsting 2001 Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection Proc Natl Acad Sci USA 98 12038 12043 10.1073/pnas.201112398
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12038-12043
    • Nollen, E.A.1    Salomons, F.A.2    Brunsting, J.F.3
  • 28
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • 10.1016/S1047-8477(02)00528-2
    • T Pederson U Aebi 2002 Actin in the nucleus: what form and what for? J Struct Biol 140 3 9 10.1016/S1047-8477(02)00528-2
    • (2002) J Struct Biol , vol.140 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 29
    • 27644486139 scopus 로고    scopus 로고
    • Actin cytoskeleton is involved in targeting of a viral Hsp70 homolog to the cell periphery
    • 10.1128/JVI.79.22.14421-14428.2005
    • AI Prokhnevsky VV Peremyslov VV Dolja 2005 Actin cytoskeleton is involved in targeting of a viral Hsp70 homolog to the cell periphery J Virol 79 14421 14428 10.1128/JVI.79.22.14421-14428.2005
    • (2005) J Virol , vol.79 , pp. 14421-14428
    • Prokhnevsky, A.I.1    Peremyslov, V.V.2    Dolja, V.V.3
  • 30
    • 13444251596 scopus 로고    scopus 로고
    • Is hypothermia a stress condition in HepG2 cells? Expression and localization of Hsp70 in human hepatoma cell line
    • 10.1016/j.tice.2004.10.003
    • A Rada P Tonino G Anselmi 2005 Is hypothermia a stress condition in HepG2 cells? Expression and localization of Hsp70 in human hepatoma cell line Tissue Cell 37 59 65 10.1016/j.tice.2004.10.003
    • (2005) Tissue Cell , vol.37 , pp. 59-65
    • Rada, A.1    Tonino, P.2    Anselmi, G.3
  • 31
    • 0028965273 scopus 로고
    • Partner proteins determine multiple functions of Hsp70
    • 10.1016/S0962-8924(00)89001-7
    • J Rassow W Voos N Pfanner 1995 Partner proteins determine multiple functions of Hsp70 Trends Cell Biol 5 207 212 10.1016/S0962-8924(00)89001-7
    • (1995) Trends Cell Biol , vol.5 , pp. 207-212
    • Rassow, J.1    Voos, W.2    Pfanner, N.3
  • 32
    • 23344453615 scopus 로고    scopus 로고
    • Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues
    • 10.1080/02656730500041921
    • M Tytell 2005 Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues Int J Hyperthermia 21 445 455 10.1080/02656730500041921
    • (2005) Int J Hyperthermia , vol.21 , pp. 445-455
    • Tytell, M.1
  • 33
    • 0000360089 scopus 로고    scopus 로고
    • Heat shock proteins: New keys to the development of cytoprotective therapies
    • 10.1517/14728222.5.2.267
    • M Tytell PL Hooper 2001 Heat shock proteins: new keys to the development of cytoprotective therapies Expert Opin Ther Targets 5 267 287 10.1517/14728222.5.2.267
    • (2001) Expert Opin Ther Targets , vol.5 , pp. 267-287
    • Tytell, M.1    Hooper, P.L.2
  • 34
    • 0022637881 scopus 로고
    • Heat shock-like protein is transferred from glia to axon
    • 10.1016/0006-8993(86)90671-2
    • M Tytell SG Greenberg RJ Lasek 1986 Heat shock-like protein is transferred from glia to axon Brain Res 363 161 164 10.1016/0006-8993(86)90671-2
    • (1986) Brain Res , vol.363 , pp. 161-164
    • Tytell, M.1    Greenberg, S.G.2    Lasek, R.J.3
  • 35
    • 0021398211 scopus 로고
    • Hsp70: Nuclear concentration during environmental stress and cytoplasmic storage during recovery
    • 10.1016/0092-8674(84)90345-3
    • JM Velazquez S Lindquist 1984 Hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery Cell 36 655 662 10.1016/0092-8674(84)90345-3
    • (1984) Cell , vol.36 , pp. 655-662
    • Velazquez, J.M.1    Lindquist, S.2
  • 36
    • 0031860326 scopus 로고    scopus 로고
    • Concomitant alterations in distribution of 70 kDa heat shock proteins, cytoskeleton and organelles in heat shocked 9L cells
    • 10.1016/S1357-2725(97)00133-7
    • TT Wang AS Chiang JJ Chu 1998 Concomitant alterations in distribution of 70 kDa heat shock proteins, cytoskeleton and organelles in heat shocked 9L cells Int J Biochem Cell Biol 30 745 759 10.1016/S1357-2725(97)00133-7
    • (1998) Int J Biochem Cell Biol , vol.30 , pp. 745-759
    • Wang, T.T.1    Chiang, A.S.2    Chu, J.J.3
  • 37
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells
    • WJ Welch JR Feramisco 1984 Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells J Biol Chem 259 4501 4513
    • (1984) J Biol Chem , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 38
    • 0023924167 scopus 로고
    • Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat-shock protein 70, intermediate filaments, and small nuclear ribonucleoprotein complexes
    • 10.1083/jcb.106.4.1117
    • WJ Welch LA Mizzen 1988 Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat-shock protein 70, intermediate filaments, and small nuclear ribonucleoprotein complexes J Cell Biol 106 1117 1130 10.1083/jcb.106.4.1117
    • (1988) J Cell Biol , vol.106 , pp. 1117-1130
    • Welch, W.J.1    Mizzen, L.A.2
  • 39
    • 0024411246 scopus 로고
    • E1a transactivation of the human HSP70 promoter is mediated through the basal transcriptional complex
    • GT Williams TK McClanahan RI Morimoto 1989 E1a transactivation of the human HSP70 promoter is mediated through the basal transcriptional complex Mol Cell Biol 9 2574 2587
    • (1989) Mol Cell Biol , vol.9 , pp. 2574-2587
    • Williams, G.T.1    McClanahan, T.K.2    Morimoto, R.I.3


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