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Volumn 1, Issue 2, 2006, Pages 238-252

Development-dependent differences in intracellular localization of stress proteins (hsps) in rainbow trout, Oncorhynchus mykiss, following heat shock

Author keywords

Development; Heat shock proteins; Intracellular localization; Rainbow trout

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; LACTATE DEHYDROGENASE;

EID: 33646353174     PISSN: 1744117X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbd.2005.12.004     Document Type: Article
Times cited : (49)

References (39)
  • 1
    • 0028939289 scopus 로고
    • Possible correlation between DNA damage induced by hydrogen peroxide and translocation of heat shock 70 protein into the nucleus
    • Abe T., Konishi T., Hirano T., Kasai H., Shimizu K., Kashimura M., and Higashi K. Possible correlation between DNA damage induced by hydrogen peroxide and translocation of heat shock 70 protein into the nucleus. Biochem. Biophys. Res. Commun. 206 (1995) 548-555
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 548-555
    • Abe, T.1    Konishi, T.2    Hirano, T.3    Kasai, H.4    Shimizu, K.5    Kashimura, M.6    Higashi, K.7
  • 2
    • 0032168649 scopus 로고    scopus 로고
    • Effects of heat shock and hypoxia on protein synthesis in rainbow trout (Oncorhynchus mykiss) cells
    • Airaksinen S., Rabergh C.M., Sistonen L., and Nikinmaa M. Effects of heat shock and hypoxia on protein synthesis in rainbow trout (Oncorhynchus mykiss) cells. J. Exp. Biol. 201 (1998) 2543-2551
    • (1998) J. Exp. Biol. , vol.201 , pp. 2543-2551
    • Airaksinen, S.1    Rabergh, C.M.2    Sistonen, L.3    Nikinmaa, M.4
  • 3
    • 0028054130 scopus 로고
    • Relationship between the induction of proteins in the hsp70 family and thermosensitivity in two species of Oryzias (Pisces)
    • Arai A., Mitani H., Naruse K., and Shima A. Relationship between the induction of proteins in the hsp70 family and thermosensitivity in two species of Oryzias (Pisces). Comp. Biochem. Physiol. 109B (1994) 647-654
    • (1994) Comp. Biochem. Physiol. , vol.109 B , pp. 647-654
    • Arai, A.1    Mitani, H.2    Naruse, K.3    Shima, A.4
  • 4
    • 0026271750 scopus 로고
    • Expression of heat shock proteins during development in Drosophila
    • Arrigo A.P., and Tanguay R.M. Expression of heat shock proteins during development in Drosophila. Results Probl. Cell Differ. 17 (1991) 106-119
    • (1991) Results Probl. Cell Differ. , vol.17 , pp. 106-119
    • Arrigo, A.P.1    Tanguay, R.M.2
  • 6
    • 0028852907 scopus 로고
    • Depressed expression of the inducible form of hsp70 (hsp72) in brain and heart after in vivo heat shock
    • Beck S.C., Paidas C.N., Tan H., Yang J., and De Maio A. Depressed expression of the inducible form of hsp70 (hsp72) in brain and heart after in vivo heat shock. Am. J. Physiol. 269 (1995) R608-R613
    • (1995) Am. J. Physiol. , vol.269
    • Beck, S.C.1    Paidas, C.N.2    Tan, H.3    Yang, J.4    De Maio, A.5
  • 8
    • 0030601988 scopus 로고    scopus 로고
    • Localization of heat shock proteins in mouse male germ cells: an immunoelectron microscopical study
    • Biggiogera M., Tanguay R.M., Marin R., Wu Y., Martin T.E., and Fakan S. Localization of heat shock proteins in mouse male germ cells: an immunoelectron microscopical study. Exp. Cell Res. 229 (1996) 77-85
    • (1996) Exp. Cell Res. , vol.229 , pp. 77-85
    • Biggiogera, M.1    Tanguay, R.M.2    Marin, R.3    Wu, Y.4    Martin, T.E.5    Fakan, S.6
  • 9
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 and co. - a holding for folding
    • Buchner J. Hsp90 and co. - a holding for folding. Trends Biochem. Sci. 24 (1999) 136-141
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 10
    • 0031827215 scopus 로고    scopus 로고
    • Heat shock protein (hsp70) in brown trout epidermis after sudden temperature rise
    • Burkhardt-Holm P., Schmidt H., and Meier W. Heat shock protein (hsp70) in brown trout epidermis after sudden temperature rise. Comp. Biochem. Physiol., A 120 (1998) 35-41
    • (1998) Comp. Biochem. Physiol., A , vol.120 , pp. 35-41
    • Burkhardt-Holm, P.1    Schmidt, H.2    Meier, W.3
  • 11
    • 0023007393 scopus 로고
    • The dynamic state of heat shock proteins in chicken embryo fibroblasts
    • Collier N.C., and Schlesinger M.J. The dynamic state of heat shock proteins in chicken embryo fibroblasts. J. Cell Biol. 103 (1986) 1495-1507
    • (1986) J. Cell Biol. , vol.103 , pp. 1495-1507
    • Collier, N.C.1    Schlesinger, M.J.2
  • 13
    • 0033845244 scopus 로고    scopus 로고
    • The effects of heat shock and acclimation temperature on hsp70 and hsp30 mRNA expression in rainbow trout: in vivo and in vitro comparisons
    • Currie S., Moyes C.D., and Tufts B.L. The effects of heat shock and acclimation temperature on hsp70 and hsp30 mRNA expression in rainbow trout: in vivo and in vitro comparisons. J. Fish Biol. 56 (2000) 398-408
    • (2000) J. Fish Biol. , vol.56 , pp. 398-408
    • Currie, S.1    Moyes, C.D.2    Tufts, B.L.3
  • 14
    • 23644450182 scopus 로고    scopus 로고
    • Are primary cultures of trout (Oncorhynchus mykiss) ventricular cardiomyocytes metabolically viable?
    • Goldstein J.P., Scott A., and Currie S. Are primary cultures of trout (Oncorhynchus mykiss) ventricular cardiomyocytes metabolically viable?. Fish Physiol. Biochem. 30 (2005) 109-117
    • (2005) Fish Physiol. Biochem. , vol.30 , pp. 109-117
    • Goldstein, J.P.1    Scott, A.2    Currie, S.3
  • 15
    • 0015822375 scopus 로고
    • Cardiovascular and respiratory changes during heat stress in rainbow trout (Salmo gairdneri)
    • Heath A.G., and Hughes G.M. Cardiovascular and respiratory changes during heat stress in rainbow trout (Salmo gairdneri). J. Exp. Biol. 59 (1973) 323-338
    • (1973) J. Exp. Biol. , vol.59 , pp. 323-338
    • Heath, A.G.1    Hughes, G.M.2
  • 16
    • 0021917408 scopus 로고
    • Acquisition of the heat-shock response and thermotolerance during early development of Xenopus laevis
    • Heikkila J.J., Kloc M., Bury J., Schulz G.A., and Browder L.W. Acquisition of the heat-shock response and thermotolerance during early development of Xenopus laevis. Dev. Biol. 107 (1985) 483-489
    • (1985) Dev. Biol. , vol.107 , pp. 483-489
    • Heikkila, J.J.1    Kloc, M.2    Bury, J.3    Schulz, G.A.4    Browder, L.W.5
  • 18
    • 0033106368 scopus 로고    scopus 로고
    • Mutation of amino acids 24-251 alters nuclear accumulation of human heat shock protein (hsp) 72 with stress, but does not reduce viability
    • Knowlton A.A. Mutation of amino acids 24-251 alters nuclear accumulation of human heat shock protein (hsp) 72 with stress, but does not reduce viability. J. Mol. Cell. Cardiol. 31 (1999) 523-532
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 523-532
    • Knowlton, A.A.1
  • 20
    • 0037258854 scopus 로고    scopus 로고
    • Intracellular localization of the 90 kDa heat shock protein (HSP90α) determined by expression of a EGFP-HSP90α-fusion protein in unstressed and heat stressed 3T3 cells
    • Langer T., Rosmus S., and Fasold H. Intracellular localization of the 90 kDa heat shock protein (HSP90α) determined by expression of a EGFP-HSP90α-fusion protein in unstressed and heat stressed 3T3 cells. Cell Biol. Int. 27 (2003) 47-52
    • (2003) Cell Biol. Int. , vol.27 , pp. 47-52
    • Langer, T.1    Rosmus, S.2    Fasold, H.3
  • 21
    • 0021471730 scopus 로고
    • A major heat-shock protein defined by a monoclonal antibody
    • LaThangue N.B. A major heat-shock protein defined by a monoclonal antibody. EMBO J. 3 (1984) 1871-1879
    • (1984) EMBO J. , vol.3 , pp. 1871-1879
    • LaThangue, N.B.1
  • 22
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang P., and MacRae T.H. Molecular chaperones and the cytoskeleton. J. Cell. Sci. 110 (1997) 1431-1440
    • (1997) J. Cell. Sci. , vol.110 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 23
    • 0036433466 scopus 로고    scopus 로고
    • The effects of environmental heat stress on heat shock mRNA and protein expression in Miramichi Atlantic salmon (Salmo salar) parr
    • Lund S.G., Caissie D., Cunjack R.A., Vijayan M.M., and Tufts B.L. The effects of environmental heat stress on heat shock mRNA and protein expression in Miramichi Atlantic salmon (Salmo salar) parr. Can. J. Fish. Aquat. Sci. 59 (2002) 1553-1562
    • (2002) Can. J. Fish. Aquat. Sci. , vol.59 , pp. 1553-1562
    • Lund, S.G.1    Caissie, D.2    Cunjack, R.A.3    Vijayan, M.M.4    Tufts, B.L.5
  • 24
    • 22044434528 scopus 로고    scopus 로고
    • Expression patterns of three heat shock protein 70 genes among developmental stages of the red flour beetle, Tribolium castaneum (Coleptera: Tenebrionidae)
    • Mahroof R., Zhu K.Y., Neven L., Subramanyam B., and Bai J. Expression patterns of three heat shock protein 70 genes among developmental stages of the red flour beetle, Tribolium castaneum (Coleptera: Tenebrionidae). Comp. Biochem. Physiol., A 141 (2005) 247-256
    • (2005) Comp. Biochem. Physiol., A , vol.141 , pp. 247-256
    • Mahroof, R.1    Zhu, K.Y.2    Neven, L.3    Subramanyam, B.4    Bai, J.5
  • 25
    • 0030601990 scopus 로고    scopus 로고
    • The neuronal stress response: nuclear translocation of heat shock proteins as an indicator of hyperthermic stress
    • Manzerra P., and Brown I.R. The neuronal stress response: nuclear translocation of heat shock proteins as an indicator of hyperthermic stress. Exp. Cell Res. 229 (1996) 35-47
    • (1996) Exp. Cell Res. , vol.229 , pp. 35-47
    • Manzerra, P.1    Brown, I.R.2
  • 26
    • 85011584143 scopus 로고
    • Hepatocytes: isolation, maintenance and utilization
    • Biochemistry and Molecular Biology of Fishes. Hochachka P.W., and Mommsen T.P. (Eds), Elsevier, New York
    • Mommsen T.P., Moon T.W., and Walsh P.J. Hepatocytes: isolation, maintenance and utilization. In: Hochachka P.W., and Mommsen T.P. (Eds). Biochemistry and Molecular Biology of Fishes. Analytical Techniques vol. 3 (1994), Elsevier, New York 355-373
    • (1994) Analytical Techniques , vol.3 , pp. 355-373
    • Mommsen, T.P.1    Moon, T.W.2    Walsh, P.J.3
  • 27
    • 2442537231 scopus 로고    scopus 로고
    • Role of hsp90 and the hsp90-binding immunophilins in signaling protein movement
    • Pratt W.B., Galigniana M.D., Harrell J.M., and DeFranco D.B. Role of hsp90 and the hsp90-binding immunophilins in signaling protein movement. Cell. Signal. 16 (2004) 857-872
    • (2004) Cell. Signal. , vol.16 , pp. 857-872
    • Pratt, W.B.1    Galigniana, M.D.2    Harrell, J.M.3    DeFranco, D.B.4
  • 28
    • 27744523559 scopus 로고    scopus 로고
    • Intracellular localization of hsp90 is influenced by developmental stage and environmental estrogens in rainbow trout, Oncorhynchus mykiss
    • Rendell J.L., and Currie S. Intracellular localization of hsp90 is influenced by developmental stage and environmental estrogens in rainbow trout, Oncorhynchus mykiss. Physiol. Biochem. Zool. 78 (2005) 937-946
    • (2005) Physiol. Biochem. Zool. , vol.78 , pp. 937-946
    • Rendell, J.L.1    Currie, S.2
  • 29
    • 0027979131 scopus 로고
    • Heat-inducible proteins that react with antibodies to chaperonin60 are localized in the nucleus of a fish cell line
    • Sanders B.M., Nguyen J., Douglass T., and Miller S. Heat-inducible proteins that react with antibodies to chaperonin60 are localized in the nucleus of a fish cell line. Biochem. J. 297 (1994) 21-25
    • (1994) Biochem. J. , vol.297 , pp. 21-25
    • Sanders, B.M.1    Nguyen, J.2    Douglass, T.3    Miller, S.4
  • 31
    • 0002067924 scopus 로고
    • The influence of hypoxia on the preferred temperature of rainbow trout Oncorhynchus mykiss
    • Schurmann H., Steffensen J.F., and Lomholt J.P. The influence of hypoxia on the preferred temperature of rainbow trout Oncorhynchus mykiss. J. Exp. Biol. 157 (1991) 75-86
    • (1991) J. Exp. Biol. , vol.157 , pp. 75-86
    • Schurmann, H.1    Steffensen, J.F.2    Lomholt, J.P.3
  • 32
    • 0032030809 scopus 로고    scopus 로고
    • Constitutive and inducible hsp70s are involved in oxidative resistance evoked by heat shock or ethanol
    • Su C.-Y., Chong K.-Y., Owen O.E., Dillmann W.H., Chang C., and Lai C.-C. Constitutive and inducible hsp70s are involved in oxidative resistance evoked by heat shock or ethanol. J. Mol. Cell. Cardiol. 30 (1998) 587-598
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 587-598
    • Su, C.-Y.1    Chong, K.-Y.2    Owen, O.E.3    Dillmann, W.H.4    Chang, C.5    Lai, C.-C.6
  • 33
    • 0030903748 scopus 로고    scopus 로고
    • Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
    • Török Z., Horvath I., Goloubinoff P., Kovács E., Glatz A., Balogh G., and Vigh L. Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 2192-2197
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2192-2197
    • Török, Z.1    Horvath, I.2    Goloubinoff, P.3    Kovács, E.4    Glatz, A.5    Balogh, G.6    Vigh, L.7
  • 35
    • 0031786750 scopus 로고    scopus 로고
    • Does the membrane's physical state control the expression of heat shock and other genes?
    • Vigh L., Maresca B., and Harwood J.L. Does the membrane's physical state control the expression of heat shock and other genes?. Trends Biochem. Sci. 23 (1998) 369-374
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 369-374
    • Vigh, L.1    Maresca, B.2    Harwood, J.L.3
  • 36
    • 0032445640 scopus 로고    scopus 로고
    • Developmentally regulate nuclear transport of transcription factors in Drosophila embryos enable the heat shock response
    • Wang Z., and Lindquist S. Developmentally regulate nuclear transport of transcription factors in Drosophila embryos enable the heat shock response. Development 125 (1998) 4841-4850
    • (1998) Development , vol.125 , pp. 4841-4850
    • Wang, Z.1    Lindquist, S.2
  • 37
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-Dalton heat shock protein in heat-shocked mammalian cells
    • Welch W.J., and Feramisco J.R. Nuclear and nucleolar localization of the 72,000-Dalton heat shock protein in heat-shocked mammalian cells. J. Biol. Chem. 259 (1984) 4501-4513
    • (1984) J. Biol. Chem. , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 38
    • 0036711571 scopus 로고    scopus 로고
    • Differential regulation of spontaneous and heat-induced hsp70 expression in developing zebrafish (Danio rerio)
    • Yeh F.-L., and Hsu T. Differential regulation of spontaneous and heat-induced hsp70 expression in developing zebrafish (Danio rerio). J. Exp. Zool. 293 (2002) 349-359
    • (2002) J. Exp. Zool. , vol.293 , pp. 349-359
    • Yeh, F.-L.1    Hsu, T.2
  • 39
    • 0026518440 scopus 로고
    • Molecular cloning and characterization of a constitutively expressed heat-shock-cognate hsc71 gene from rainbow trout
    • Zafarullah M., Wisniewski J., Shworak N.W., Schieman S., Misra S., and Gedamu L. Molecular cloning and characterization of a constitutively expressed heat-shock-cognate hsc71 gene from rainbow trout. Eur. J. Biochem. 204 (1992) 8900-8983
    • (1992) Eur. J. Biochem. , vol.204 , pp. 8900-8983
    • Zafarullah, M.1    Wisniewski, J.2    Shworak, N.W.3    Schieman, S.4    Misra, S.5    Gedamu, L.6


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