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Volumn 119, Issue 2, 1998, Pages 381-389

Heat-Shock-Induced Assembly of Hsp30 Family Members into High Molecular Weight Aggregates in Xenopus laevis Cultured Cells

Author keywords

A6 cells; Heat shock protein; hsp70; Pore exclusion limit electrophoresis; Rate zonal centrifugation; Xenopus laevis

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 30; HEAT SHOCK PROTEIN 70; UNCLASSIFIED DRUG;

EID: 0031895813     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(97)00364-7     Document Type: Article
Times cited : (22)

References (32)
  • 1
    • 0000694228 scopus 로고
    • Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity
    • Anderson, L.; Borg, H.; Mikaelsson, M. Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity. FEBS Lett. 20:199-202;1972.
    • (1972) FEBS Lett. , vol.20 , pp. 199-202
    • Anderson, L.1    Borg, H.2    Mikaelsson, M.3
  • 2
    • 0002241311 scopus 로고
    • Expression and function of the low-molecular-weight heat shock proteins
    • Morimoto, R.I.; Tissieres, A.; Georgopolous, C. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Arrigo, A-P.; Landry, J. Expression and function of the low-molecular-weight heat shock proteins. In: Morimoto, R.I.; Tissieres, A.; Georgopolous, C. (eds). The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 1994:335-373.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.-P.1    Landry, J.2
  • 3
    • 0024285837 scopus 로고
    • Identity of the 19S "prosome" particle with the large multifunctional protease complex of mammalian cells (the proteasome)
    • Arrigo, A.-P.; Tanaka, K.; Goldberg, A. Identity of the 19S "prosome" particle with the large multifunctional protease complex of mammalian cells (the proteasome). Nature 331: 192-194;1988.
    • (1988) Nature , vol.331 , pp. 192-194
    • Arrigo, A.-P.1    Tanaka, K.2    Goldberg, A.3
  • 4
    • 0023656751 scopus 로고
    • Characterization and purification of the mammalian 28,000 dalton heat shock protein
    • Arrigo, A-P.; Welch, W.J. Characterization and purification of the mammalian 28,000 dalton heat shock protein. J. Biol. Chem. 262:15359-15369;1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15359-15369
    • Arrigo, A.-P.1    Welch, W.J.2
  • 6
    • 0026530483 scopus 로고
    • The small heat-shock protein hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate
    • Bentley, N.J.; Fitch, I.T.; Tuite, M.F. The small heat-shock protein hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate. Yeast 8:95-106;1992.
    • (1992) Yeast , vol.8 , pp. 95-106
    • Bentley, N.J.1    Fitch, I.T.2    Tuite, M.F.3
  • 7
    • 0023941655 scopus 로고
    • Ultrastructural and biochemical analysis of the stress granule in chicken embryo fibroblasts
    • Collier, N.C.; Heuser, J.; Aach Levy, M.; Schlesinger, M.J. Ultrastructural and biochemical analysis of the stress granule in chicken embryo fibroblasts. J. Biol. Chem. 106:1131-1139; 1988.
    • (1988) J. Biol. Chem. , vol.106 , pp. 1131-1139
    • Collier, N.C.1    Heuser, J.2    Aach Levy, M.3    Schlesinger, M.J.4
  • 9
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.-U. Molecular chaperones in cellular protein folding. Nature 381:571-680;1996.
    • (1996) Nature , vol.381 , pp. 571-680
    • Hartl, F.-U.1
  • 10
    • 0030766710 scopus 로고    scopus 로고
    • Heat shock protein gene expression during Xenopus development
    • Heikkila, J.J.; Ohan, N.; Tam, Y.; Ali, A. Heat shock protein gene expression during Xenopus development. Cell. Mol. Life Sci. 53:114-121;1997.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 114-121
    • Heikkila, J.J.1    Ohan, N.2    Tam, Y.3    Ali, A.4
  • 11
    • 0027434618 scopus 로고
    • Localization of small heat shock proteins to the higher plant endomembrane system
    • Helm, K.; LaFayette, P.; Nagao, R.; Key, J.; Vierling, E. Localization of small heat shock proteins to the higher plant endomembrane system. Mol. Cell Biol. 13:238-247;1993.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 238-247
    • Helm, K.1    LaFayette, P.2    Nagao, R.3    Key, J.4    Vierling, E.5
  • 12
    • 0026081094 scopus 로고
    • Studies of the small heat shock proteins of Caenorhabditis elegans using anti-peptide antibodies
    • Hockertz, M.K.; Clark-Lewis, I.; Candido, E.P.M. Studies of the small heat shock proteins of Caenorhabditis elegans using anti-peptide antibodies. FEBS Lett. 280:375-378;1991.
    • (1991) FEBS Lett. , vol.280 , pp. 375-378
    • Hockertz, M.K.1    Clark-Lewis, I.2    Candido, E.P.M.3
  • 13
    • 0028346451 scopus 로고
    • Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
    • Kato, K.H.; Hasegawa, K.; Goto, S.; Inaguma, Y. Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27. J. Biol. Chem. 269:11274-11278; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11274-11278
    • Kato, K.H.1    Hasegawa, K.2    Goto, S.3    Inaguma, Y.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227:680-685; 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0024345716 scopus 로고
    • Heat shock resistance conferred by expression of the human hsp27 gene in rodent cells
    • Landry, J.; Chretien, P.; Lambert, H.; Hickey, E.; Weber, L.A. Heat shock resistance conferred by expression of the human hsp27 gene in rodent cells. J. Cell Biol. 109:7-15;1989.
    • (1989) J. Cell Biol. , vol.109 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, H.3    Hickey, E.4    Weber, L.A.5
  • 16
    • 0031020927 scopus 로고    scopus 로고
    • Purification, structure and molecular chaperone activity in vitro of Artemia p26, a small heat shock/α-crystallin protein
    • Liang, P.; Amons, R.; Clegg, J.S.; MacRae, T.H. Purification, structure and molecular chaperone activity in vitro of Artemia p26, a small heat shock/α-crystallin protein. Eur. J. Biochem. 243:225-232;1997.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 225-232
    • Liang, P.1    Amons, R.2    Clegg, J.S.3    MacRae, T.H.4
  • 18
    • 0014105804 scopus 로고
    • Tables for estimating sedimentation through linear concentration gradients of sucrose solution
    • McEwen, C.R. Tables for estimating sedimentation through linear concentration gradients of sucrose solution. Anal. Biochem. 20:114-1149;1967.
    • (1967) Anal. Biochem. , vol.20 , pp. 114-1149
    • McEwen, C.R.1
  • 19
    • 0028263008 scopus 로고
    • The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization
    • Mehlen, P.; Arrigo, A-P. The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization. Eur. J. Biochem. 221:327-334:1994.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 327-334
    • Mehlen, P.1    Arrigo, A.-P.2
  • 22
    • 85140937411 scopus 로고
    • Intracellular localization and related functions of heat shock proteins
    • Nover, L. (ed). Boca Raton, FL: CRC Press
    • Nover, L.; Neumann, D.; Scharf, D. Intracellular localization and related functions of heat shock proteins. In: Nover, L. (ed). The Heat Shock Response. Boca Raton, FL: CRC Press; 1991:373-407.
    • (1991) The Heat Shock Response , pp. 373-407
    • Nover, L.1    Neumann, D.2    Scharf, D.3
  • 23
    • 0024639409 scopus 로고
    • Cytoplasmic heat shock granules are formed from precursor particles and contain a specific set of mRNAs
    • Nover, L.; Scharf, D.; Neumann, D. Cytoplasmic heat shock granules are formed from precursor particles and contain a specific set of mRNAs. Mol. Cell. Biol. 9:1298-1308;1989.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1298-1308
    • Nover, L.1    Scharf, D.2    Neumann, D.3
  • 24
    • 0020826867 scopus 로고
    • Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves
    • Nover, L.; Scharf, D.; Neumann, D. Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves. Mol. Cell. Biol. 3:1648-1655;1983.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1648-1655
    • Nover, L.1    Scharf, D.2    Neumann, D.3
  • 25
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007-4021;1975.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.1
  • 26
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D.A.; Lindquist, S. The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Ann. Rev. Genet. 27:437-496;1993.
    • (1993) Ann. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 27
    • 0021886204 scopus 로고
    • Analysis of cytoplasmic 19 S ringtype particles in Drosophila which contain hsp 23 at normal growth temperature
    • Schuldt, C.; Kloetzel, P-M. Analysis of cytoplasmic 19 S ringtype particles in Drosophila which contain hsp 23 at normal growth temperature. Dev. Biol. 110:65-72;1985.
    • (1985) Dev. Biol. , vol.110 , pp. 65-72
    • Schuldt, C.1    Kloetzel, P.-M.2
  • 29
    • 0029558353 scopus 로고
    • Identification of members of the hsp30 small heat shock protein family and characterization of their developmental regulation in heat shocked Xenoptts laevis embryos
    • Tam, Y.; Heikkila, J.J. Identification of members of the hsp30 small heat shock protein family and characterization of their developmental regulation in heat shocked Xenoptts laevis embryos. Dev. Gen. 17:331-339;1995.
    • (1995) Dev. Gen. , vol.17 , pp. 331-339
    • Tam, Y.1    Heikkila, J.J.2
  • 30
    • 0028097732 scopus 로고
    • Variation in heat-shock proteins among species of desert fishes (Poeciliidae, Poeciliopsis)
    • White, C.N.; Hightower, L.E.; Schultz, R.J. Variation in heat-shock proteins among species of desert fishes (Poeciliidae, Poeciliopsis). Mol. Biol. Evol. 11:106-119;1994.
    • (1994) Mol. Biol. Evol. , vol.11 , pp. 106-119
    • White, C.N.1    Hightower, L.E.2    Schultz, R.J.3
  • 31
    • 0024369102 scopus 로고
    • Induction of glucose-regulated proteins in Xenopus laevis A6 cells
    • Winning, R.; Heikkila, J.J.; Bols, N. Induction of glucose-regulated proteins in Xenopus laevis A6 cells. J. Cell Physiol. 140:239-245;1989.
    • (1989) J. Cell Physiol. , vol.140 , pp. 239-245
    • Winning, R.1    Heikkila, J.J.2    Bols, N.3
  • 32
    • 0010193025 scopus 로고
    • Measurement of sedimentation coefficients and computer simulation of rate-zonal separations
    • Rickwood, D. (ed). Oxford: IRL Press
    • Young, B.D. Measurement of sedimentation coefficients and computer simulation of rate-zonal separations. In: Rickwood, D. (ed). Centrifugation: A Practical Approach. Oxford: IRL Press; 1984:127-159.
    • (1984) Centrifugation: A Practical Approach , pp. 127-159
    • Young, B.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.