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Volumn 276, Issue 1, 2009, Pages 286-302

Biochemical insights into the mechanisms central to the response of mammalian cells to cold stress and subsequent rewarming

Author keywords

Chaperones; CHO cells; Cold stress; Cytoskeleton; eIF3i

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; INITIATION FACTOR 3; INITIATION FACTOR 3I; PROTEIN GRP75; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 57649187405     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06781.x     Document Type: Article
Times cited : (93)

References (47)
  • 1
    • 33646066296 scopus 로고    scopus 로고
    • The cold-shock response in cultured mammalian cells: Harnessing the response for the improvement of recombinant protein production
    • Al-Fageeh MB, Marchant RJ, Carden MJ Smales CM (2006) The cold-shock response in cultured mammalian cells: harnessing the response for the improvement of recombinant protein production. Biotechnol Bioeng 93, 829 835.
    • (2006) Biotechnol Bioeng , vol.93 , pp. 829-835
    • Al-Fageeh, M.B.1    Marchant, R.J.2    Carden, M.J.3    Smales, C.M.4
  • 3
    • 33746079244 scopus 로고    scopus 로고
    • Control and regulation of the cellular responses to cold shock: The responses in yeast and mammalian systems
    • Al-Fageeh MB Smales CM (2006) Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems. Biochem J 397, 247 259.
    • (2006) Biochem J , vol.397 , pp. 247-259
    • Al-Fageeh, M.B.1    Smales, C.M.2
  • 4
    • 0036096124 scopus 로고    scopus 로고
    • Effects of heat and cold stress on mammalian gene expression
    • Sonna LA, Fujita J, Gaffin SL Lilly CM (2002) Effects of heat and cold stress on mammalian gene expression. J Appl Physiol 92, 1725 1742.
    • (2002) J Appl Physiol , vol.92 , pp. 1725-1742
    • Sonna, L.A.1    Fujita, J.2    Gaffin, S.L.3    Lilly, C.M.4
  • 5
    • 0031591694 scopus 로고    scopus 로고
    • Increased transcript level of RBM3, a member of the glycine-rich RNA-binding protein family, in human cells in response to cold stress
    • Danno S, Nishiyama H, Higashitsuji H, Yokoi H, Xue JH, Itoh K, Matsuda T Fujita J (1997) Increased transcript level of RBM3, a member of the glycine-rich RNA-binding protein family, in human cells in response to cold stress. Biochem Biophys Res Commun 236, 804 807.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 804-807
    • Danno, S.1    Nishiyama, H.2    Higashitsuji, H.3    Yokoi, H.4    Xue, J.H.5    Itoh, K.6    Matsuda, T.7    Fujita, J.8
  • 6
    • 0031578903 scopus 로고    scopus 로고
    • Cloning and characterization of human CIRP (cold-inducible RNA-binding protein) cDNA and chromosomal assignment of the gene
    • Nishiyama H, Higashitsuji H, Yokoi H, Itoh K, Danno S, Matsuda T Fujita J (1997) Cloning and characterization of human CIRP (cold-inducible RNA-binding protein) cDNA and chromosomal assignment of the gene. Gene 204, 115 120.
    • (1997) Gene , vol.204 , pp. 115-120
    • Nishiyama, H.1    Higashitsuji, H.2    Yokoi, H.3    Itoh, K.4    Danno, S.5    Matsuda, T.6    Fujita, J.7
  • 7
    • 13844309577 scopus 로고    scopus 로고
    • Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis
    • Dresios J, Aschrafi A, Owens GC, Vanderklish PW, Edelman GM Mauro VP (2005) Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis. Proc Natl Acad Sci USA 102, 1865 1870.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1865-1870
    • Dresios, J.1    Aschrafi, A.2    Owens, G.C.3    Vanderklish, P.W.4    Edelman, G.M.5    Mauro, V.P.6
  • 8
    • 52049120427 scopus 로고    scopus 로고
    • Metabolic rates, growth phase, and mRNA levels influence cell-specific antibody production levels from in vitro-cultured mammalian cells at sub-physiological temperatures
    • Marchant RJ, Al-Fageeh MB, Underhill MF, Racher AJ Smales CM (2008) Metabolic rates, growth phase, and mRNA levels influence cell-specific antibody production levels from in vitro-cultured mammalian cells at sub-physiological temperatures. Mol Biotechnol 39, 69 77.
    • (2008) Mol Biotechnol , vol.39 , pp. 69-77
    • Marchant, R.J.1    Al-Fageeh, M.B.2    Underhill, M.F.3    Racher, A.J.4    Smales, C.M.5
  • 9
    • 0030975108 scopus 로고    scopus 로고
    • A glycine-rich RNA-binding protein mediating cold-inducible suppression of mammalian cell growth
    • Nishiyama H, Itoh K, Kaneko Y, Kishishita M, Yoshida O Fujita J (1997) A glycine-rich RNA-binding protein mediating cold-inducible suppression of mammalian cell growth. J Cell Biol 137, 899 908.
    • (1997) J Cell Biol , vol.137 , pp. 899-908
    • Nishiyama, H.1    Itoh, K.2    Kaneko, Y.3    Kishishita, M.4    Yoshida, O.5    Fujita, J.6
  • 10
    • 0022560286 scopus 로고
    • Microtubule dynamics during the cell cycle: The effects of taxol and nocodazole on the microtubule system of Pt K2 cells at different stages of the mitotic cycle
    • De Brabander M, Geuens G, Nuydens R, Willebrords R, Aerts F De Mey J (1986) Microtubule dynamics during the cell cycle: the effects of taxol and nocodazole on the microtubule system of Pt K2 cells at different stages of the mitotic cycle. Int Rev Cytol 101, 215 274.
    • (1986) Int Rev Cytol , vol.101 , pp. 215-274
    • De Brabander, M.1    Geuens, G.2    Nuydens, R.3    Willebrords, R.4    Aerts, F.5    De Mey, J.6
  • 15
    • 0032965702 scopus 로고    scopus 로고
    • Characterization of p53 in Chinese hamster cell lines CHO-K1, CHO-WBL, and CHL: Implications for genotoxicity testing
    • Hu T, Miller CM, Ridder GM Aardema MJ (1999) Characterization of p53 in Chinese hamster cell lines CHO-K1, CHO-WBL, and CHL: implications for genotoxicity testing. Mutat Res 426, 51 62.
    • (1999) Mutat Res , vol.426 , pp. 51-62
    • Hu, T.1    Miller, C.M.2    Ridder, G.M.3    Aardema, M.J.4
  • 16
    • 0028232785 scopus 로고
    • Transient cold shock induces the heat shock response upon recovery at 37 °c in human cells
    • Liu AY-C, Bian H, Huang E Lee YK (1994) Transient cold shock induces the heat shock response upon recovery at 37 °C in human cells. J Biol Chem 269, 14768 14775.
    • (1994) J Biol Chem , vol.269 , pp. 14768-14775
    • Ay-C, L.1    Bian, H.2    Huang, E.3    Lee, Y.K.4
  • 17
    • 0027509361 scopus 로고
    • The constitutive and stress inducible forms of hsp70 exhibit functional similarities and interact with one another in an ATP-dependent fashion
    • Brown CR, Martin RL, Hansen WJ, BecKmann RP Welch WJ (1993) The constitutive and stress inducible forms of hsp70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. J Cell Biol 120, 1101 1112.
    • (1993) J Cell Biol , vol.120 , pp. 1101-1112
    • Brown, C.R.1    Martin, R.L.2    Hansen, W.J.3    Beckmann, R.P.4    Welch, W.J.5
  • 18
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya K, Myers MP, Murphy SP Morimoto MI (1992) The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev 6, 1153 1164.
    • (1992) Genes Dev , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, M.I.4
  • 19
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI (1998) Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 12, 3788 3796.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 20
    • 0027461364 scopus 로고
    • Activation of heat shock gene transcription by heat shock factor 1 involves oligomerisation, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress
    • Sarge KD, Murphy SP Morimoto RI (1993) Activation of heat shock gene transcription by heat shock factor 1 involves oligomerisation, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress. Mol Cell Biol 13, 1392 1407.
    • (1993) Mol Cell Biol , vol.13 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 21
    • 0030043401 scopus 로고    scopus 로고
    • Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation
    • Cotto JJ, Kline M Morimoto M (1996) Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. J Biol Chem 271, 3355 3358.
    • (1996) J Biol Chem , vol.271 , pp. 3355-3358
    • Cotto, J.J.1    Kline, M.2    Morimoto, M.3
  • 22
    • 44949259971 scopus 로고    scopus 로고
    • Mechanistic elements of protein cold denaturation
    • Lopez CF, Darst RK Rossky PJ (2008) Mechanistic elements of protein cold denaturation. J Phys Chem B 112, 5961 5967.
    • (2008) J Phys Chem B , vol.112 , pp. 5961-5967
    • Lopez, C.F.1    Darst, R.K.2    Rossky, P.J.3
  • 23
    • 0031017476 scopus 로고    scopus 로고
    • A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperaures
    • Kaneko Y, Nishiyama H, Nonoguchi K, Higashitsuji H, Kishishita M Fugita J (1997) A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperaures. J Biol Chem 272, 2640 2645.
    • (1997) J Biol Chem , vol.272 , pp. 2640-2645
    • Kaneko, Y.1    Nishiyama, H.2    Nonoguchi, K.3    Higashitsuji, H.4    Kishishita, M.5    Fugita, J.6
  • 25
    • 33845937441 scopus 로고    scopus 로고
    • On the effect of transient expression of mutated eIF2 alpha and eIF4E eukaryotic translation initiation factors on reporter gene expression in mammalian cells upon cold-shock
    • Underhill MF, Marchant RJ, Carden MJ, James DC Smales CM (2006) On the effect of transient expression of mutated eIF2 alpha and eIF4E eukaryotic translation initiation factors on reporter gene expression in mammalian cells upon cold-shock. Mol Biotechnol 34, 141 149.
    • (2006) Mol Biotechnol , vol.34 , pp. 141-149
    • Underhill, M.F.1    Marchant, R.J.2    Carden, M.J.3    James, D.C.4    Smales, C.M.5
  • 26
    • 0031033314 scopus 로고    scopus 로고
    • Conservation and diversity of eukaryotic translation factor eIF3
    • Asano K, Kinzy TG, Merrick WC Hershey JWB (1997) Conservation and diversity of eukaryotic translation factor eIF3. J Biol Chem 272, 1101 1109.
    • (1997) J Biol Chem , vol.272 , pp. 1101-1109
    • Asano, K.1    Kinzy, T.G.2    Merrick, W.C.3    Hershey, J.W.B.4
  • 27
    • 33748924333 scopus 로고    scopus 로고
    • EIF3: A versatile scaffold for translation initiation complexes
    • Hinnebusch AG (2006) eIF3: a versatile scaffold for translation initiation complexes. Trends Biochem Sci 31, 553 562.
    • (2006) Trends Biochem Sci , vol.31 , pp. 553-562
    • Hinnebusch, A.G.1
  • 28
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valasek L, Nielsen KH Hinnebusch AG (2002) Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO J 21, 5886 5898.
    • (2002) EMBO J , vol.21 , pp. 5886-5898
    • Valasek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 29
    • 34547178178 scopus 로고    scopus 로고
    • Reconstitution reveals the functional core of mammalian eIF3
    • Matsutani M, Sonenberg N, Yokoyama S Imataka H (2007) Reconstitution reveals the functional core of mammalian eIF3. EMBO J 26, 3373 3383.
    • (2007) EMBO J , vol.26 , pp. 3373-3383
    • Matsutani, M.1    Sonenberg, N.2    Yokoyama, S.3    Imataka, H.4
  • 30
    • 33845397658 scopus 로고    scopus 로고
    • Carcinoma-associated eIF3i overexpression facilitates mTOR-dependent growth transformation
    • Ahlemann M, Zeidler R, Lang S, Mack B, Munz M Gires O (2006) Carcinoma-associated eIF3i overexpression facilitates mTOR-dependent growth transformation. Mol Carcinog 45, 957 967.
    • (2006) Mol Carcinog , vol.45 , pp. 957-967
    • Ahlemann, M.1    Zeidler, R.2    Lang, S.3    MacK, B.4    Munz, M.5    Gires, O.6
  • 31
    • 34247165835 scopus 로고    scopus 로고
    • Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells
    • Zhang L, Pan X Hershey JW (2007) Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells. J Biol Chem 282, 5790 5800.
    • (2007) J Biol Chem , vol.282 , pp. 5790-5800
    • Zhang, L.1    Pan, X.2    Hershey, J.W.3
  • 32
    • 0033526546 scopus 로고    scopus 로고
    • Influence of low temperature on productivity, proteome and protein phosphorylation of CHO cells
    • Kaufmann H, Mazur X, Fussenegger M Bailey JE (1999) Influence of low temperature on productivity, proteome and protein phosphorylation of CHO cells. Biotechnol Bioeng 63, 573 582.
    • (1999) Biotechnol Bioeng , vol.63 , pp. 573-582
    • Kaufmann, H.1    Mazur, X.2    Fussenegger, M.3    Bailey, J.E.4
  • 33
    • 0032250227 scopus 로고    scopus 로고
    • Hypothermia causes a reversible, p53-mediated cell cycle arrest in cultured fibroblasts
    • Matijasevic Z, Snyder JE Ludlum DB (1998) Hypothermia causes a reversible, p53-mediated cell cycle arrest in cultured fibroblasts. Oncol Res 10, 605 610.
    • (1998) Oncol Res , vol.10 , pp. 605-610
    • Matijasevic, Z.1    Snyder, J.E.2    Ludlum, D.B.3
  • 34
    • 0032546272 scopus 로고    scopus 로고
    • P53-dependent induction of WAF1 by cold shock human glioblastoma cells
    • Ohnishi T, Wang X, Ohnishi K Takahashi A (1998) p53-dependent induction of WAF1 by cold shock human glioblastoma cells. Oncogene 16, 1507 1511.
    • (1998) Oncogene , vol.16 , pp. 1507-1511
    • Ohnishi, T.1    Wang, X.2    Ohnishi, K.3    Takahashi, A.4
  • 35
    • 28244470279 scopus 로고    scopus 로고
    • Activation of wild type p53 function by its mortalin-binding, cytoplasmically localizing carboxyl terminus peptides
    • Kaul SC, Aaida S, Yaguchi T, Kaur K Wadhwa R (2005) Activation of wild type p53 function by its mortalin-binding, cytoplasmically localizing carboxyl terminus peptides. J Biol Chem 280, 39373 39379.
    • (2005) J Biol Chem , vol.280 , pp. 39373-39379
    • Kaul, S.C.1    Aaida, S.2    Yaguchi, T.3    Kaur, K.4    Wadhwa, R.5
  • 36
    • 34247887536 scopus 로고    scopus 로고
    • Direct evidence for the role of centrosomally localized p53 in the regulation of centrosome duplication
    • Shinmura K, Bennett RA, Tarapore P Fukasawa K (2007) Direct evidence for the role of centrosomally localized p53 in the regulation of centrosome duplication. Oncogene 26, 2939 2944.
    • (2007) Oncogene , vol.26 , pp. 2939-2944
    • Shinmura, K.1    Bennett, R.A.2    Tarapore, P.3    Fukasawa, K.4
  • 37
    • 0035909514 scopus 로고    scopus 로고
    • Difference in the centrosome duplication regulatory activity among p53 'hot spot' mutants: Potential role of Ser 315 phophorylation-dependent centrosome binding of p53
    • Tarapore P, Tokuyama Y, Horn HF Fukasawa K (2001) Difference in the centrosome duplication regulatory activity among p53 'hot spot' mutants: potential role of Ser 315 phophorylation-dependent centrosome binding of p53. Oncogene 20, 6851 6863.
    • (2001) Oncogene , vol.20 , pp. 6851-6863
    • Tarapore, P.1    Tokuyama, Y.2    Horn, H.F.3    Fukasawa, K.4
  • 38
    • 33748286872 scopus 로고    scopus 로고
    • Mortalin controls centrosome duplication via modulating centrosomal localization of p53
    • Ma Z, Izumi H, Kanai M, Kabuyama Y, Ahn N Fukasawa K (2006) Mortalin controls centrosome duplication via modulating centrosomal localization of p53. Oncogene 25, 5377 5390.
    • (2006) Oncogene , vol.25 , pp. 5377-5390
    • Ma, Z.1    Izumi, H.2    Kanai, M.3    Kabuyama, Y.4    Ahn, N.5    Fukasawa, K.6
  • 40
    • 0028916402 scopus 로고
    • Thermal adaptation in biological membranes: Is homeoviscous adaptation the explanation?
    • Hazel JR (1995) Thermal adaptation in biological membranes: is homeoviscous adaptation the explanation? Annu Rev Physiol 57, 19 42.
    • (1995) Annu Rev Physiol , vol.57 , pp. 19-42
    • Hazel, J.R.1
  • 41
    • 0030798256 scopus 로고    scopus 로고
    • Alterations in cellular lipids may be responsible for the transient nature of the yeast heat shock response
    • Chatterjee MT, Khalawan SA Curran BP (1997) Alterations in cellular lipids may be responsible for the transient nature of the yeast heat shock response. Microbiology 143, 3063 3068.
    • (1997) Microbiology , vol.143 , pp. 3063-3068
    • Chatterjee, M.T.1    Khalawan, S.A.2    Curran, B.P.3
  • 42
    • 38349054555 scopus 로고    scopus 로고
    • The increase of cell-membranous phosphatidylcholines containing polyunsaturated fatty acid residues induces phosphorylation of p53 through activation of ATR
    • Zhang XH, Zhao C Ma ZA (2007) The increase of cell-membranous phosphatidylcholines containing polyunsaturated fatty acid residues induces phosphorylation of p53 through activation of ATR. J Cell Sci 120, 4134 4143.
    • (2007) J Cell Sci , vol.120 , pp. 4134-4143
    • Zhang, X.H.1    Zhao, C.2    Ma, Z.A.3
  • 43
    • 0042197431 scopus 로고
    • Comparison of amino acid uptake and incorporation in Tetrahymena pyriformis and HeLa cells
    • Wheatley DN Walker E (1980) Comparison of amino acid uptake and incorporation in Tetrahymena pyriformis and HeLa cells. J Comp Phys B 140, 267 274.
    • (1980) J Comp Phys B , vol.140 , pp. 267-274
    • Wheatley, D.N.1    Walker, E.2
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 46
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies
    • Woods A, Sherwin T, Sasse R, MacRae TH, Baines AJ Gull K (1989) Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies. J Cell Sci 93, 491 500.
    • (1989) J Cell Sci , vol.93 , pp. 491-500
    • Woods, A.1    Sherwin, T.2    Sasse, R.3    MacRae, T.H.4    Baines, A.J.5    Gull, K.6
  • 47
    • 0032587044 scopus 로고    scopus 로고
    • Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle
    • Roobol A Carden MJ (1999) Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle. Eur J Cell Biol 78, 21 32.
    • (1999) Eur J Cell Biol , vol.78 , pp. 21-32
    • Roobol, A.1    Carden, M.J.2


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