메뉴 건너뛰기




Volumn 3, Issue 3, 2005, Pages 155-164

Resistance to dehydration damage in HeLa cells correlates with the presence of endogenous heat shock proteins

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; TREHALOSE;

EID: 27644556802     PISSN: 1538344X     EISSN: None     Source Type: Journal    
DOI: 10.1089/cpt.2005.3.155     Document Type: Article
Times cited : (8)

References (54)
  • 1
    • 0001371293 scopus 로고
    • Tissue culture studies of the proliferative capacity of cervical carcinoma and normal epithelium
    • Gey GO, Coffman WD, Kubicek MT. Tissue culture studies of the proliferative capacity of cervical carcinoma and normal epithelium. Cancer Res 1952; 12:264-265.
    • (1952) Cancer Res , vol.12 , pp. 264-265
    • Gey, G.O.1    Coffman, W.D.2    Kubicek, M.T.3
  • 2
    • 0016156033 scopus 로고
    • Banded marker chromosomes as indicators of intraspecies cellular contamination
    • Nelson-Rees WA, Flandermeyer RR, Hawthorne PK. Banded marker chromosomes as indicators of intraspecies cellular contamination. Science 1974;184: 1093-1096.
    • (1974) Science , vol.184 , pp. 1093-1096
    • Nelson-Rees, W.A.1    Flandermeyer, R.R.2    Hawthorne, P.K.3
  • 4
    • 12344255887 scopus 로고    scopus 로고
    • Cell line cross contamination: How aware are mammalian cell culturists of the problem and how to monitor it?
    • Buehring GC, Eby EA, Eby MJ. Cell line cross contamination: How aware are mammalian cell culturists of the problem and how to monitor it? In Vitro Cell Dev Biol: Animal 2004;40:211-215.
    • (2004) In Vitro Cell Dev Biol: Animal , vol.40 , pp. 211-215
    • Buehring, G.C.1    Eby, E.A.2    Eby, M.J.3
  • 5
    • 0026592339 scopus 로고
    • Temperature-dependent perturbation of phospholipids bilayers by dimethylsulfoxide
    • Anchordoguy TJ, Carpenter JF, Crowe JH, et al. Temperature-dependent perturbation of phospholipids bilayers by dimethylsulfoxide. Biochim Biophys Acta 1992;1104:117-122.
    • (1992) Biochim Biophys Acta , vol.1104 , pp. 117-122
    • Anchordoguy, T.J.1    Carpenter, J.F.2    Crowe, J.H.3
  • 6
    • 0025353404 scopus 로고
    • The basis for toxicity of certain cryoprotectants: A hypothesis
    • Arakawa T, Carpenter JF, Kita YA, et al. The basis for toxicity of certain cryoprotectants: a hypothesis. Cryobiology 1990;27:401-415.
    • (1990) Cryobiology , vol.27 , pp. 401-415
    • Arakawa, T.1    Carpenter, J.F.2    Kita, Y.A.3
  • 7
    • 0028838470 scopus 로고
    • Trehalose and sucrose both protect the membranes and proteins in intact bacteria during drying
    • Leslie SB, Israeli E, Lighthart B, et al. Trehalose and sucrose both protect the membranes and proteins in intact bacteria during drying. Appl Environ Microbiol 1995;61:3592-3597.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3592-3597
    • Leslie, S.B.1    Israeli, E.2    Lighthart, B.3
  • 8
    • 0033973790 scopus 로고    scopus 로고
    • Preservation of mammalian cells-learning nature's tricks
    • Crowe JH, Crowe LM. Preservation of mammalian cells-learning nature's tricks. Nat Biotechnol 2000;18: 145-146.
    • (2000) Nat Biotechnol , vol.18 , pp. 145-146
    • Crowe, J.H.1    Crowe, L.M.2
  • 9
    • 0013218062 scopus 로고    scopus 로고
    • Survival of desiccated mammalian cells: Beneficial effects of isotonic media
    • Acker JP, Fowler A, Lauman B, et al. Survival of desiccated mammalian cells: beneficial effects of isotonic media. Cell Preserv Technol 2002;1:129-140.
    • (2002) Cell Preserv Technol , vol.1 , pp. 129-140
    • Acker, J.P.1    Fowler, A.2    Lauman, B.3
  • 10
    • 0242668771 scopus 로고    scopus 로고
    • Desiccation tolerance of spermatozoa dried at ambient temperature: Production of fetal mice
    • Bhowmick S, Zhu L, McGinnis L, et al. Desiccation tolerance of spermatozoa dried at ambient temperature: production of fetal mice. Biolo Reprod 2003;68: 1779-1786.
    • (2003) Biolo Reprod , vol.68 , pp. 1779-1786
    • Bhowmick, S.1    Zhu, L.2    McGinnis, L.3
  • 11
    • 0034869661 scopus 로고    scopus 로고
    • Engineering mammalian cells for solid-state sensor applications
    • Bloom FR, Price P, Lao G, et al. Engineering mammalian cells for solid-state sensor applications. Biosens Bioelectron 2001;16:603-608.
    • (2001) Biosens Bioelectron , vol.16 , pp. 603-608
    • Bloom, F.R.1    Price, P.2    Lao, G.3
  • 12
    • 0036191709 scopus 로고    scopus 로고
    • Recovery of human mesenchymal stem cells following dehydration and rehydration
    • Gordon SL, Oppenheimer SR, Mackay AM, et al. Recovery of human mesenchymal stem cells following dehydration and rehydration. Cryobiology 2001;43: 182-187.
    • (2001) Cryobiology , vol.43 , pp. 182-187
    • Gordon, S.L.1    Oppenheimer, S.R.2    Mackay, A.M.3
  • 13
    • 0033950708 scopus 로고    scopus 로고
    • Trehalose expression confers desiccation tolerance on human cells
    • Guo N, Puhlev I, Brown DR, et al. Trehalose expression confers desiccation tolerance on human cells. Nat Biotechnol 2000;18:168-171.
    • (2000) Nat Biotechnol , vol.18 , pp. 168-171
    • Guo, N.1    Puhlev, I.2    Brown, D.R.3
  • 14
    • 0034796520 scopus 로고    scopus 로고
    • Desiccation tolerance in human cells
    • Puhlev I, Guo N, Brown DR, et al. Desiccation tolerance in human cells. Cryobiology 2001;42:207-217.
    • (2001) Cryobiology , vol.42 , pp. 207-217
    • Puhlev, I.1    Guo, N.2    Brown, D.R.3
  • 15
    • 0344076342 scopus 로고    scopus 로고
    • Comprehensive and definitive molecular cytogenetic characterization of HeLa cells by spectral karyotyping
    • Macville M, Schrock E, Padilla-Nash H, et al. Comprehensive and definitive molecular cytogenetic characterization of HeLa cells by spectral karyotyping. Cancer Res 1999;59:141-150.
    • (1999) Cancer Res , vol.59 , pp. 141-150
    • Macville, M.1    Schrock, E.2    Padilla-Nash, H.3
  • 16
    • 23444443329 scopus 로고    scopus 로고
    • A small stress protein acts synergistically with trehalose to confer desiccation tolerance on mammalian cells
    • Ma X, Jamil K, MacRae TH, et al. A small stress protein acts synergistically with trehalose to confer desiccation tolerance on mammalian cells. Cryobiology 2005;51:15-28.
    • (2005) Cryobiology , vol.51 , pp. 15-28
    • Ma, X.1    Jamil, K.2    MacRae, T.H.3
  • 17
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S. The heat-shock response. Annu Rev Biochem 1986;55:1151-1191.
    • (1986) Annu Rev Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 18
    • 0025330639 scopus 로고
    • Heat shock proteins
    • Schlesinger MJ. Heat shock proteins. J Biol Chem 1990;265:12111-12114.
    • (1990) J Biol Chem , vol.265 , pp. 12111-12114
    • Schlesinger, M.J.1
  • 19
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • Hendrick JP, Hartl FU. The role of molecular chaperones in protein folding. FASEB J 1995;9:1559-1569.
    • (1995) FASEB J , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.U.2
  • 20
    • 0035377254 scopus 로고    scopus 로고
    • Heat-induced nuclear accumulation of hsc70s is regulated by phosphorylation and inhibited in confluent cells
    • Chu A, Matusiewicz N, Stochaj U. Heat-induced nuclear accumulation of hsc70s is regulated by phosphorylation and inhibited in confluent cells. FASEB J 2001;15:1478-1480.
    • (2001) FASEB J , vol.15 , pp. 1478-1480
    • Chu, A.1    Matusiewicz, N.2    Stochaj, U.3
  • 21
    • 0002003685 scopus 로고
    • Expression and function of stress proteins in the ischemic heart
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Benjamin IJ, Williams RS. Expression and function of stress proteins in the ischemic heart. In: The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 1994:533-552.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 533-552
    • Benjamin, I.J.1    Williams, R.S.2
  • 22
    • 0002430625 scopus 로고
    • Postischemic stress response in brain
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Nowak TS, Abe H. Postischemic stress response in brain. In: The Biology of Heat Shock Proteins and Molecular Chaperones, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 1994:553-575.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 553-575
    • Nowak, T.S.1    Abe, H.2
  • 23
    • 3042637828 scopus 로고    scopus 로고
    • A small heat-shock protein, p26, from crustacean Artemia protects mammalian cells (Cos-1) against oxidative damage
    • Collins CH, Clegg JS. A small heat-shock protein, p26, from crustacean Artemia protects mammalian cells (Cos-1) against oxidative damage. Cell Biol Int 2004;28:449-455.
    • (2004) Cell Biol Int , vol.28 , pp. 449-455
    • Collins, C.H.1    Clegg, J.S.2
  • 24
    • 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, MacRae TH, et al. Purification, structure and molecular chaperone activity in vitro of Artemia p26, a small heat shock/α- crystallin protein. Eur J Biochem 1997;243:225-232.
    • (1997) Eur J Biochem , vol.243 , pp. 225-232
    • Liang, P.1    Amons, R.2    MacRae, T.H.3
  • 25
    • 0029862011 scopus 로고    scopus 로고
    • Dehydration, damage to cellular membranes, and heat-shock proteins in maize hybrids from different climates
    • Ristic Z, Williams G, Yang G, et al. Dehydration, damage to cellular membranes, and heat-shock proteins in maize hybrids from different climates. J Plant Physiol 1996;149:424-432.
    • (1996) J Plant Physiol , vol.149 , pp. 424-432
    • Ristic, Z.1    Williams, G.2    Yang, G.3
  • 26
    • 0031786304 scopus 로고    scopus 로고
    • Evidence of association between specific heat-shock protein(s) and the drought and heat tolerance phenotype in maize
    • Ristic Z, Yang G, Martin B, et al. Evidence of association between specific heat-shock protein(s) and the drought and heat tolerance phenotype in maize. J Plant Physiol 1998;153:497-505.
    • (1998) J Plant Physiol , vol.153 , pp. 497-505
    • Ristic, Z.1    Yang, G.2    Martin, B.3
  • 27
    • 1642298383 scopus 로고    scopus 로고
    • Desiccation and rehydration elicit distinct heat shock protein transcript responses in the flesh fly pupae
    • Hayward SAL, Rinehart JP, Denlinger DL. Desiccation and rehydration elicit distinct heat shock protein transcript responses in the flesh fly pupae. J Exp Biol 2004;207:963-971.
    • (2004) J Exp Biol , vol.207 , pp. 963-971
    • Hayward, S.A.L.1    Rinehart, J.P.2    Denlinger, D.L.3
  • 28
    • 0742322606 scopus 로고    scopus 로고
    • Molecular chaperones, stress resistance and development in Artemia franciscana
    • MacRae TH. Molecular chaperones, stress resistance and development in Artemia franciscana. Semin. Cell Dev Biol 2003;14:251-258.
    • (2003) Semin Cell Dev Biol , vol.14 , pp. 251-258
    • MacRae, T.H.1
  • 29
    • 0035745767 scopus 로고    scopus 로고
    • Nuclear p26, a small heat shock/alpha-crystallin protein, and its relationship to stress resistance in Artemia franciscana embryos
    • Willsie JK, Clegg JS. Nuclear p26, a small heat shock/alpha-crystallin protein, and its relationship to stress resistance in Artemia franciscana embryos. J Exp Biol 2001;204:2339-2350.
    • (2001) J Exp Biol , vol.204 , pp. 2339-2350
    • Willsie, J.K.1    Clegg, J.S.2
  • 30
    • 0031786750 scopus 로고    scopus 로고
    • Does the membrane's physical state control the expression of heat shock and other genes?
    • Vigh L, Maresca B, Harwood JL. Does the membrane's physical state control the expression of heat shock and other genes? Trends Biochem Sci 1998;23:369-374.
    • (1998) Trends Biochem Sci , vol.23 , pp. 369-374
    • Vigh, L.1    Maresca, B.2    Harwood, J.L.3
  • 31
    • 0037453103 scopus 로고    scopus 로고
    • Heat shock protein coinducers with no effect on protein denaturation specifically modulate the membrane lipid phase
    • Torok Z, Tsvetkova NM, Balogh G, et al. Heat shock protein coinducers with no effect on protein denaturation specifically modulate the membrane lipid phase. PNAS 2003;100:3131-3136.
    • (2003) PNAS , vol.100 , pp. 3131-3136
    • Torok, Z.1    Tsvetkova, N.M.2    Balogh, G.3
  • 32
    • 0023987021 scopus 로고
    • The effect of heat shock on primary cultures of brain capillary endothelium: Inhibition of assembly of zonulae occludentes and the synthesis of heat-shock proteins
    • Shivers RR, Pollock M, Bowman PD, et al. The effect of heat shock on primary cultures of brain capillary endothelium: inhibition of assembly of zonulae occludentes and the synthesis of heat-shock proteins. Eur J Cell Biol 1988;46:181-195.
    • (1988) Eur J Cell Biol , vol.46 , pp. 181-195
    • Shivers, R.R.1    Pollock, M.2    Bowman, P.D.3
  • 33
    • 0004198354 scopus 로고
    • New York: Academic Press
    • Sies H (Ed.). Oxidative Stress. New York: Academic Press; 1985.
    • (1985) Oxidative Stress
    • Sies, H.1
  • 34
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: Role in inflammatory disease and progression to cancer
    • Wiseman H, Halliwell B. Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochem J 1996;313:17-29.
    • (1996) Biochem J , vol.313 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2
  • 35
    • 0027408080 scopus 로고
    • Free radicals as mediators of tissue injury and disease
    • Kehrer JP. Free radicals as mediators of tissue injury and disease. Crit Rev Toxicol 1993;23:21-48.
    • (1993) Crit Rev Toxicol , vol.23 , pp. 21-48
    • Kehrer, J.P.1
  • 37
    • 5344279749 scopus 로고    scopus 로고
    • HSP25 protects skeletal muscle cells against oxidative stress
    • Escobedo J, Pucci AM, Koh TJ. HSP25 protects skeletal muscle cells against oxidative stress. Free Radic Biol Med 2004;37:1455-1462.
    • (2004) Free Radic Biol Med , vol.37 , pp. 1455-1462
    • Escobedo, J.1    Pucci, A.M.2    Koh, T.J.3
  • 38
    • 4444335833 scopus 로고    scopus 로고
    • Protective effect of heat shock protein 70 against oxidative stresses in human corneal fibroblasts
    • Kim YS, Han JA, Cheong TB, et al. Protective effect of heat shock protein 70 against oxidative stresses in human corneal fibroblasts. J Korean Med Sci 2004;19:591-597.
    • (2004) J Korean Med Sci , vol.19 , pp. 591-597
    • Kim, Y.S.1    Han, J.A.2    Cheong, T.B.3
  • 39
    • 13544267800 scopus 로고    scopus 로고
    • Heat shock pretreatment may protect against heat stroke induced circulatory shock and cerebral ischemia by reducing oxidative stress and energy depletion
    • Wang JL, Ke DS, Lin MT. Heat shock pretreatment may protect against heat stroke induced circulatory shock and cerebral ischemia by reducing oxidative stress and energy depletion. Shock 2005;23:161-167.
    • (2005) Shock , vol.23 , pp. 161-167
    • Wang, J.L.1    Ke, D.S.2    Lin, M.T.3
  • 40
    • 0347360092 scopus 로고    scopus 로고
    • Loading human mesenchymal stem cells with trehalose by fluid-phase endocytosis
    • Oliver A, Jamil K, Crowe JH, et al. Loading human mesenchymal stem cells with trehalose by fluid-phase endocytosis. Cell Preserv Technol 2004;2:35-49.
    • (2004) Cell Preserv Technol , vol.2 , pp. 35-49
    • Oliver, A.1    Jamil, K.2    Crowe, J.H.3
  • 41
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow E, Lane D. Antibodies. A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 1988;447.
    • (1988) Antibodies. A Laboratory Manual , pp. 447
    • Harlow, E.1    Lane, D.2
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli EK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, E.K.1
  • 43
    • 0034456451 scopus 로고    scopus 로고
    • Lipid phase separation correlates with activation in platelets during chilling
    • Tsvetkova NM, Walker NJ, Crowe JH, et al. Lipid phase separation correlates with activation in platelets during chilling. Mol Mem Biology 2000;17:209-218.
    • (2000) Mol Mem Biology , vol.17 , pp. 209-218
    • Tsvetkova, N.M.1    Walker, N.J.2    Crowe, J.H.3
  • 44
    • 0035888288 scopus 로고    scopus 로고
    • Ammonia-induced production of free radicals in primary cultures of rat astrocytes
    • Murthy CRK, Rama Rao KV, Bai G, et al. Ammonia-induced production of free radicals in primary cultures of rat astrocytes. J Neurosci Res 2001;66:282-288.
    • (2001) J Neurosci Res , vol.66 , pp. 282-288
    • Murthy, C.R.K.1    Rama Rao, K.V.2    Bai, G.3
  • 45
    • 0001361740 scopus 로고    scopus 로고
    • Ratio-fluorescence microscopy of lipid oxidation in living cells using C11-BODIPY(581/591)
    • Pap EH, Drummen GP, Winter VJ, et al. Ratio-fluorescence microscopy of lipid oxidation in living cells using C11-BODIPY(581/591). FEBS Lett 1999; 453:278-282.
    • (1999) FEBS Lett , vol.453 , pp. 278-282
    • Pap, E.H.1    Drummen, G.P.2    Winter, V.J.3
  • 46
    • 0035853131 scopus 로고    scopus 로고
    • Synechocystis HSP17 in an amphitropic protein that stabilizes heat-stresses membranes and binds denatured proteins for subsequent chaperone-mediated refolding
    • Torok Z, Goloubinoff P, Horvath I, et al. Synechocystis HSP17 in an amphitropic protein that stabilizes heat-stresses membranes and binds denatured proteins for subsequent chaperone-mediated refolding. PNAS 2001;98:3098-3103.
    • (2001) PNAS , vol.98 , pp. 3098-3103
    • Torok, Z.1    Goloubinoff, P.2    Horvath, I.3
  • 47
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002;295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 48
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • Young JC, Barrai JM, Hartl FU. More than folding: localized functions of cytosolic chaperones. Trends Biochem Sci 2003;28:541-547.
    • (2003) Trends Biochem Sci , vol.28 , pp. 541-547
    • Young, J.C.1    Barrai, J.M.2    Hartl, F.U.3
  • 49
    • 0018614808 scopus 로고
    • Membrane microenvironmental changes during activation of human blood platelets by thrombin. A study with a fluorescent probe
    • Nathan I, Fleischer G, Livne A, et al. Membrane microenvironmental changes during activation of human blood platelets by thrombin. A study with a fluorescent probe. J Biol Chem 1979;254:9822-9828.
    • (1979) J Biol Chem , vol.254 , pp. 9822-9828
    • Nathan, I.1    Fleischer, G.2    Livne, A.3
  • 50
    • 0023530117 scopus 로고
    • Oxidative stress and heat shock protein induction in human cells
    • Burdon RH, Gill VM, Rice-Evans C. Oxidative stress and heat shock protein induction in human cells. Free Radic Res Commun 1987;3:129-139.
    • (1987) Free Radic Res Commun , vol.3 , pp. 129-139
    • Burdon, R.H.1    Gill, V.M.2    Rice-Evans, C.3
  • 51
    • 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
    • Torok Z, Horvath I, Goloubinoff P, et al. Evidence for a lipochaperonin: association of active protein folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proc Natl Acad Sci 1997;94:2192-2197.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 2192-2197
    • Torok, Z.1    Horvath, I.2    Goloubinoff, P.3
  • 52
    • 0029947822 scopus 로고    scopus 로고
    • Mitochondria are selective targets for the protective effects of heat shock against oxidative injury
    • Polla BS, Kantengwa S, Francois D, et al. Mitochondria are selective targets for the protective effects of heat shock against oxidative injury. Proc Natl Acad Sci 1996;93:6458-6463.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 6458-6463
    • Polla, B.S.1    Kantengwa, S.2    Francois, D.3
  • 53
    • 0023950963 scopus 로고
    • Protein synthesis in perfused rat hearts after in vivo hyperthermia and in vitro cold ischemia
    • Currie RW. Protein synthesis in perfused rat hearts after in vivo hyperthermia and in vitro cold ischemia. Biochem Cell Biol 1988;66:13-19.
    • (1988) Biochem Cell Biol , vol.66 , pp. 13-19
    • Currie, R.W.1
  • 54
    • 0027773172 scopus 로고
    • The protective effect of heat stress against reperfusion arrhythmias in the rat
    • Steare SE, Yellon DM. The protective effect of heat stress against reperfusion arrhythmias in the rat. J Mol Cell Cardiol 1993;25:1471-1481.
    • (1993) J Mol Cell Cardiol , vol.25 , pp. 1471-1481
    • Steare, S.E.1    Yellon, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.