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Volumn 81, Issue 4, 2001, Pages 1461-1497

Heat shock proteins and cardiovascular pathophysiology

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN;

EID: 0034784780     PISSN: 00319333     EISSN: None     Source Type: Journal    
DOI: 10.1152/physrev.2001.81.4.1461     Document Type: Review
Times cited : (344)

References (456)
  • 21
    • 0027474909 scopus 로고
    • Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1
    • (1993) Mol Cell Biol , vol.13 , pp. 2486-2496
    • Baler, R.1    Dahl, G.2    Voellmy, R.3
  • 22
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins: Hsp70 as a potential autoregulatory factor
    • (1992) J Cell Biol , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.2    Voellmy, R.3
  • 77
    • 0023854047 scopus 로고
    • Evidence suggesting that the two isoforms of heme oxygenase are products of different genes
    • (1988) J Biol Chem , vol.263 , pp. 3348-3353
    • Cruse, I.1    Maines, M.D.2
  • 80
    • 0023231632 scopus 로고
    • Effects of ischemia and reperfusion temperature on the synthesis of stress-induced (heat shock) proteins in isolated and perfused rat hearts
    • (1987) J Mol Cell Cardiol , vol.19 , pp. 795-808
    • Currie, R.W.1
  • 81
    • 0023950963 scopus 로고
    • Protein synthesis in perfused rat hearts after in vivo hyperthermia and in vitro cold ischemia
    • (1988) Biochem Cell Biol , vol.66 , pp. 13-19
    • Currie, R.W.1
  • 82
    • 0025072049 scopus 로고
    • Improved post-ischemic ventricular recovery in the absence of changes in energy metabolism in working rat hearts following heat-shock
    • (1990) J Mol Cell Cardiol , vol.22 , pp. 631-636
    • Currie, R.W.1    Karmazyn, M.2
  • 88
    • 0024431720 scopus 로고
    • Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins
    • (1989) J Biol Chem , vol.264 , pp. 18019-18023
    • Dang, C.V.1    Lee, W.M.F.2
  • 119
    • 0028251043 scopus 로고
    • HSP70: A multi-gene, multi-structure, multi-function family with potential Clinical applications
    • (1994) Experientia , vol.50 , pp. 979-986
    • Feige, U.1    Polla, B.S.2
  • 125
    • 0030844524 scopus 로고    scopus 로고
    • Protein folding. The difference with prokaryotes
    • (1997) Nature , vol.388 , pp. 329-330
    • Gething, M.-J.1
  • 128
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • (1995) Cell , vol.80 , pp. 11-14
    • Glick, B.S.1
  • 132
    • 0022541510 scopus 로고
    • Purification and initial characterization of the 71-kilodalton rat heat shock protein and its cognate as fatty acid binding proteins
    • (1986) Biochemistry , vol.25 , pp. 3231-3239
    • Guidon P.T., Jr.1    Hightower, L.E.2
  • 133
    • 0028110180 scopus 로고
    • BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum
    • (1994) Experientia , vol.50 , pp. 1012-1020
    • Hass, I.G.1
  • 152
    • 0019494188 scopus 로고
    • Cellular responses to stress. Comparison of a family of 71-73 kilodalton proteins rapidly synthesized in rat tissue slices and canavanine-treated cells in culture
    • (1981) J Cell Physiol , vol.108 , pp. 261-275
    • Hightower, L.E.1    White, F.P.2
  • 153
    • 0000028642 scopus 로고
    • Preferential synthesis of rat heat-shock and glucose-regulated proteins in stressed cardiovascular cells
    • edited by Schlesinger MJ, Ashburner M, and Tissières A. Cold Spring Harbor, NY: Cold Spring Harbor
    • (1982) Heat Shock: From Bacteria to Man , pp. 369-377
    • Hightower, L.E.1    White, F.P.2
  • 156
    • 0028321786 scopus 로고
    • A short element required for turning off heat shock transcription factor: Evidence that phosphorylation enhances deactivation
    • (1994) EMBO J , vol.13 , pp. 2617-2624
    • Hoj, A.1    Jacobsen, B.K.2
  • 165
    • 0026670678 scopus 로고
    • Heat-shock protein induction in adriamycin and picornavirus-infected cardiocytes
    • (1992) Lab Invest , vol.67 , pp. 218-224
    • Huber, S.A.1
  • 168
    • 0025237397 scopus 로고
    • Characterization and sequence of a mouse hsp70 gene and its expression in mouse cell lines
    • (1990) Gene , vol.87 , pp. 199-204
    • Hunt, C.1    Calderwood, S.2
  • 171
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/HSP27 pathway in vascular endothelial cells
    • (1997) Circ Res , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 176
    • 0029932270 scopus 로고    scopus 로고
    • Age-related changes before and after imposition of hemodynamic stress in the mammalian heart
    • (1996) Life Sci , vol.58 , pp. 1601-1614
    • Isoyama, S.1
  • 202
    • 0033106368 scopus 로고    scopus 로고
    • Mutation of amino acids 246-251 alters nuclear accumulation of human heat shock protein (HSP) 72 with stress, but does not reduce viability
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 523-532
    • Knowlton, A.A.1
  • 225
    • 0031030098 scopus 로고    scopus 로고
    • A 16-kDa protein functions as a new regulatory protein for Hsc70 molecular chaperone and is identified as a member of the Nm23/nucleoside diphosphate kinase family
    • (1997) J Biol Chem , vol.272 , pp. 2607-2614
    • Leung, S.-M.1    Hightower, L.E.2
  • 228
    • 0022327491 scopus 로고
    • Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein
    • (1985) EMBO J , vol.4 , pp. 3137-3143
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 232
    • 0028958828 scopus 로고
    • Effects of expressing human Hsp70 and its deletion derivatives on heat killing and on RNA and protein synthesis
    • (1995) Exp Cell Res , vol.217 , pp. 460-468
    • Li, L.1    Shen, G.2    Li, G.C.3
  • 238
    • 0026734257 scopus 로고
    • Expression of human hsp70 in rat fibroblasts enhances cell survival and facilitates recovery from translational and transcriptional inhibition following heat shock
    • (1992) Cancer Res , vol.52 , pp. 3667-3673
    • Liu, R.Y.1    Li, X.2    Li, L.3    Li, G.C.4
  • 242
    • 0032555355 scopus 로고    scopus 로고
    • Protein phosphatase inhibitors and heat preconditioning prevent Hsp27 dephosphorylation, F-actin disruption and deterioration of morphology in ATP-depleted endothelial cells
    • (1998) FEBS Lett , vol.433 , pp. 294-300
    • Loktionova, S.A.1    Kabakov, A.B.2
  • 247
  • 249
    • 0029188297 scopus 로고
    • Heat-shock proteins and molecular chaperones: Implications for pathogenesis, diagnostics, and therapeutics
    • (1995) Int J Clin Lab Res , vol.25 , pp. 59-70
    • Macario, A.J.L.1
  • 255
    • 0026092493 scopus 로고
    • Myocardial stunning and hibernation: The physiology behind the colloquialisms
    • (1901) Circulation , vol.83 , pp. 681-688
    • Marban, E.1
  • 270
    • 0029122013 scopus 로고
    • Myocardial self-preservation: Absence of heat shock factor activation and heat shock proteins 70 mRNA accumulation in the human heart during cardiac surgery
    • (1995) J Cardiac Surg , vol.10 , pp. 400-406
    • McGrath, L.B.1    Locke, M.2
  • 285
    • 0024430704 scopus 로고
    • Mutational analysis of the human HSP70 protein: Distinct domains for nucleolar localization and adenosine triphosphate binding
    • (1989) J Cell Biol , vol.109 , pp. 1947-1962
    • Milarski, K.L.1    Morimoto, R.I.2
  • 291
    • 0027522356 scopus 로고
    • Cells in stress: Transcriptional activation of heat shock genes
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.I.1
  • 300
    • 0027475243 scopus 로고
    • HSP90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl propyl isomerases
    • (1993) J Biol Chem , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 301
    • 0027406535 scopus 로고
    • Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway
    • (1993) Mol Cell Biol , vol.13 , pp. 1983-1997
    • Nakai, A.1    Morimoto, R.I.2
  • 306
  • 315
    • 0027398633 scopus 로고
    • Identification of a nuclear protein that constitutively recognizes the sequence containing a heat-shock element. Its binding properties and possible function modulating heat-shock induction of the rat heme oxygenase gene
    • (1993) Eur J Biochem , vol.212 , pp. 167-175
    • Okinaga, S.1    Shibahara, S.2
  • 321
    • 0028098051 scopus 로고
    • Protection of the heart by ischaemic preconditioning: Mechanisms and possibilities for pharmacological exploitation
    • (1994) Trends Pharmacol Sci , vol.15 , pp. 19-25
    • Parratt, J.R.1
  • 328
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • (1993) J Biol Chem , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 339
    • 34250561475 scopus 로고
    • A new puffing pattern induced by a temperature shock and DNP in Drosophila
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.M.1
  • 344
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothman, J.1
  • 352
    • 0027461364 scopus 로고
    • Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress
    • (1993) Mol Cell Biol , vol.13 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 359
    • 0030031771 scopus 로고    scopus 로고
    • Coexpression of heat shock protein 60 and intercellular-adhesion molecule-1 is related to increased adhesion of monocytes and T-cells to aortic endothelium of rats in response to endotoxin
    • (1996) Lab Invest , vol.74 , pp. 241-252
    • Seitz, C.S.1    Kleindienst, R.2    Xu, Q.3    Wick, G.4
  • 372
    • 0023316845 scopus 로고
    • Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells
    • (1987) EMBO J , vol.6 , pp. 993-998
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 375
    • 85047675260 scopus 로고
    • Increased endogenous catalase activity caused by heat stress does not protect the isolated rat heart against exogenous hydrogen peroxide
    • (1994) Cardiovasc Res , vol.28 , pp. 1096-1101
    • Steare, S.E.1    Yellon, D.M.2
  • 376
    • 0032519758 scopus 로고    scopus 로고
    • The nuclear factor interleukin-6 (NF-IL6) and signal transducer and activator of transcription-3 (STAT-3) signaling pathways co-operate to mediate the activation of the hsp90β gene by interleukin-6 but have opposite effects on its inducibility by heat shock
    • (1998) Biochem J , vol.330 , pp. 189-195
    • Stephanou, A.1    Isenberg, D.A.2    Akira, S.3    Kishimoto, T.4    Latchman, D.S.5
  • 399
    • 0022441522 scopus 로고
    • Role of catalase in metabolism of hydrogen peroxide
    • (1986) FEBS Lett , vol.202 , pp. 137-140
    • Thayer, W.S.1
  • 400
    • 0023890443 scopus 로고
    • Human gene encoding the 78.000-dalton glucose-regulated protein and its pseudogene: Structure, conservation, and regulation
    • (1988) DNA , vol.7 , pp. 275-286
    • Ting, J.1    Lee, A.S.2
  • 403
    • 0027157056 scopus 로고
    • New model for 70 kDa heat-shock proteins' potential mechanisms of function
    • (1993) FEBS Lett , vol.323 , pp. 1-3
    • Tsang, T.C.1
  • 416
    • 0021398211 scopus 로고
    • HSP70: Nuclear concentration during environmental stress and cytoplasmic storage during recovery
    • (1984) Cell , vol.36 , pp. 655-662
    • Velazquez, J.M.1    Lindquist, S.2
  • 421
    • 0032102443 scopus 로고    scopus 로고
    • Rabbit cardiac and skeletal muscle myocytes differ in constitutive and inducible expression of the glucose-regulated protein GRP94
    • (1998) Biochem J , vol.332 , pp. 351-359
    • Vitadello, M.1    Colpo, P.2    Gorza, L.3
  • 429
    • 0021908896 scopus 로고
    • Phorbol ester calcium ionophore, or serum added to quiescent rat embryo fibroblast cells all result in the elevated phosphorylation of two 28,000-dalton mammalian stress proteins
    • (1985) J Biol Chem , vol.1985 , pp. 3058-3062
    • Welch, W.J.1
  • 430
    • 0026460892 scopus 로고
    • Mammalian stress response: Cell physiology, structure/ function of stress proteins, and implications for medicine and disease
    • (1992) Physiol Rev , vol.72 , pp. 1063-1081
    • Welch, W.J.1
  • 433
  • 434
    • 0022379715 scopus 로고
    • Morphological study of the mammalian stress response: Characterization of changes in cytoplasmic organelle, cytoskeleton, and nucleoli, and the appearance of intranuclear actin filaments in rat fibroblasts after heat shock treatment
    • (1985) J Biol Chem , vol.101 , pp. 1198-1211
    • Welch, W.J.1    Suhan, J.P.2
  • 437
    • 0023924167 scopus 로고
    • Characterization of the thermotolerant cell. Effects of the intracellular distribution of heat-shock protein 70, intermediate filamants, and small nuclear ribonucleoprotein complexes
    • (1988) J Cell Biol , vol.106 , pp. 1117-1130
    • Welch, W.W.1    Mizzen, L.A.2
  • 441
    • 0031055277 scopus 로고    scopus 로고
    • Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active trimers
    • (1997) J Biol Chem , vol.272 , pp. 4094-4102
    • Xia, W.1    Voellmy, R.2
  • 442
  • 446
    • 0030229050 scopus 로고    scopus 로고
    • The role of heat shock proteins in protection and pathophysiology of the arterial wall
    • (1996) Mol Med Today , vol.2 , pp. 372-379
    • Xu, Q.1    Wick, G.2


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