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Volumn 270, Issue 6 PART 2, 1996, Pages

Prior heat stress enhances survival of renal epithelial cells after ATP depletion

Author keywords

Adenosine 5' triphosphate depletion; Heat stress protein 70; Heat stress protein 72; Hyperthermia; Ischemia; Membrane injury; Metabolic stress

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYCLOHEXIMIDE; DEOXYGLUCOSE; DNA; GLUCOSE; HEAT SHOCK PROTEIN; LACTATE DEHYDROGENASE; SODIUM CYANIDE;

EID: 0029823673     PISSN: 00029513     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajprenal.1996.270.6.f1057     Document Type: Article
Times cited : (63)

References (40)
  • 1
    • 0023275774 scopus 로고
    • Change in energy reserves in different segments of the nephron during brief ischemia
    • Bastin, J., N. Cambon, M. Thompson, O. H. Lowry, and H. B. Burch. Change in energy reserves in different segments of the nephron during brief ischemia. Kidney Int. 31: 1239-1247, 1987.
    • (1987) Kidney Int. , vol.31 , pp. 1239-1247
    • Bastin, J.1    Cambon, N.2    Thompson, M.3    Lowry, O.H.4    Burch, H.B.5
  • 2
    • 0025303147 scopus 로고
    • Interaction of HSP 70 with newly synthesized proteins: Implications for protein folding and assembly events
    • Beckmann, R. P., L. A. Mizzen, and W. J. Welch. Interaction of HSP 70 with newly synthesized proteins: implications for protein folding and assembly events. Science Wash. DC 248: 850-854, 1990.
    • (1990) Science Wash. DC , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 3
    • 0026653034 scopus 로고
    • Induction of stress proteins in cultured myogenic cells: Molecular signals for the activation of heat shock transcription factor during ischemia
    • Benjamin, I. J., S. Horie, M. L. Greenberg, R. J. Alpern, and R. S. Williams. Induction of stress proteins in cultured myogenic cells: molecular signals for the activation of heat shock transcription factor during ischemia. J. Clin. Invest. 89: 1685-1689, 1992.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1685-1689
    • Benjamin, I.J.1    Horie, S.2    Greenberg, M.L.3    Alpern, R.J.4    Williams, R.S.5
  • 4
    • 0027489270 scopus 로고
    • Heat stress protein-associated cytoprotection of inner medullary collecting duct (IMCD) cells from rat kidney
    • Borkan, S. C., A. Emami, and J. H. Schwartz. Heat stress protein-associated cytoprotection of inner medullary collecting duct (IMCD) cells from rat kidney. Am. J. Physiol. 265 (Renal Fluid Electrolyte Physiol. 34): F333-F341; 1993.
    • (1993) Am. J. Physiol. 265 (Renal Fluid Electrolyte Physiol. 34) , vol.265
    • Borkan, S.C.1    Emami, A.2    Schwartz, J.H.3
  • 6
    • 0024341302 scopus 로고
    • Role of oxygen free radical species (OFRS) in mediating proximal tubular injury in an in vitro model of ischemia
    • Borkan, S. C., and J. H. Schwartz. Role of oxygen free radical species (OFRS) in mediating proximal tubular injury in an in vitro model of ischemia. Am. J. Physiol. 257 (Renal Fluid Electrolyte Physiol. 26): F114-F125, 1989.
    • (1989) Am. J. Physiol. 257 (Renal Fluid Electrolyte Physiol. 26) , vol.257
    • Borkan, S.C.1    Schwartz, J.H.2
  • 7
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H. L., S. R. Terlecky, C. P. Plant, and J. F. Dice. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science Wash. DC 246: 382-385, 1989.
    • (1989) Science Wash. DC , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 8
    • 0021685896 scopus 로고
    • Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth
    • Craig, E. A., and K. Jacobsen. Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth. Cell 28: 841-849, 1984.
    • (1984) Cell , vol.28 , pp. 841-849
    • Craig, E.A.1    Jacobsen, K.2
  • 9
    • 0028593362 scopus 로고
    • Characterization of a renal epithelial cell model of apoptosis using okadaic acid and the NRK-52E cell line
    • Davis, M. A., M. W. Smith, S. H. Chang, and B. J. Trump. Characterization of a renal epithelial cell model of apoptosis using okadaic acid and the NRK-52E cell line. Toxicol. Pathol. 22: 595-605, 1994.
    • (1994) Toxicol. Pathol. , vol.22 , pp. 595-605
    • Davis, M.A.1    Smith, M.W.2    Chang, S.H.3    Trump, B.J.4
  • 11
    • 0027237165 scopus 로고
    • Rise in heat-shock protein level confers tolerance to energy deprivation
    • Gabai, V. L., and A. E. Kabakov. Rise in heat-shock protein level confers tolerance to energy deprivation. FEBS Lett. 327: 247-250, 1993.
    • (1993) FEBS Lett. , vol.327 , pp. 247-250
    • Gabai, V.L.1    Kabakov, A.E.2
  • 12
    • 0026630990 scopus 로고
    • Are cytosolic components of the nuclear, ER and mitochondrial import apparatus functionally related?
    • Goldfarb, D. S. Are cytosolic components of the nuclear, ER and mitochondrial import apparatus functionally related? Cell 70: 185-188, 1982.
    • (1982) Cell , vol.70 , pp. 185-188
    • Goldfarb, D.S.1
  • 13
    • 0025777354 scopus 로고
    • Heat shock, stress proteins and proteotoxicity
    • Hightower, L. E. Heat shock, stress proteins and proteotoxicity. Cell 66: 191-197, 1991.
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 14
    • 0024290215 scopus 로고
    • Competitive inhibition of HSP 70 gene expression causes thermosensitivity
    • Johnston, R. N., and B. L. Kucey. Competitive inhibition of HSP 70 gene expression causes thermosensitivity. Science Wash. DC 241: 1551-1554; 1988.
    • (1988) Science Wash. DC , vol.241 , pp. 1551-1554
    • Johnston, R.N.1    Kucey, B.L.2
  • 15
    • 0027170257 scopus 로고
    • Protein aggregation as primary and characteristic cell reaction to various stresses
    • Kabakov, E., and V. L. Gabai. Protein aggregation as primary and characteristic cell reaction to various stresses. Experientia Basel 49: 706-710, 1993.
    • (1993) Experientia Basel , vol.49 , pp. 706-710
    • Kabakov, E.1    Gabai, V.L.2
  • 16
    • 0028271110 scopus 로고
    • Heat shock proteins maintain the viability of ATP-depleted cells: What is the mechanism?
    • Kabakov, E., and V. L. Gabai. Heat shock proteins maintain the viability of ATP-depleted cells: what is the mechanism? Trends Cell Biol. 4; 193-196, 1994.
    • (1994) Trends Cell Biol. , vol.4 , pp. 193-196
    • Kabakov, E.1    Gabai, V.L.2
  • 17
    • 0025039149 scopus 로고
    • Requirement for HSP 70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang, P. J., J. Ostermann, J. Shilling, W. Neupert, E. A. Craig, and N. Pfanner. Requirement for HSP 70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature Lond. 348;: 137-143, 1990.
    • (1990) Nature Lond. , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 18
    • 0025977175 scopus 로고
    • Heat shock proteins hsp 60 and hsp 70: Their roles in folding, assembly and membrane translocation of proteins
    • Langer, T., and W. Neupert. Heat shock proteins hsp 60 and hsp 70: their roles in folding, assembly and membrane translocation of proteins. Curr. Top. Microbiol. Immunol. 167; 3-30, 1991.
    • (1991) Curr. Top. Microbiol. Immunol. , vol.167 , pp. 3-30
    • Langer, T.1    Neupert, W.2
  • 19
    • 0026507980 scopus 로고
    • Heat shock protein hsp70 protects cells from thermal stress even after deletion of its ATP-binding domain
    • Li, G. C., L. Li, R. Y. Liu, M. Rehman, and W. M. Lee. Heat shock protein hsp70 protects cells from thermal stress even after deletion of its ATP-binding domain. Proc. Natl. Acad. Sci. USA 89: 2036-2040, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2036-2040
    • Li, G.C.1    Li, L.2    Liu, R.Y.3    Rehman, M.4    Lee, W.M.5
  • 20
    • 0027762495 scopus 로고
    • Li, Y., M. Chopp, Z. G. Zhang, R. L. Zhang, and J. H. Garcia. Neuronal survival is associated with 72-kDa heat shock protein expression after transient middle cerebral artery occlusion in the rat. J. Neural. Sci. 120; 187-194, 1993.
    • (1993) J. Neural. Sci. , vol.120 , pp. 187-194
    • Chopp, M.1    Zhang, Z.G.2    Zhang, R.L.3
  • 21
    • 0021319032 scopus 로고
    • Creatinine kinase expression and creatine phosphate accumulation are developmentally regulated during differentiation of mouse and human monocytes
    • Loike, J. D., V. F. Kozler, and S. C. Silverstein. Creatinine kinase expression and creatine phosphate accumulation are developmentally regulated during differentiation of mouse and human monocytes. J. Exp. Med. 159: 746-757, 1984.
    • (1984) J. Exp. Med. , vol.159 , pp. 746-757
    • Loike, J.D.1    Kozler, V.F.2    Silverstein, S.C.3
  • 22
    • 0027260315 scopus 로고
    • Heat shock protects neuronal cells from programmed cell death by apoptosis
    • Mailhos, C., M. K. Howard, and D. S. Latchman. Heat shock protects neuronal cells from programmed cell death by apoptosis. Neuroscience 55: 621-627, 1993.
    • (1993) Neuroscience , vol.55 , pp. 621-627
    • Mailhos, C.1    Howard, M.K.2    Latchman, D.S.3
  • 23
    • 0025062614 scopus 로고
    • Intracellular glutathione in the protection from anoxic injury in renal proximal tubules. J
    • Mandel, L. J., R. G. Schnellmann, and W. R. Jacobs. Intracellular glutathione in the protection from anoxic injury in renal proximal tubules. J. Clin. Invest. 85: 316-324, 1990.
    • (1990) Clin. Invest. , vol.85 , pp. 316-324
    • Mandel, L.J.1    Schnellmann, R.G.2    Jacobs, W.R.3
  • 24
    • 0028330146 scopus 로고
    • Myocardial protection after whole body heat stress in the rabbit is dependent on metablic substrate and is related to the amount of of inducible 70-kd heat stress protein
    • Marber, S., J. M. Walker, D. S. Latchman, and D. M. Yellon. Myocardial protection after whole body heat stress in the rabbit is dependent on metablic substrate and is related to the amount of of inducible 70-kd heat stress protein. J. Clin. Invest. 93: 1087-1094, 1994.
    • (1994) J. Clin. Invest. , vol.93 , pp. 1087-1094
    • Marber, S.1    Walker, J.M.2    Latchman, D.S.3    Yellon, D.M.4
  • 25
    • 0026702578 scopus 로고
    • Chaperonin cpn 60 from Escherichia coli protects the mitochondrial enzyme rhodanase against heat inactivation and supports folding at elevated temperatures
    • Mendoza, J. A., G. H. Lorimer, and P. M. Horowitz. Chaperonin cpn 60 from Escherichia coli protects the mitochondrial enzyme rhodanase against heat inactivation and supports folding at elevated temperatures. J. Biol. Chem. 367: 17631-17634, 1992.
    • (1992) J. Biol. Chem. , vol.367 , pp. 17631-17634
    • Mendoza, J.A.1    Lorimer, G.H.2    Horowitz, P.M.3
  • 26
    • 0028293462 scopus 로고
    • Expression of inducible stress protein 70 in rat myogenic cells confers protection against simulated ischemiainduced injury
    • Mestril, R., C. Shun-Hua, R. Sayen, K. O'Reilly, and W. H. Dillmann. Expression of inducible stress protein 70 in rat myogenic cells confers protection against simulated ischemiainduced injury. J. Clin. Invest. 93: 759-757, 1994.
    • (1994) J. Clin. Invest. , vol.93 , pp. 759-1757
    • Mestril, R.1    Shun-Hua, C.2    Sayen, R.3    O'Reilly, K.4    Dillmann, W.H.5
  • 27
    • 0028260658 scopus 로고
    • Characterization of denatured protein inducers of the heat shock (stress) response in Xenopus laevis oocytes
    • Mifflin, L. C., and R. E. Cohen. Characterization of denatured protein inducers of the heat shock (stress) response in Xenopus laevis oocytes. J. Biol. Chem. 269: 15710-15717, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15710-15717
    • Mifflin, L.C.1    Cohen, R.E.2
  • 28
    • 0022702374 scopus 로고
    • Effects of amiloride on thermosensitivity of Chinese hamster cells under neutral and acidic pH
    • Miyakoshi, J., W. Oda, M. Hirata, N. Fukuhori, and C. Inagaki. Effects of amiloride on thermosensitivity of Chinese hamster cells under neutral and acidic pH. Cancer Res. 46: 1840-1843, 1986.
    • (1986) Cancer Res. , vol.46 , pp. 1840-1843
    • Miyakoshi, J.1    Oda, W.2    Hirata, M.3    Fukuhori, N.4    Inagaki, C.5
  • 29
    • 0024110669 scopus 로고
    • A role for glyceraldehyde3-phosphate dehydrogenase in the development of thermotolernace in Xenopus laevis embyos
    • Nickells, R. W., and L. W. Browder. A role for glyceraldehyde3-phosphate dehydrogenase in the development of thermotolernace in Xenopus laevis embyos. J. Cell Biol. 107: 1901-1909, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 1901-1909
    • Nickells, R.W.1    Browder, L.W.2
  • 30
    • 0024361230 scopus 로고
    • Protein denaturation during heat shock and related stress
    • Nguyen, V. T., M. Morange, and O. Bensaude. Protein denaturation during heat shock and related stress. J. Biol Chem. 264:10487-10492, 1989.
    • (1989) J. Biol Chem. , vol.264 , pp. 10487-10492
    • Nguyen, V.T.1    Morange, M.2    Bensaude, O.3
  • 32
    • 0024293984 scopus 로고
    • Heat shock induced lethality in cells microinjected with antibodies specific forhsp 70
    • Riabowol, K., L. A. Mizzen, and W. J. Welch. Heat shock induced lethality in cells microinjected with antibodies specific forhsp 70. Science Wash. DC 242: 433-436, 1988.
    • (1988) Science Wash. DC , vol.242 , pp. 433-436
    • Riabowol, K.1    Mizzen, L.A.2    Welch, W.J.3
  • 33
    • 0026551591 scopus 로고
    • Morphologic, biochemical and molecular evidence of apoptosis during the reperfusion phase after brief periods of renal ischemia
    • Schumer, M., M. C. Colombel, I. S. Sawczuk, G. Globe, G, J. Connor, K. M. O'Toole, C. A. Olsson, G. J. Wise, and R. Buttyan. Morphologic, biochemical and molecular evidence of apoptosis during the reperfusion phase after brief periods of renal ischemia. Am J. Pathol. 140: 831-838, 1992.
    • (1992) Am J. Pathol. , vol.140 , pp. 831-838
    • Schumer, M.1    Colombel, M.C.2    Sawczuk, I.S.3    Globe, G.4    Connor, J.5    O'Toole, K.M.6    Olsson, C.A.7    Wise, G.J.8    Buttyan, R.9
  • 38
    • 0026034137 scopus 로고
    • Response of mammalian cells to metabolic stress: Changes in cell physiology and structure/function of stress proteins
    • Welch, W. J., H. S. Kang, P. Beckmann, and L. A. Mizzen. Response of mammalian cells to metabolic stress: changes in cell physiology and structure/function of stress proteins. Curr. Top. Microbiol. Immunol. 167: 31-55, 1991.
    • (1991) Curr. Top. Microbiol. Immunol. , vol.167 , pp. 31-55
    • Welch, W.J.1    Kang, H.S.2    Beckmann, P.3    Mizzen, L.A.4
  • 39
    • 0022976650 scopus 로고
    • Cellular and biochemical events in mammalian cells during and after recovery from physiologic stress
    • Welch, W. J., and J. P. Suhan. Cellular and biochemical events in mammalian cells during and after recovery from physiologic stress. J. Cell Biol. 103: 2035-2052, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 2035-2052
    • Welch, W.J.1    Suhan, J.P.2
  • 40
    • 0027203476 scopus 로고
    • Human heat stress protein 70 (hsp 70) protects murine cells from injury during metabolic stress
    • Williams, R. S., J. A. Thomas, M. Fina, Z. German, and I. J. Benjamin. Human heat stress protein 70 (hsp 70) protects murine cells from injury during metabolic stress. J. Clin. Invest. 92: 503-508, 1993.
    • (1993) J. Clin. Invest. , vol.92 , pp. 503-508
    • Williams, R.S.1    Thomas, J.A.2    Fina, M.3    German, Z.4    Benjamin, I.J.5


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