메뉴 건너뛰기




Volumn 274, Issue 6 43-6, 1998, Pages

Characterization of the Hsp110/SSE gene family response to hyperosmolality and other stresses

Author keywords

BiP binding protein; Heat shock; Heat stress protein 70; Kidney; Molecular chaperone; Stress tolerance

Indexed keywords

CADMIUM CHLORIDE; CHAPERONE; CYCLOHEXIMIDE; HEAT SHOCK PROTEIN; TUMOR NECROSIS FACTOR ALPHA; TUNICAMYCIN;

EID: 0031866430     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.1998.274.6.f1054     Document Type: Article
Times cited : (59)

References (45)
  • 1
    • 0027474909 scopus 로고
    • Activation of human heat shock genes is accompained by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1
    • Baler, R., G. Dahl, and R. Voellmy. Activation of human heat shock genes is accompained by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Mol. Cell. Biol. 13: 2486-2496, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2486-2496
    • Baler, R.1    Dahl, G.2    Voellmy, R.3
  • 2
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent peptides and denatured proteins: Hsp70 as a potential autoregulatory factor
    • Baler, R., W. J. Welch, and R. Voellmy. Heat shock gene regulation by nascent peptides and denatured proteins: hsp70 as a potential autoregulatory factor. J. Cell Biol. 117: 1151-1159, 1992.
    • (1992) J. Cell Biol. , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.J.2    Voellmy, R.3
  • 3
    • 0026623463 scopus 로고
    • Examining the function and regulation of hsp 70 in cells subjected to metabolic stress
    • Beckmann, R. P., M. Lovett, and W. J. Welch. Examining the function and regulation of hsp 70 in cells subjected to metabolic stress. J. Cell Biol. 117: 1137-1150, 1992.
    • (1992) J. Cell Biol. , vol.117 , pp. 1137-1150
    • Beckmann, R.P.1    Lovett, M.2    Welch, W.J.3
  • 4
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann, R. P., L. A. Mizzen, and W. J. Welch. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 248: 850-854, 1990.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 5
    • 0028894492 scopus 로고
    • Molecular basis of osmotic regulation
    • Renal Fluid Electrolyte Physiol. 37
    • Burg, M. B. Molecular basis of osmotic regulation. Am. J. Physiol. 268 (Renal Fluid Electrolyte Physiol. 37): F983-F996, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Burg, M.B.1
  • 6
    • 0030052105 scopus 로고    scopus 로고
    • The 170 kDa glucose regulated stress protein is a large Hsp70, HspllO-like protein of endoplasmic reticulum
    • Chen, X., D. Easton, H. J. Oh, D. S. Lee-Yoon, X. Liu, and J. Subjeck. The 170 kDa glucose regulated stress protein is a large Hsp70, HspllO-like protein of endoplasmic reticulum. FEBS Lett. 380: 68-72, 1996.
    • (1996) FEBS Lett. , vol.380 , pp. 68-72
    • Chen, X.1    Easton, D.2    Oh, H.J.3    Lee-Yoon, D.S.4    Liu, X.5    Subjeck, J.6
  • 7
    • 17344366901 scopus 로고
    • Transcripton factors and stress proteins in renal epithelial cell adaptation to hyperosmotic stress
    • edited by K. Strange. Boca Raton, FL: CRC
    • Cohen, D. M., and S. R. Gullans. Transcripton factors and stress proteins in renal epithelial cell adaptation to hyperosmotic stress. In: Cellular and Molecular Physiology of Cell Volume Regulation, edited by K. Strange. Boca Raton, FL: CRC, 1993, p. 363-372.
    • (1993) Cellular and Molecular Physiology of Cell Volume Regulation , pp. 363-372
    • Cohen, D.M.1    Gullans, S.R.2
  • 8
    • 0025946371 scopus 로고
    • Immediate early gene and HSP70 expression in hyperosmotic stress in MDCK cells
    • Cell Physiol. 30
    • Cohen, D. M., J. C. Wasserman, and S. R. Gullans. Immediate early gene and HSP70 expression in hyperosmotic stress in MDCK cells. Am. J. Physiol. 261 (Cell Physiol. 30): C594-C601, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • Cohen, D.M.1    Wasserman, J.C.2    Gullans, S.R.3
  • 9
    • 0027963178 scopus 로고
    • HSP70RY: Further characterization of a novel member of the Hsp70 protein family
    • Dyer, K. D., M. C. Lavigne, and H. F. Rosenberg. HSP70RY: Further characterization of a novel member of the Hsp70 protein family. Biochem. Biophys. Res. Commun. 203: 577-581, 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 577-581
    • Dyer, K.D.1    Lavigne, M.C.2    Rosenberg, H.F.3
  • 10
    • 0027181575 scopus 로고
    • Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5
    • Fathallah, D. M., D. Cherif, K. Dellagi, and M. A. Arnaout. Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5. J. Immunol. 151: 810-813, 1993.
    • (1993) J. Immunol. , vol.151 , pp. 810-813
    • Fathallah, D.M.1    Cherif, D.2    Dellagi, K.3    Arnaout, M.A.4
  • 11
    • 0027416845 scopus 로고
    • Sea urchin egg receptor for sperm: Sequence similarity of binding domain and hsp70
    • Foltz, K. R., J. S. Partin, and W. J. Lennarz. Sea urchin egg receptor for sperm: sequence similarity of binding domain and hsp70. Science 259: 1421-1425, 1993.
    • (1993) Science , vol.259 , pp. 1421-1425
    • Foltz, K.R.1    Partin, J.S.2    Lennarz, W.J.3
  • 12
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., E. Nimmesgern, K. Ohtsuka, and F. U. Hartl. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370: 111-117, 1994.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 13
    • 0028099856 scopus 로고
    • Genetic aspects os the hsp70 multigene family in vertebrates
    • Gunther, E., and L. Walter. Genetic aspects os the hsp70 multigene family in vertebrates. Experientia 50: 987-1001, 1994.
    • (1994) Experientia , vol.50 , pp. 987-1001
    • Gunther, E.1    Walter, L.2
  • 14
    • 0028110180 scopus 로고
    • Bip (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum
    • Haas, I. G. Bip (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum. Experientia. 50: 1012-1020, 1994.
    • (1994) Experientia , vol.50 , pp. 1012-1020
    • Haas, I.G.1
  • 15
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. Molecular chaperones in cellular protein folding. Nature 381: 571-579, 1996.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 16
    • 0027968222 scopus 로고
    • Coordinate and independent regulation of alfaB-crystallin and Hsp27 expression in response to physiological stress
    • Head, M. W., E. Corbin, and J. E. Goldman. Coordinate and independent regulation of alfaB-crystallin and Hsp27 expression in response to physiological stress. J. Cell. Physiol. 159: 41-50, 1994.
    • (1994) J. Cell. Physiol. , vol.159 , pp. 41-50
    • Head, M.W.1    Corbin, E.2    Goldman, J.E.3
  • 17
    • 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 temperatures
    • Kaneko, Y., H. Nishiyama, K. Nonoguchi, H. Higashitsuji, M. Kishishita, and J. Fujita. 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 temperatures. J. Biol. Chem. 272: 2640-2645, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2640-2645
    • Kaneko, Y.1    Nishiyama, H.2    Nonoguchi, K.3    Higashitsuji, H.4    Kishishita, M.5    Fujita, J.6
  • 18
    • 0026492552 scopus 로고
    • Effect of hyperosmolality on alkaline phosphatase and stress-reponse protein 27 of MCF-breast cancer cells
    • Kato, M., D. Brijlall, S. A. Adler, S. Kato, and F. Herz. Effect of hyperosmolality on alkaline phosphatase and stress-reponse protein 27 of MCF-breast cancer cells. Breast Cancer Res. Treat. 23: 241-249, 1992.
    • (1992) Breast Cancer Res. Treat. , vol.23 , pp. 241-249
    • Kato, M.1    Brijlall, D.2    Adler, S.A.3    Kato, S.4    Herz, F.5
  • 19
    • 17544366510 scopus 로고    scopus 로고
    • Osmotic stress protein 94 (Osp94): A new member of the Hsp110/ SSE gene subfamily
    • Kojima, R., J. Randall, B. M. Brenner, and S. R. Gullans. Osmotic stress protein 94 (Osp94): a new member of the Hsp110/ SSE gene subfamily. J. Biol. Chem. 271: 12327-12332, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12327-12332
    • Kojima, R.1    Randall, J.2    Brenner, B.M.3    Gullans, S.R.4
  • 20
    • 0029079045 scopus 로고
    • Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein
    • Lee-Yoon, D., D. Easton, M. Murawski, R. Burd, and J. R. Subjeck. Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein. J. Biol. Chem. 270: 15725-15733, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15725-15733
    • Lee-Yoon, D.1    Easton, D.2    Murawski, M.3    Burd, R.4    Subjeck, J.R.5
  • 21
    • 0028948241 scopus 로고
    • Induction of heat, freezing and salt tolerance by heat and salt shock in Sccharomyces cerevisiae
    • Lewis, J. G., R. P. Learmonth, and K. Watson. Induction of heat, freezing and salt tolerance by heat and salt shock in Sccharomyces cerevisiae. Microbiology 141: 687-694, 1995.
    • (1995) Microbiology , vol.141 , pp. 687-694
    • Lewis, J.G.1    Learmonth, R.P.2    Watson, K.3
  • 22
    • 0024430704 scopus 로고
    • Mutational analysis of the human HSP70 protein: Distinct domains for localization and adenosine triphosphate binding
    • Milarski, K. L., and R. I. Morimoto. Mutational analysis of the human HSP70 protein: distinct domains for localization and adenosine triphosphate binding. J. Cell Biol. 109: 1947-1962, 1989.
    • (1989) J. Cell Biol. , vol.109 , pp. 1947-1962
    • Milarski, K.L.1    Morimoto, R.I.2
  • 23
    • 0028848045 scopus 로고
    • Clinical implications of the stress response
    • Minowada, G., and W. J. Welch. Clinical implications of the stress response. J. Clin. Invest. 95: 3-12, 1995.
    • (1995) J. Clin. Invest. , vol.95 , pp. 3-12
    • Minowada, G.1    Welch, W.J.2
  • 25
    • 0001824746 scopus 로고
    • Progress and perspective on the biology of heat shock proteins and molecular chaperones
    • edited by R. I. Morimoto, A. Tissieres and C. Georgopoulos. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Morimoto, R. I., A. Tissieres, and C. Georgopoulos. Progress and perspective on the biology of heat shock proteins and molecular chaperones. In: The Biology of Heat Shock Proteins and Molecular Chaperones (1st ed.), edited by R. I. Morimoto, A. Tissieres and C. Georgopoulos. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1994, p. 1-30.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones (1st Ed.) , pp. 1-30
    • Morimoto, R.I.1    Tissieres, A.2    Georgopoulos, C.3
  • 26
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • Mosser, D. D., P. T. Kotzbauer, K. D. Sarge, and R. I. Morimoto. In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc. Natl. Acad. Sci. USA 87: 3748-3752, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 27
    • 0023815651 scopus 로고
    • Coordinate changes in heat shock clement-binding activity and hsp70 gene transcription rates in human cells
    • Mosser, D. D., N. G. Theodorakis, and R. I. Morimoto. Coordinate changes in heat shock clement-binding activity and hsp70 gene transcription rates in human cells. Mol. Cell. Biol. 8: 4736-4744, 1988.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4736-4744
    • Mosser, D.D.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 28
    • 0027445375 scopus 로고
    • Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family
    • Mukai, H., T. Kuno, H. Tanaka, D. Hirata, T. Miyakawa, and C. Tanaka. Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family. Gene 132: 57-66, 1993.
    • (1993) Gene , vol.132 , pp. 57-66
    • Mukai, H.1    Kuno, T.2    Tanaka, H.3    Hirata, D.4    Miyakawa, T.5    Tanaka, C.6
  • 29
    • 0029897874 scopus 로고    scopus 로고
    • Heat shock proteins hsp25, hsp60, hsp72, hsp73 in isoosmotic cortex and hyperosmotic medulla of rat kidney
    • Müller, E., W. Neuhofer, A. Ohno, S. Rucker, K. Thurau, and F. Beck. Heat shock proteins hsp25, hsp60, hsp72, hsp73 in isoosmotic cortex and hyperosmotic medulla of rat kidney. Pflügers Arch. 431: 608-617, 1996.
    • (1996) Pflügers Arch. , vol.431 , pp. 608-617
    • Müller, E.1    Neuhofer, W.2    Ohno, A.3    Rucker, S.4    Thurau, K.5    Beck, F.6
  • 30
    • 0027525215 scopus 로고
    • An osmotically tolerant inner medullary collecting duct cell line from an SV40 transgenic mouse
    • Renal Fluid Electrolyte Physiol. 34
    • Rauchman, M. I., S. K. Nigam, E. Delpire, and S. R. Gullans. An osmotically tolerant inner medullary collecting duct cell line from an SV40 transgenic mouse. Am. J. Physiol. 265 (Renal Fluid Electrolyte Physiol. 34): F416-F424, 1993.
    • (1993) Am. J. Physiol. , vol.265
    • Rauchman, M.I.1    Nigam, S.K.2    Delpire, E.3    Gullans, S.R.4
  • 31
    • 0030845194 scopus 로고    scopus 로고
    • Induction of molecular chaperones by hyperosmotic stress in mouse inner medullary collecting duct (mIMCD3) cells
    • Renal Physiol. 42
    • Rauchman, M. I., J. Pullman, and S. R. Gullans. Induction of molecular chaperones by hyperosmotic stress in mouse inner medullary collecting duct (mIMCD3) cells. Am. J. Physiol. 273 (Renal Physiol. 42): F9-F17, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Rauchman, M.I.1    Pullman, J.2    Gullans, S.R.3
  • 32
    • 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 abscence of stress
    • Sarge, K. D., S. P. Murphy, and R. I. Morimoto. 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 abscence of stress. Mol. Cell. Biol. 13: 1392-1407, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 33
    • 0027981731 scopus 로고
    • Induction of gene expression by heat shock versus osmotic stress
    • Renal Fluid Electrolyte Physiol. 36
    • Sheikh-Hamad, D., A. Garcia-Perez, J. D. Ferraris, E. M. Peters, and M. B. Burg. Induction of gene expression by heat shock versus osmotic stress. Am. J. Physiol. 267 (Renal Fluid Electrolyte Physiol. 36): F28-F34, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Sheikh-Hamad, D.1    Garcia-Perez, A.2    Ferraris, J.D.3    Peters, E.M.4    Burg, M.B.5
  • 34
    • 0027491078 scopus 로고
    • MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae
    • Shirayama, M., K. Kawakami, Y. Matsui, K. Tanaka, and A. Toh-e. MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae. Mol. Gen. Genet. 240: 323-332, 1993.
    • (1993) Mol. Gen. Genet. , vol.240 , pp. 323-332
    • Shirayama, M.1    Kawakami, K.2    Matsui, Y.3    Tanaka, K.4    Toh-e, A.5
  • 35
    • 0021033680 scopus 로고
    • Association between mammalian 110,000-dalton heat shock protein and nucleoli
    • Subjeck, J. R., T. Shyy, J. Shen, and R. J. Johnson. Association between mammalian 110,000-dalton heat shock protein and nucleoli. J. Cell Biol. 97: 1389-1395, 1983.
    • (1983) J. Cell Biol. , vol.97 , pp. 1389-1395
    • Subjeck, J.R.1    Shyy, T.2    Shen, J.3    Johnson, R.J.4
  • 37
    • 0030920718 scopus 로고    scopus 로고
    • Different thresholds in the responses of two heat shock transcription factors, HSF1 and HSF3
    • Tanabe, M., A. Nakai, Y. Kawazoe, and K. Nagata. Different thresholds in the responses of two heat shock transcription factors, HSF1 and HSF3. J. Biol. Chem. 272: 15389-15395, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15389-15395
    • Tanabe, M.1    Nakai, A.2    Kawazoe, Y.3    Nagata, K.4
  • 38
    • 0023707208 scopus 로고
    • Expression of heat shock and glucose-regulated genes: Differential effects of glucose starvation and hypertonicity
    • Tanaka, K., G. Jay, and K. Isselbacher. Expression of heat shock and glucose-regulated genes: differential effects of glucose starvation and hypertonicity. Biochim. Biophys. Acta 950: 138-146, 1988.
    • (1988) Biochim. Biophys. Acta , vol.950 , pp. 138-146
    • Tanaka, K.1    Jay, G.2    Isselbacher, K.3
  • 39
    • 0024559209 scopus 로고
    • Signal for induction of aldose reductase in renal medullary cells by high external NaCl
    • Cell Physiol. 25
    • Uchida, S., A. Garcia-Perez, H. Murphy, and M. B. Burg. Signal for induction of aldose reductase in renal medullary cells by high external NaCl. Am. J. Physiol. 256 (Cell Physiol. 25): C614-C620, 1989.
    • (1989) Am. J. Physiol. , vol.256
    • Uchida, S.1    Garcia-Perez, A.2    Murphy, H.3    Burg, M.B.4
  • 40
    • 0026662473 scopus 로고
    • Stress proteins and cross-protection by heat shock and salt stress in Bacillus subtilis
    • Volker, U., H. Mach, R. Schmid, and M. Hecker. Stress proteins and cross-protection by heat shock and salt stress in Bacillus subtilis. J. Gen. Microbiol. 138: 2125-2135, 1992.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2125-2135
    • Volker, U.1    Mach, H.2    Schmid, R.3    Hecker, M.4
  • 41
    • 0027433805 scopus 로고
    • Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding
    • Wang, T.-F., J.-H. Chang, and C. Wang. Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding. J. Biol. Chem. 268: 26049-26051, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26049-26051
    • Wang, T.-F.1    Chang, J.-H.2    Wang, C.3
  • 42
    • 0029823673 scopus 로고    scopus 로고
    • Prior heat stress enhances survival of renal epithelial cells after ATP depletion
    • Renal Fluid Electrolyte Physiol. 39
    • Wang, Y.-H., and S. C. Borkan. Prior heat stress enhances survival of renal epithelial cells after ATP depletion. Am. J. Physiol. 270 (Renal Fluid Electrolyte Physiol. 39): F1057-F1065, 1996.
    • (1996) Am. J. Physiol. , vol.270
    • Wang, Y.-H.1    Borkan, S.C.2
  • 44
    • 0030961030 scopus 로고    scopus 로고
    • Nitric oxide induces heat-shock protein 70 expression in vascular smooth muscle cells via activation of heat shock factor 1
    • Xu, Q., Y. Hu, R. Kleindienst, and G. Wick. Nitric oxide induces heat-shock protein 70 expression in vascular smooth muscle cells via activation of heat shock factor 1. J. Clin. Invest. 100: 1089-1097, 1997.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1089-1097
    • Xu, Q.1    Hu, Y.2    Kleindienst, R.3    Wick, G.4
  • 45
    • 0029564092 scopus 로고
    • Cloning and expression of murine high molecular mass heat shock proteins, Hsp105
    • Yasuda, K., A. Nakai, T. Hatayama, and K. Nagata. Cloning and expression of murine high molecular mass heat shock proteins, Hsp105. J. Biol. Chem. 270: 29718-29723, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29718-29723
    • Yasuda, K.1    Nakai, A.2    Hatayama, T.3    Nagata, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.