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Volumn 274, Issue 6 PART 2, 1998, Pages

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

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EID: 33746668686     PISSN: 00029513     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (45)
  • 1
    • 0027474909 scopus 로고    scopus 로고
    • 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
    • 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.
    • Mol. Cell. Biol. 13:2486-2496,1993.
    • Baler, R.1
  • 2
    • 0026750001 scopus 로고    scopus 로고
    • W. J. Welch, and R. Voellmy. Heat shock gene regulation by nascent peptides and denatured proteins: HspTO as a potential autoregulatory factor
    • Baler, R. W. J. Welch, and R. Voellmy. Heat shock gene regulation by nascent peptides and denatured proteins: hspTO as a potential autoregulatory factor. J. Cell Biol. 117: 1151-1159, 1992.
    • J. Cell Biol. 117: 1151-1159, 1992.
    • Baler, R.1
  • 3
    • 0026623463 scopus 로고    scopus 로고
    • M. Lovett, and W. J. Welch. Examining the function and regulation of hsp 70 in cells subjected to metabolic stress. J
    • 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.
    • Cell Biol. 117:1137-1150,1992.
    • Beckmann, R.P.1
  • 4
    • 0025303147 scopus 로고    scopus 로고
    • L. A. Mizzen, and W. J. Welch. 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.
    • Science 248:850-854,1990.
    • Beckmann, R.P.1
  • 6
    • 0030052105 scopus 로고    scopus 로고
    • 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
    • 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. FEES Lett. 380:68-72,1996.
    • FEES Lett. 380:68-72,1996.
    • Chen, X.1
  • 8
    • 0025946371 scopus 로고    scopus 로고
    • J. C. Wassermaii, and S. R. Gullans. Immediate early gene and HSP70 expression in hyperosmotic stress in MDCK cells
    • Cohen, D. M. J. C. Wassermaii, 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.
    • Am. J. Physiol. 261 (Cell Physiol. 30): C594-C601, 1991.
    • Cohen, D.M.1
  • 9
    • 0027963178 scopus 로고    scopus 로고
    • M. C. Lavigne, and H. F. Rosenberg. 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.
    • Biochem. Biophys. Res. Commun. 203:577-581,1994.
    • Dyer, K.D.1
  • 10
    • 0027181575 scopus 로고    scopus 로고
    • 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
    • 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.
    • J. Immunol. 151: 810-813, 1993.
    • Fathallah, D.M.1
  • 11
    • 0027416845 scopus 로고    scopus 로고
    • J. S. Partin, and W. J. Lennarz. 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.
    • Science 259:1421-1425,1993.
    • Foltz, K.R.1
  • 12
    • 0028361309 scopus 로고    scopus 로고
    • E. Nimmesgern, K. Ohtsuka, and F. U. Hartl. 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.
    • Nature 370: 111-117, 1994.
    • Frydman, J.1
  • 13
    • 0028099856 scopus 로고    scopus 로고
    • And L. Walter. Genetic aspects os the hspTO multigene family in vertebrates
    • Günther, E. and L. Walter. Genetic aspects os the hspTO multigene family in vertebrates. Experientia 50:987-1001,1994.
    • Experientia 50:987-1001,1994.
    • Günther, E.1
  • 14
    • 0028110180 scopus 로고    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.
    • Experientia 50:1012-1020,1994.
    • 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.
    • Nature 381:571-579,1996.
    • Hartl, F.U.1
  • 16
    • 0027968222 scopus 로고    scopus 로고
    • E. Corbin, and J. E. Goldman. 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.
    • J. Cell. Physiol. 159: 41-50, 1994.
    • Head, M.W.1
  • 17
    • 0031017476 scopus 로고    scopus 로고
    • H. Nishiyama, K. Nonoguchi, H. Higashitsuji, M. Kishishita, and J. Fujita. A novel hspllO-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 hspllO-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.
    • J. Biol. Chem. 272:2640-2645,1997.
    • Kaneko, Y.1
  • 18
    • 0026492552 scopus 로고    scopus 로고
    • D. Brylall, S. A. Adler, S. Kato, and F. Herz. Effect of hyperosmolality on alkaline phosphatase and stress-réponse protein 27 of MCF-breast cancer cells
    • Kato, M. D. Brylall, S. A. Adler, S. Kato, and F. Herz. Effect of hyperosmolality on alkaline phosphatase and stress-réponse protein 27 of MCF-breast cancer cells. Breast Cancer Res. Treat. 23: 241-249,1992.
    • Breast Cancer Res. Treat. 23: 241-249,1992.
    • Kato, M.1
  • 19
    • 17544366510 scopus 로고    scopus 로고
    • J. Randall, B. M. Brenner, and S. R. Gullans. Osmotic stress protein 94 (Osp94): A new member of the HspllO/ SSE gene subfamily
    • Kojima, R. J. Randall, B. M. Brenner, and S. R. Gullans. Osmotic stress protein 94 (Osp94): a new member of the HspllO/ SSE gene subfamily. J. Biol. Chem. 271:12327-12332,1996.
    • J. Biol. Chem. 271:12327-12332,1996.
    • Kojima, R.1
  • 20
    • 85177159787 scopus 로고    scopus 로고
    • 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
    • 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.
    • J. Biol. Chem. 270:15725-15733,1995.
    • Lee-Yoon, D.1
  • 21
    • 0028948241 scopus 로고    scopus 로고
    • R. P. Learmonth, and K. Watson. Induction of heat, freezing and salt tolerance by heat and salt shock in Sccharo'myces cerevisiae
    • Lewis, J. G. R. P. Learmonth, and K. Watson. Induction of heat, freezing and salt tolerance by heat and salt shock in Sccharo'myces cerevisiae. Microbiology 141: 687-694,1995.
    • Microbiology 141: 687-694,1995.
    • Lewis, J.G.1
  • 22
    • 0024430704 scopus 로고    scopus 로고
    • And R. I. Morimoto. 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.
    • J. Cell Biol. 109: 1947-1962, 1989.
    • Milarski, K.L.1
  • 23
    • 0028848045 scopus 로고    scopus 로고
    • And W. J. Welch. Clinical implications of the stress response
    • 23.' Minowada, G. and W. J. Welch. Clinical implications of the stress response. J. Clin. Invest. 95:3-12,1995.
    • J. Clin. Invest. 95:3-12,1995.
    • Minowada, G.1
  • 26
    • 0025300038 scopus 로고    scopus 로고
    • 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
    • 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. Sei. USA 87: 3748-3752, 1990.
    • Proc. Natl. Acad. Sei. USA 87: 3748-3752, 1990.
    • Mosser, D.D.1
  • 27
    • 0023815651 scopus 로고    scopus 로고
    • N. G. Theodorakis, and R. I. Morimoto. Coordinate changes in heat shock element-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 element-binding activity and hsp70 gene transcription rates in human cells. Mol. Cell. Biol. 8: 4736-4744,1988.
    • Mol. Cell. Biol. 8: 4736-4744,1988.
    • Mosser, D.D.1
  • 28
    • 0027445375 scopus 로고    scopus 로고
    • T. Kuno, H. Tanaka, D. Hirata, T. Miyakawa, and C. Tanaka. Isolation and characterization of SSEl'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 SSEl'and SSE2, new members of the yeast HSP70 multigene family. Gene 132: : 57-66,1993.
    • Gene 132: : 57-66,1993.
    • Mukai, H.1
  • 29
    • 0029897874 scopus 로고    scopus 로고
    • 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
    • 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.
    • Pflügers Arch. 431:608-617,1996.
    • Müller, E.1
  • 30
    • 0027525215 scopus 로고    scopus 로고
    • S. K. Nigam, E. Delpire, and S. R. Gullans. An osmotically tolerant inner medullary collecting duct cell line from an SV40 transgenic mouse
    • 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.
    • Am. J. Physiol. 265 (Renal Fluid Electrolyte Physiol. 34): F416-F424,1993.
    • Rauchman, M.I.1
  • 31
    • 0030845194 scopus 로고    scopus 로고
    • J. Pullman, and S. R. Gullans. Induction of molecular chaperones by hyperosmotic stress in mouse inner medullary collecting duct (mIMCDS) cells
    • Rauchman, M. I. J. Pullman, and S. R. Gullans. Induction of molecular chaperones by hyperosmotic stress in mouse inner medullary collecting duct (mIMCDS) cells. Am. J. Physiol. 273 (Renal Physiol. 42): F9-F17,1997. i
    • Am. J. Physiol. 273 (Renal Physiol. 42): F9-F17,1997. i
    • Rauchman, M.I.1
  • 32
    • 0027461364 scopus 로고    scopus 로고
    • 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
    • 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.
    • Mol. Cell. Biol. 13:1392-1407,1993.
    • Sarge, K.D.1
  • 33
    • 0027981731 scopus 로고    scopus 로고
    • A. Garcia-Perez, J. D. Ferraris, E. M. Peters, and M. B. Burg. Induction of gene expression by heat shock versus osmotic stress
    • 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.
    • Am. J. Physiol. 267 (Renal Fluid Electrolyte Physiol. 36): F28-F34,1994.
    • Sheikh-Hamad, D.1
  • 34
    • 0027491078 scopus 로고    scopus 로고
    • 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
    • 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.
    • Mol. Gen. Genet. 240: 323-332,1993.
    • Shirayama, M.1
  • 35
    • 0021033680 scopus 로고    scopus 로고
    • T. Shyy, J. Shen, and R. J. Johnson. 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.
    • J. Cell Biol. 97:1389-1395,1983.
    • Subjeck, J.R.1
  • 36
    • 0026577362 scopus 로고    scopus 로고
    • Z. Du, K. Thomas, R. Wilson, L. Hillier, R. Staden, N. Halloran, P. Green, J. Thierry-Mieg, L. Qui, S. Dear, A. Coulson, M. Craxton, R. Durbin, M. Berks, M. Metzstein, T. Hawkins, R. Ainscough, and R. Waterston. the C
    • Sulston, J. Z. Du, K. Thomas, R. Wilson, L. Hillier, R. Staden, N. Halloran, P. Green, J. Thierry-Mieg, L. Qui, S. Dear, A. Coulson, M. Craxton, R. Durbin, M. Berks, M. Metzstein, T. Hawkins, R. Ainscough, and R. Waterston. The C. elegans genome sequencing project: a beginning. Nature 356:37-41,1992.
    • Elegans Genome Sequencing Project: A Beginning. Nature 356:37-41,1992.
    • Sulston, J.1
  • 37
    • 0030920718 scopus 로고    scopus 로고
    • A. Nakai, Y. Kawazoe, and K. Nagata. 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.
    • J. Biol. Chem.272:15389-15395,1997.
    • Tanabe, M.1
  • 38
    • 0023707208 scopus 로고    scopus 로고
    • G. Jay, and K. Isselbacher. 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: 138146,1988.
    • Biochim. Biophys. Acta 950: 138146,1988.
    • Tanaka, K.1
  • 39
    • 33746671509 scopus 로고    scopus 로고
    • A. Garcia-Perez, H. Murphy, and M. B. Burg. Signal for induction of aldose reductase in renal medullary cells by high external NaCl
    • 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.
    • Am. J. Physiol. 256 (Cell Physiol. 25): C614-C620,1989.
    • Uchida, S.1
  • 40
    • 0026662473 scopus 로고    scopus 로고
    • H. Mach, R. Schmid, and M. Hecker. Stress proteins and cross-protection by heat shock and salt stress in
    • 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.
    • Bacillus Subtilis. J. Gen. Microbiol. 138:2125-2135,1992.
    • Volker, U.1
  • 41
    • 0027433805 scopus 로고    scopus 로고
    • 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
    • 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.
    • J. Biol. Chem. 268:26049-26051,1993.
    • Wang, T.-F.1
  • 43
    • 0028295681 scopus 로고    scopus 로고
    • Mb of contiguous nucleotide sequence from chromosome III of C. elegans
    • R. Ainscough, K. Anderson, C. Baynes, M. Berks, J. Bonfield, J. Burton, M. Connell, T. Copsey, J. Cooper, A. Coulson, M. Craxton, D. S. Z. Du, R. Durbin, A. Favello, A. Fraser, A. Fulton, A. Gardner, P. Green, T. Hawkins, L. Hillier, M. Jier, L. Johnston, M. Jones, J. Kershaw, J. Kirsten, M. Laisster, P. Latreille, J. Lightning, B. Mortimore, M. O'Callaghan, J. Parsons, C. Percy, L. Rifken, A, Roopra, D. Saunders, R. Shownkeen, M. Sims, N. Smaldon, A. Smith, M. Smith, E. Sonnhammer.'R. Staden, J. Sulston, J. Thierry-Mieg, K. Thomas, M. Vaudin, K. Vaughan, R. Waterson, A. Watson, L. Weinstock, L. Wilkinstock, J. Wilkinson-Sproat, and P. Wohldman. 2.2
    • Wilson, R. R. Ainscough, K. Anderson, C. Baynes, M. Berks, J. Bonfield, J. Burton, M. Connell, T. Copsey, J. Cooper, A. Coulson, M. Craxton, D. S. Z. Du, R. Durbin, A. Favello, A. Fraser, A. Fulton, A. Gardner, P. Green, T. Hawkins, L. Hillier, M. Jier, L. Johnston, M. Jones, J. Kershaw, J. Kirsten, M. Laisster, P. Latreille, J. Lightning, B. Mortimore, M. O'Callaghan, J. Parsons, C. Percy, L. Rifken, A, Roopra, D. Saunders, R. Shownkeen, M. Sims, N. Smaldon, A. Smith, M. Smith, E. Sonnhammer.'R. Staden, J. Sulston, J. Thierry-Mieg, K. Thomas, M. Vaudin, K. Vaughan, R. Waterson, A. Watson, L. Weinstock, L. Wilkinstock, J. Wilkinson-Sproat, and P. Wohldman. 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 368:32-38,1994.
    • Nature 368:32-38,1994.
    • Wilson, R.1
  • 44
    • 0030961030 scopus 로고    scopus 로고
    • 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
    • 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.
    • J. Clin. Invest. 100:1089-1097,1997.
    • Xu, Q.1
  • 45
    • 0029564092 scopus 로고    scopus 로고
    • A. Nakai, T. Hatayama, and K. Nagata. Cloning and expression of murine high molecular mass heat shock proteins, HsplOS
    • Yasuda, K. A. Nakai, T. Hatayama, and K. Nagata. Cloning and expression of murine high molecular mass heat shock proteins, HsplOS. J. Biol. Chem. 270:29718-29723,1995.
    • J. Biol. Chem. 270:29718-29723,1995.
    • Yasuda, K.1


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