메뉴 건너뛰기




Volumn 856, Issue , 1998, Pages 206-213

Heat shock proteins and the inflammatory response

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; HEAT SHOCK PROTEIN;

EID: 0031772471     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.1998.tb08327.x     Document Type: Conference Paper
Times cited : (139)

References (45)
  • 1
    • 0001824746 scopus 로고
    • Progress and perspectives on the biology of heat shock proteins and molecular chaperones
    • R. I. Morimoto et al, Eds. : Cold Spring Harbor Laboratory Press. Cold Spring Harbor, MA
    • MORIMOTO, R. I. et al. 1994. Progress and perspectives on the biology of heat shock proteins and molecular chaperones. In The Biology of Heat Shock Proteins and Molecular Chaperones. R. I. Morimoto et al, Eds. : 1-30. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, MA.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 1-30
    • Morimoto, R.I.1
  • 2
    • 0023924166 scopus 로고
    • Characterization of the thermotolerant cell. I: Effects on protein synthesis activity and the regulation of the heat-shock protein 70 expression
    • MIZZEN, L. A. et al. 1988. Characterization of the thermotolerant cell. I: Effects on protein synthesis activity and the regulation of the heat-shock protein 70 expression. J. Cell. Biol. 106: 1106-1116.
    • (1988) J. Cell. Biol. , vol.106 , pp. 1106-1116
    • Mizzen, L.A.1
  • 3
    • 0022002022 scopus 로고
    • Structure and expression of the human gene encoding major heat shock protein HSP 70
    • WU, B. et al. 1985. Structure and expression of the human gene encoding major heat shock protein HSP 70. Mol. Cell. Biol. 5: 330-341.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 330-341
    • Wu, B.1
  • 4
    • 0023094286 scopus 로고
    • Heat-inducible human factor that binds to a human HSP 70 promoter
    • KINGSTON, R. E. et al. 1987. Heat-inducible human factor that binds to a human HSP 70 promoter. Mol. Cell. Biol. 7: 1530-1534.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1530-1534
    • Kingston, R.E.1
  • 5
    • 0027315754 scopus 로고
    • Heat stress regulates the human 70kD heat shock gene through its 3′ untranslated region
    • MOSELEY, P. L. et al. 1993. Heat stress regulates the human 70kD heat shock gene through its 3′ untranslated region. Am. J. Physiol. 64: L533-L537.
    • (1993) Am. J. Physiol. , vol.64
    • Moseley, P.L.1
  • 6
    • 0005733433 scopus 로고
    • Acidosis alters hyperthermic cytotoxicity and the cellular stress response
    • GAPEN, C. et al. 1995. Acidosis alters hyperthermic cytotoxicity and the cellular stress response. Therm. Biol. 20: 321-325.
    • (1995) Therm. Biol. , vol.20 , pp. 321-325
    • Gapen, C.1
  • 7
    • 0025303147 scopus 로고
    • Interaction of heat shock protein 70 with newly synthesized proteins: Implications for protein folding and assembly
    • BECKMANN, R. P. et al. 1990. Interaction of heat shock protein 70 with newly synthesized proteins: Implications for protein folding and assembly. Science 248: 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1
  • 8
    • 0002441161 scopus 로고
    • Structure, function, and regulation of the endoplasmic reticulum chaperone, BiP
    • R. I. Morimoto et al. Eds. : Cold Spring Harbor Laboratory Press. Cold Spring Harbor, MA
    • KNITTLER, M. R. et al. 1992. Structure, function, and regulation of the endoplasmic reticulum chaperone, BiP. In The Biology of Heat Shock Proteins and Molecular Chaperones. R. I. Morimoto et al. Eds. : 111-135. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, MA.
    • (1992) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 111-135
    • Knittler, M.R.1
  • 9
    • 0026569212 scopus 로고
    • Interaction of BiP with newly synthesized immunoglobulin light chain molecules: Cycles of sequential binding and release
    • KNITTLER, M. R. et al. 1992. Interaction of BiP with newly synthesized immunoglobulin light chain molecules: Cycles of sequential binding and release. EMBO J. 11: 1573-1581.
    • (1992) EMBO J , vol.11 , pp. 1573-1581
    • Knittler, M.R.1
  • 10
    • 0030724378 scopus 로고    scopus 로고
    • Heat shock proteins and heat adaptation of the whole organism
    • MOSELEY, P. L. 1997. Heat shock proteins and heat adaptation of the whole organism. J. Appl. Physiol. 83: 5.
    • (1997) J. Appl. Physiol. , vol.83 , pp. 5
    • Moseley, P.L.1
  • 11
    • 0021089337 scopus 로고
    • Heat-induced protection of mice against thermal death
    • LI, G. C. et al. 1983. Heat-induced protection of mice against thermal death. Cancer Res. 43: 5758-5760.
    • (1983) Cancer Res , vol.43 , pp. 5758-5760
    • Li, G.C.1
  • 12
    • 0026644826 scopus 로고
    • Acute heat stress protects rats against endotoxin shock
    • RYAN, A. J. et al. 1992. Acute heat stress protects rats against endotoxin shock. J. Appl. Physiol. 73: 1517-1522.
    • (1992) J. Appl. Physiol. , vol.73 , pp. 1517-1522
    • Ryan, A.J.1
  • 13
    • 0027715708 scopus 로고
    • Hyperthermia protects mice against the lethal effects of endotoxin
    • HOTCHKISS, R. et al. 1993. Hyperthermia protects mice against the lethal effects of endotoxin. Am. J. Physiol. 265: R1447-R1457.
    • (1993) Am. J. Physiol. , vol.265
    • Hotchkiss, R.1
  • 14
    • 0028923827 scopus 로고
    • Heat shock protein synthesis and thermotolerance in cataglyphis, an ant from the Sahara Desert
    • GEHRING, W. J. et al. 1995. Heat shock protein synthesis and thermotolerance in cataglyphis, an ant from the Sahara Desert. Proc. Natl. Acad. Sci. 92: 2994-2998.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 2994-2998
    • Gehring, W.J.1
  • 15
    • 0026567428 scopus 로고
    • Heat shock proteins and thermoresistance in lizards
    • ULMASOV, K. A. et al. 1992. Heat shock proteins and thermoresistance in lizards. Proc. Natl. Acad. Sci. 89: 1666-1670.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 1666-1670
    • Ulmasov, K.A.1
  • 16
    • 0027254809 scopus 로고    scopus 로고
    • Induction of heat shock response leads to apoptosis in endothelial cells previously exposed to endotoxin
    • BUCHMAN, T. G. et al. 1996. Induction of heat shock response leads to apoptosis in endothelial cells previously exposed to endotoxin. Am. J. Physiol. 265: H165-H170.
    • (1996) Am. J. Physiol. , vol.265
    • Buchman, T.G.1
  • 17
    • 0026033354 scopus 로고
    • Expression of a heat-inducible gene of the heat shock protein 70 family in human myelomonocytic cells: Regulation by bacterial products and cytokines
    • FINCATO, G. et al. 1991. Expression of a heat-inducible gene of the heat shock protein 70 family in human myelomonocytic cells: Regulation by bacterial products and cytokines. Blood 77: 579-586.
    • (1991) Blood , vol.77 , pp. 579-586
    • Fincato, G.1
  • 18
    • 0026029006 scopus 로고
    • Heat shock protein induction in rat pancreatic islets by recombinant human interleukin 1β
    • HELQVIST, S. et al. 1991. Heat shock protein induction in rat pancreatic islets by recombinant human interleukin 1β. Diabetologia 34: 150-156.
    • (1991) Diabetologia , vol.34 , pp. 150-156
    • Helqvist, S.1
  • 19
    • 0026571479 scopus 로고
    • Cytokines induce stress protein formation in cultured cardiac myocytes
    • LOW-FRIEDRICH, I. et al. 1991. Cytokines induce stress protein formation in cultured cardiac myocytes. Basic Res. Cardiol. 87: 12-18.
    • (1991) Basic Res. Cardiol. , vol.87 , pp. 12-18
    • Low-Friedrich, I.1
  • 20
    • 0025809962 scopus 로고
    • Decreased heat and tumor necrosis factor-mediated HSP28 phosphorylation in thermotolerant hela cells
    • ARRIGO, A. P. et al. 1991. Decreased heat and tumor necrosis factor-mediated HSP28 phosphorylation in thermotolerant hela cells. FEBS Lett. 282: 152-156.
    • (1991) FEBS Lett , vol.282 , pp. 152-156
    • Arrigo, A.P.1
  • 21
    • 0027211998 scopus 로고
    • Interaction between tumor necrosis factor-α and HSP-70 in human leukemia cells
    • MÜLLER, E. et al. 1993. Interaction between tumor necrosis factor-α and HSP-70 in human leukemia cells. Leukocyte Res. 17: 523-526.
    • (1993) Leukocyte Res , vol.17 , pp. 523-526
    • Müller, E.1
  • 22
    • 0027469435 scopus 로고
    • Heat shock proteins protect cells from monocyte cytotoxicity: Possible mechanism of self protection
    • JÄÄTTELÄ, M. et al. 1993. Heat shock proteins protect cells from monocyte cytotoxicity: Possible mechanism of self protection. J. Exp. Med. 177: 231-236.
    • (1993) J. Exp. Med. , vol.177 , pp. 231-236
    • Jäättelä, M.1
  • 24
    • 0028080586 scopus 로고
    • Differential effects on hyperthermia on macrophage interleukin-6 and tumor necrosis factor-α expression
    • ENSOR, J. E. et al. 1994. Differential effects on hyperthermia on macrophage interleukin-6 and tumor necrosis factor-α expression. Am. J. Physiol. 266: C967-C974.
    • (1994) Am. J. Physiol. , vol.266
    • Ensor, J.E.1
  • 25
    • 0026683542 scopus 로고
    • Transcriptional inhibition of endotoxin-induced monokine synthesis following heat shock in murine peritoneal macrophages
    • SNYDER, Y. M. et al. 1992. Transcriptional inhibition of endotoxin-induced monokine synthesis following heat shock in murine peritoneal macrophages. J. Leukocyte Biol. 51: 181-187.
    • (1992) J. Leukocyte Biol. , vol.51 , pp. 181-187
    • Snyder, Y.M.1
  • 26
    • 0030770549 scopus 로고    scopus 로고
    • Effect of heat stress on LPS-induced fever and tumor necrosis factor
    • KLUGER, M. J. et al. 1997. Effect of heat stress on LPS-induced fever and tumor necrosis factor. Am. J. Physiol. 273: R858-R863.
    • (1997) Am. J. Physiol. , vol.273
    • Kluger, M.J.1
  • 27
    • 0028201732 scopus 로고
    • How is self-tolerance induced and maintained. Horror autotoxicus
    • MATZINGER, P. 1994. How is self-tolerance induced and maintained. Horror autotoxicus. Annu. Rev. Immunol. 12: 991-1045.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 28
    • 0028848045 scopus 로고
    • Perspectives in clinical implications of the stress response
    • MINOWADA, G. et al. 1995. Perspectives in clinical implications of the stress response. J. Clin. Invest. 95: 3-12.
    • (1995) J. Clin. Invest. , vol.95 , pp. 3-12
    • Minowada, G.1
  • 29
    • 33646335758 scopus 로고    scopus 로고
    • Molecular chaperones and the immune response
    • YOUNG, D. et al. Molecular chaperones and the immune response. Phil. Trans. R. Soc. London B. 339-363.
    • Phil. Trans. R. Soc. London B. , pp. 339-363
    • Young, D.1
  • 30
    • 0027260585 scopus 로고
    • Heat shock protein 70-associated peptides elicit specific cancer immunity
    • HEIICHIRO, U. 1993. Heat shock protein 70-associated peptides elicit specific cancer immunity. J. Exp. Med. 178: 1391-1396.
    • (1993) J. Exp. Med. , vol.178 , pp. 1391-1396
    • Heiichiro, U.1
  • 31
    • 0028301079 scopus 로고
    • Comparison of tumor-specific immunogenicities of stress-induced proteins GP96, HSP90, and HSP70
    • HEIICHIRO, U. et al. 1994. Comparison of tumor-specific immunogenicities of stress-induced proteins GP96, HSP90, and HSP70. J. Immun. 152: 5398-5403.
    • (1994) J. Immun. , vol.152 , pp. 5398-5403
    • Heiichiro, U.1
  • 32
    • 0030820099 scopus 로고    scopus 로고
    • Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations
    • TAMURA, Y. et al. 1997. Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations. Science 278: 117-120.
    • (1997) Science , vol.278 , pp. 117-120
    • Tamura, Y.1
  • 33
    • 0030891397 scopus 로고    scopus 로고
    • In vivo gene therapy of malignant tumors with heat shock protein-65 gene
    • LUKACS, K. V. et al. 1997. In vivo gene therapy of malignant tumors with heat shock protein-65 gene. Gene Ther. 4: 346-350.
    • (1997) Gene Ther , vol.4 , pp. 346-350
    • Lukacs, K.V.1
  • 34
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • PRAMOD, K. et al. 1994. Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics 39: 93-98.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Pramod, K.1
  • 35
    • 0028979675 scopus 로고
    • Mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • RYUICHIRO, S. et al. 1995. Mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269: 1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Ryuichiro, S.1
  • 36
    • 0030775140 scopus 로고    scopus 로고
    • Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T-lymphocyte response and tumor immunity
    • BLACHERE, N. et al. 1997. Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T-lymphocyte response and tumor immunity. J. Exp. Med. 186: 1315-1322.
    • (1997) J. Exp. Med. , vol.186 , pp. 1315-1322
    • Blachere, N.1
  • 37
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • FERRARINI, L. et al. 1992. Unusual expression and localization of heat-shock proteins in human tumor cells. Int. J. Cancer 51: 613-619.
    • (1992) Int. J. Cancer , vol.51 , pp. 613-619
    • Ferrarini, L.1
  • 38
    • 0026690529 scopus 로고
    • Surface expressed heat shock proteins by stressed or human immunodeficiency virus (HIV)-infected lymphoid cells represent the target for antibody-dependent cellular cytotoxicity
    • DI-CESARE S. et al. 1992. Surface expressed heat shock proteins by stressed or human immunodeficiency virus (HIV)-infected lymphoid cells represent the target for antibody-dependent cellular cytotoxicity. J. Immunol. 76: 341.
    • (1992) J. Immunol. , vol.76 , pp. 341
    • Di-Cesare, S.1
  • 39
    • 33646284809 scopus 로고    scopus 로고
    • Human renal carcinoma cells express an inducible heat shock protein (HSP72) on their cell surface after hyperthermia; implications for clinical treatment
    • Humboldt University. Berlin, Germany
    • ROIGAS, J. et al. 1997. Human renal carcinoma cells express an inducible heat shock protein (HSP72) on their cell surface after hyperthermia; implications for clinical treatment. Collected abstracts of the 16th Annual Meeting of the European Society for Hyperthermic Oncology. No. ESHO-97. Humboldt University. Berlin, Germany.
    • (1997) Collected Abstracts of the 16th Annual Meeting of the European Society for Hyperthermic Oncology. No. ESHO-97
    • Roigas, J.1
  • 40
    • 0028978682 scopus 로고
    • - large granular lymphocytes recognize a heat-inducible immunogenic determinant associated with the 72-kD heat shock protein on human sarcoma cells
    • - large granular lymphocytes recognize a heat-inducible immunogenic determinant associated with the 72-kD heat shock protein on human sarcoma cells. Blood 86: 1374-1382.
    • (1995) Blood , vol.86 , pp. 1374-1382
    • Multhoff, G.1
  • 41
    • 0031132876 scopus 로고    scopus 로고
    • Heat shock protein 72 on tumor cells: A recognition structure for NK cells
    • MULTHOFF, G. et al. 1997. Heat shock protein 72 on tumor cells: A recognition structure for NK cells. J. Immunol. 158: 4341-4350.
    • (1997) J. Immunol. , vol.158 , pp. 4341-4350
    • Multhoff, G.1
  • 42
    • 0030022121 scopus 로고    scopus 로고
    • Induction of autologous tumor killing by heat treatment of fresh human tumor cells: Involvement of γδ T cells and heat shock protein 70
    • WEI, Y. et al. 1996. Induction of autologous tumor killing by heat treatment of fresh human tumor cells: Involvement of γδ T cells and heat shock protein 70. Cancer Res. 56: 1104-1110.
    • (1996) Cancer Res , vol.56 , pp. 1104-1110
    • Wei, Y.1
  • 43
    • 0029925942 scopus 로고    scopus 로고
    • Non-cytotoxic alkyl-lysophospholipid treatment increases sensitivity of leukemic K562 cells to lysis by natural killer (NK) cells
    • BOTZLER, C. et al. 1996. Non-cytotoxic alkyl-lysophospholipid treatment increases sensitivity of leukemic K562 cells to lysis by natural killer (NK) cells. Int. J. Cancer. 65: 633-638.
    • (1996) Int. J. Cancer. , vol.65 , pp. 633-638
    • Botzler, C.1
  • 44
    • 0029445568 scopus 로고
    • Immune function of dendritic cells against cancers
    • CHAUX, P. 1995. Immune function of dendritic cells against cancers. Pathol. Biol. 43: 897-903.
    • (1995) Pathol. Biol. , vol.43 , pp. 897-903
    • Chaux, P.1
  • 45
    • 0029850387 scopus 로고    scopus 로고
    • Subcellular redistribution of HSP72 protein during cisplatin-induced apoptosis in hela-cells
    • MELENDEZZAJGLA, J. et al. 1996. Subcellular redistribution of HSP72 protein during cisplatin-induced apoptosis in hela-cells. Biochem. Mol. Biol. Int. 40: 253-261.
    • (1996) Biochem. Mol. Biol. Int. , vol.40 , pp. 253-261
    • Melendezzajgla, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.