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Volumn 51, Issue 3, 2009, Pages 219-228

Dual role of chaperones in the response of a cell and of a whole organism to stress

Author keywords

Cancer; Chaperones; Heat shock protein; Neurodegenerative disease

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70;

EID: 67649213523     PISSN: 00413771     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (17)

References (60)
  • 1
    • 77449149333 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 2
    • 77449106922 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 3
    • 77449092718 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 4
    • 77449087752 scopus 로고    scopus 로고
    • Russian source
    • Russian source
  • 6
  • 7
    • 0344443774 scopus 로고    scopus 로고
    • BAG-1 - a nucleotide exchange factor of Hsc70 with multiple cellular functions
    • Alberti S., Esser C., Höhfeld J. 2003. BAG-1 - a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones. 8 : 225-231.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 225-231
    • Alberti, S.1    Esser, C.2    Höhfeld, J.3
  • 8
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A., Kraeft S. K., Kurt-Jones E. A., Stevenson M. A., Chen L. B., Finberg R. W., Koo G. C., Calderwood S. K. 2000. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6 : 435-442.
    • (2000) Nat. Med , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 11
    • 34047097917 scopus 로고    scopus 로고
    • Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes
    • Bivik C., Rosdahl I., Ollinger K. 2007. Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes. Carcinogenesis. 28 : 537-544.
    • (2007) Carcinogenesis , vol.28 , pp. 537-544
    • Bivik, C.1    Rosdahl, I.2    Ollinger, K.3
  • 13
    • 35548939457 scopus 로고    scopus 로고
    • Heat shock proteins and protection of the nervous system
    • Brown I. R. 2007. Heat shock proteins and protection of the nervous system. Ann. N. Y. Acad. Sci. 1113 : 147-158.
    • (2007) Ann. N. Y. Acad. Sci , vol.1113 , pp. 147-158
    • Brown, I.R.1
  • 14
    • 38449100535 scopus 로고    scopus 로고
    • Extracellular heat shock proteins in cell signaling and immunity
    • Calderwood S. K., Mambula S. S., Gray P. J., Jr. 2007. Extracellular heat shock proteins in cell signaling and immunity. Ann. N. Y. Acad. Sci. 1113 : 28-39.
    • (2007) Ann. N. Y. Acad. Sci , vol.1113 , pp. 28-39
    • Calderwood, S.K.1    Mambula, S.S.2    Gray Jr., P.J.3
  • 16
    • 0038281358 scopus 로고    scopus 로고
    • The regulatory effect of memantine on expression and synthesis of heat shock protein 70 gene in neonatal rat models with cerebral hypoxic ischemia
    • Chen H., Liu Z., Zhou Z., Jiang M., Qian L., Wu S. 2003. The regulatory effect of memantine on expression and synthesis of heat shock protein 70 gene in neonatal rat models with cerebral hypoxic ischemia. Chin. Med. J. (Engl.). 116 : 558-564.
    • (2003) Chin. Med. J. (Engl.) , vol.116 , pp. 558-564
    • Chen, H.1    Liu, Z.2    Zhou, Z.3    Jiang, M.4    Qian, L.5    Wu, S.6
  • 17
    • 27144529107 scopus 로고    scopus 로고
    • More efficient induction of HLA-A*0201-restricted and carcinoembryonic antigen (CEA)-specific CTL response by immunization with exosomes prepared from heat-stressed CEA-positive tumor cells
    • Dai S., Wan T., Wang B., Zhou X., Xiu F., Chen T., Wu Y., Cao X. 2005. More efficient induction of HLA-A*0201-restricted and carcinoembryonic antigen (CEA)-specific CTL response by immunization with exosomes prepared from heat-stressed CEA-positive tumor cells. Clin. Cancer Res. 11 : 7554-7563.
    • (2005) Clin. Cancer Res , vol.11 , pp. 7554-7563
    • Dai, S.1    Wan, T.2    Wang, B.3    Zhou, X.4    Xiu, F.5    Chen, T.6    Wu, Y.7    Cao, X.8
  • 19
    • 33747041690 scopus 로고    scopus 로고
    • Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin: Comparison with caspase-inhibitor- and cycle-arrest-mediated cytoprotection
    • Demidenko Z. N., Vivo C., Halicka H. D., Li C. J., Bhalla K., Broude E. V., Blagosklonny M. V. 2006. Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin: comparison with caspase-inhibitor- and cycle-arrest-mediated cytoprotection. Cell Death Differ. 13 : 1434-1441.
    • (2006) Cell Death Differ , vol.13 , pp. 1434-1441
    • Demidenko, Z.N.1    Vivo, C.2    Halicka, H.D.3    Li, C.J.4    Bhalla, K.5    Broude, E.V.6    Blagosklonny, M.V.7
  • 21
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis J. 1987. Proteins as molecular chaperones. Nature. 328 : 378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 22
    • 2942551229 scopus 로고    scopus 로고
    • Evdonin A. L., Guzhova I. V., Margulis B. A., Medvedeva N. D. 2004. Phospholipase c inhibitor, u73122, stimulates release of hsp-70 stress protein from A431 human carcinoma cells. Cancer Cell. Intern. 4 : 2.
    • Evdonin A. L., Guzhova I. V., Margulis B. A., Medvedeva N. D. 2004. Phospholipase c inhibitor, u73122, stimulates release of hsp-70 stress protein from A431 human carcinoma cells. Cancer Cell. Intern. 4 : 2.
  • 23
    • 37849185221 scopus 로고    scopus 로고
    • Extracellular heat shock protein 70 mediates heat stress-induced epidermal growth factor receptor transactivation in A431 carcinoma cells
    • Evdonin A. L., Guzhova I. V., Margulis B. A., Medvedeva N. D. 2006. Extracellular heat shock protein 70 mediates heat stress-induced epidermal growth factor receptor transactivation in A431 carcinoma cells. FEBS Lett. 580 : 6674-6678.
    • (2006) FEBS Lett , vol.580 , pp. 6674-6678
    • Evdonin, A.L.1    Guzhova, I.V.2    Margulis, B.A.3    Medvedeva, N.D.4
  • 25
    • 3042636977 scopus 로고    scopus 로고
    • Cat exposure induces both intra- and extracellular Hsp72: The role of adrenal hormones
    • Fleshner M., Campisi J., Amiri L., Diamond D. M. 2004. Cat exposure induces both intra- and extracellular Hsp72: the role of adrenal hormones. Psychoneuroendocrinology. 29 : 1142-1152.
    • (2004) Psychoneuroendocrinology , vol.29 , pp. 1142-1152
    • Fleshner, M.1    Campisi, J.2    Amiri, L.3    Diamond, D.M.4
  • 26
    • 1642536402 scopus 로고    scopus 로고
    • The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells
    • Gastpar R., Gross C., Rossbacher L., Ellwart J., Riegger J., Multhoff G. 2004. The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. J. Immunol. 172 : 972-980.
    • (2004) J. Immunol , vol.172 , pp. 972-980
    • Gastpar, R.1    Gross, C.2    Rossbacher, L.3    Ellwart, J.4    Riegger, J.5    Multhoff, G.6
  • 27
    • 48849109369 scopus 로고    scopus 로고
    • Regulation of apoptotic and inflammatory cell signaling in cerebral ischemia: The complex roles of heat shock protein 70
    • Giffard R. G., Han R. Q., Emery J. F., Duan M., Pittet J. F. 2008. Regulation of apoptotic and inflammatory cell signaling in cerebral ischemia: the complex roles of heat shock protein 70. Anesthesiology. 109 : 339-348.
    • (2008) Anesthesiology , vol.109 , pp. 339-348
    • Giffard, R.G.1    Han, R.Q.2    Emery, J.F.3    Duan, M.4    Pittet, J.F.5
  • 29
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance
    • Guzhova I., Kislyakova K., Moskaliova O., Fridlanskaya I., Tytell M., Cheetham M., Margulis B. 2001. In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance. Brain Res. 914 : 66-73.
    • (2001) Brain Res , vol.914 , pp. 66-73
    • Guzhova, I.1    Kislyakova, K.2    Moskaliova, O.3    Fridlanskaya, I.4    Tytell, M.5    Cheetham, M.6    Margulis, B.7
  • 30
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl F. U., Hayer-Hartl V. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 295 : 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, V.2
  • 32
    • 1642527106 scopus 로고    scopus 로고
    • Potent antitumor effect elicited by superantigen-linked tumor cells transduced with heat shock protein 70 gene
    • Huang C., Yu H., Wang Q., Ma W., Xia D., Yi P., Zhang L., Cao X. 2004. Potent antitumor effect elicited by superantigen-linked tumor cells transduced with heat shock protein 70 gene. Cancer Sci. 95 : 160-167.
    • (2004) Cancer Sci , vol.95 , pp. 160-167
    • Huang, C.1    Yu, H.2    Wang, Q.3    Ma, W.4    Xia, D.5    Yi, P.6    Zhang, L.7    Cao, X.8
  • 35
    • 33646088155 scopus 로고    scopus 로고
    • Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
    • Johnson J. D., Fleshner M. 2006. Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72. J. Leukoc. Biol. 79 : 425-434.
    • (2006) J. Leukoc. Biol , vol.79 , pp. 425-434
    • Johnson, J.D.1    Fleshner, M.2
  • 36
    • 53149114499 scopus 로고    scopus 로고
    • Kalmar B., Novoselov S., Gray A., Cheetham M. E., Margulis B., Greensmith L. 2008. Late stage treatment with Arimoclomol delays disease progression and prevents protein aggregation in the SOD1(G93A) mouse model of ALS. J. Neurochem. Sep 2. 107 : 339-350.
    • Kalmar B., Novoselov S., Gray A., Cheetham M. E., Margulis B., Greensmith L. 2008. Late stage treatment with Arimoclomol delays disease progression and prevents protein aggregation in the SOD1(G93A) mouse model of ALS. J. Neurochem. Sep 2. 107 : 339-350.
  • 37
    • 33646010643 scopus 로고    scopus 로고
    • Chaperones in preventing protein denaturation in living cells and protecting against cellular stress
    • Kampinga H. H. 2006. Chaperones in preventing protein denaturation in living cells and protecting against cellular stress. Handb. Exp. Pharmacol. 172 : 1-42.
    • (2006) Handb. Exp. Pharmacol , vol.172 , pp. 1-42
    • Kampinga, H.H.1
  • 38
    • 37549011770 scopus 로고    scopus 로고
    • Curcumin treatment enhances islet recovery by induction of heat shock response proteins, Hsp70 and heme oxygenase-1, during cryopreservation
    • Kanitkar M., Bhonde R. R. 2008. Curcumin treatment enhances islet recovery by induction of heat shock response proteins, Hsp70 and heme oxygenase-1, during cryopreservation. Life Sci. 82 : 182-189.
    • (2008) Life Sci , vol.82 , pp. 182-189
    • Kanitkar, M.1    Bhonde, R.R.2
  • 39
    • 34347408042 scopus 로고    scopus 로고
    • Chaperone-rich cell lysate embedded with BCR-ABL peptide demonstrates enhanced anti-tumor activity against a murine BCR-ABL positive leukemia
    • Kislin K. L., Marron M. T., Li G., Graner M. W., Katsanis E. 2007. Chaperone-rich cell lysate embedded with BCR-ABL peptide demonstrates enhanced anti-tumor activity against a murine BCR-ABL positive leukemia. FASEB J. 21 : 2173-2184.
    • (2007) FASEB J , vol.21 , pp. 2173-2184
    • Kislin, K.L.1    Marron, M.T.2    Li, G.3    Graner, M.W.4    Katsanis, E.5
  • 41
    • 2542558307 scopus 로고    scopus 로고
    • Treatment of colon and lung cancer patients with ex vivo heat shock protein 70-peptide-activated, autologous natural killer cells: A clinical phase trial
    • Krause S. W., Gastpar R., Andreesen R., Gross C., Ullrich H., Thonigs G., Pfister K., Multhoff G. 2004. Treatment of colon and lung cancer patients with ex vivo heat shock protein 70-peptide-activated, autologous natural killer cells: a clinical phase trial. Clin. Cancer Res. 10 : 3699-3707.
    • (2004) Clin. Cancer Res , vol.10 , pp. 3699-3707
    • Krause, S.W.1    Gastpar, R.2    Andreesen, R.3    Gross, C.4    Ullrich, H.5    Thonigs, G.6    Pfister, K.7    Multhoff, G.8
  • 42
    • 33646348746 scopus 로고    scopus 로고
    • Mechanisms of stress-induced cellular HSP72 release: Implications for exercise-induced increases in extracellular HSP72
    • Lancaster G. I., Febbraio M. A. 2005. Mechanisms of stress-induced cellular HSP72 release: implications for exercise-induced increases in extracellular HSP72. Exerc. Immunol. Rev. 11 : 46-52.
    • (2005) Exerc. Immunol. Rev , vol.11 , pp. 46-52
    • Lancaster, G.I.1    Febbraio, M.A.2
  • 43
    • 33845637791 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis
    • Lui J. C., Kong S. K. 2007. Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis. FEBS Lett. 581 : 109-117.
    • (2007) FEBS Lett , vol.581 , pp. 109-117
    • Lui, J.C.1    Kong, S.K.2
  • 44
    • 36549077002 scopus 로고    scopus 로고
    • Nutraceutical strategy in aging: Targeting heat shock protein and inflammatory profile through understanding interleukin-6 polymorphism
    • Marotta F., Koike K., Lorenzetti A., Naito Y., Fayet F., Shimizu H., Marandola P. 2007. Nutraceutical strategy in aging: targeting heat shock protein and inflammatory profile through understanding interleukin-6 polymorphism. Ann. N. Y. Acad. Sci. 1119 : 196-202.
    • (2007) Ann. N. Y. Acad. Sci , vol.1119 , pp. 196-202
    • Marotta, F.1    Koike, K.2    Lorenzetti, A.3    Naito, Y.4    Fayet, F.5    Shimizu, H.6    Marandola, P.7
  • 45
    • 33644858948 scopus 로고    scopus 로고
    • Reduction of caspase-8 and -9 cleavage is associated with increased c-FLIP and increased binding of Apaf-1 and Hsp70 after neonatal hypoxic/ischemic injury in mice overexpressing Hsp70
    • Matsumori Y., Northington F. J., Hong S. M., Kayama T., Sheldon R. A., Vexler Z. S., Ferriero D. M., Weinstein P. R., Liu J. 2006. Reduction of caspase-8 and -9 cleavage is associated with increased c-FLIP and increased binding of Apaf-1 and Hsp70 after neonatal hypoxic/ischemic injury in mice overexpressing Hsp70. Stroke. 37 : 507-512.
    • (2006) Stroke , vol.37 , pp. 507-512
    • Matsumori, Y.1    Northington, F.J.2    Hong, S.M.3    Kayama, T.4    Sheldon, R.A.5    Vexler, Z.S.6    Ferriero, D.M.7    Weinstein, P.R.8    Liu, J.9
  • 48
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
    • Nylandsted J., Rohde M., Brand K., Bastholm L., Elling F., Jäättelä M. 2000. Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc. Nat. Acad. Sci. USA. 97 : 7871-7876.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jäättelä, M.6
  • 49
    • 28844480953 scopus 로고    scopus 로고
    • Valproic acid-mediated Hsp70 induction and anti-apoptotic neuroprotection in SH-SY5Y cells
    • Pan T., Li X., Xie W., Jankovic J., Le W. 2005. Valproic acid-mediated Hsp70 induction and anti-apoptotic neuroprotection in SH-SY5Y cells. FEBS Lett. 579 : 6716-6720.
    • (2005) FEBS Lett , vol.579 , pp. 6716-6720
    • Pan, T.1    Li, X.2    Xie, W.3    Jankovic, J.4    Le, W.5
  • 50
    • 34247352104 scopus 로고    scopus 로고
    • Leishmania major heat shock protein 70 (HSP70) is not protective in murine models of cutaneous leishmaniosis and stimulates strong humoral responses in cutaneous and visceral leishmaniosis patients
    • Rafati S., Gholami E., Hassani N., Ghaemimanesh F., Taslimi Y., Taheri T., Soong L. 2007. Leishmania major heat shock protein 70 (HSP70) is not protective in murine models of cutaneous leishmaniosis and stimulates strong humoral responses in cutaneous and visceral leishmaniosis patients. Vaccine. 25 : 4159-4169.
    • (2007) Vaccine , vol.25 , pp. 4159-4169
    • Rafati, S.1    Gholami, E.2    Hassani, N.3    Ghaemimanesh, F.4    Taslimi, Y.5    Taheri, T.6    Soong, L.7
  • 51
    • 0037609376 scopus 로고    scopus 로고
    • Postinsult treatment with lithium reduces brain damage and facilitates neurological recovery in a rat ischemia/reperfusion model
    • Ren M., Senatorov V. V., Chen R. W., Chuang D. M. 2003. Postinsult treatment with lithium reduces brain damage and facilitates neurological recovery in a rat ischemia/reperfusion model. Proc. Nat. Acad. Sci. USA. 100 : 6210-6215.
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100 , pp. 6210-6215
    • Ren, M.1    Senatorov, V.V.2    Chen, R.W.3    Chuang, D.M.4
  • 53
    • 10944266160 scopus 로고    scopus 로고
    • Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1
    • Steel R., Doherty J. P., Buzzard K., Clemons N., Hawkins C. J., Anderson R. L. 2004. Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1. J. Biol. Chem. 279 : 51 490-51 499.
    • (2004) J. Biol. Chem , vol.279
    • Steel, R.1    Doherty, J.P.2    Buzzard, K.3    Clemons, N.4    Hawkins, C.J.5    Anderson, R.L.6
  • 55
    • 0022637881 scopus 로고
    • Heat shock-like protein is transferred from glia to axon
    • Tytell M., Greenberg S. G., Lasek R. J. 1986. Heat shock-like protein is transferred from glia to axon. Brain Res. 363 : 161-164.
    • (1986) Brain Res , vol.363 , pp. 161-164
    • Tytell, M.1    Greenberg, S.G.2    Lasek, R.J.3
  • 59
    • 0030766734 scopus 로고    scopus 로고
    • Mammalian protein RAP46: An interaction partner and modulator of 70 kDa heat shock proteins
    • Zeiner M., Gebauer M., Gehring U. 1997. Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins. EMBO J. 16 : 5483-5490.
    • (1997) EMBO J , vol.16 , pp. 5483-5490
    • Zeiner, M.1    Gebauer, M.2    Gehring, U.3
  • 60
    • 36849044616 scopus 로고    scopus 로고
    • Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response
    • Zhang Y. Q., Sarge K. D. 2007. Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response. J. Mol. Med. 85 : 1421-1428.
    • (2007) J. Mol. Med , vol.85 , pp. 1421-1428
    • Zhang, Y.Q.1    Sarge, K.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.