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Volumn 101, Issue 6, 2009, Pages 351-360

Extracellular HspBP1 and Hsp72 synergistically activate epidermal growth factor receptor

Author keywords

Epidermal growth factor receptor (EGFR); Extracellular chaperones; Heat shock; Hsp72; Hsp72 binding protein 1 (HspBP1); Signalling

Indexed keywords

1 [[6 (3 METHOXYESTRA 1,3,5(10) TRIEN 17BETA YL)AMINO]HEXYL] 1H PYRROLE 2,5 DIONE; BINDING PROTEIN; CHROMOGRANIN A; EPIDERMAL GROWTH FACTOR RECEPTOR; HEAT SHOCK PROTEIN 72; HEAT SHOCK PROTEIN 72 BINDING PROTEIN 1; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PHOSPHOLIPASE C; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; 1 (6 ((3 METHOXYESTRA 1,3,5(10) TRIEN 17 YL)AMINO)HEXYL) 1H PYRROLE 2,5 DIONE; 1-(6-((3-METHOXYESTRA-1,3,5(10)-TRIEN-17-YL)AMINO)HEXYL)-1H-PYRROLE-2,5-DIONE; 2 PYRROLIDONE DERIVATIVE; CHAPERONE; ESTRANE DERIVATIVE; HEAT SHOCK PROTEIN 27; HSPB1 PROTEIN, HUMAN;

EID: 67449100861     PISSN: 02484900     EISSN: 1768322X     Source Type: Journal    
DOI: 10.1042/BC20080069     Document Type: Article
Times cited : (11)

References (32)
  • 1
    • 33747224323 scopus 로고    scopus 로고
    • Initiation of the immune response by extracellular Hsp72: Chaperokine activity of Hsp72
    • Asea, A. (2006) Initiation of the immune response by extracellular Hsp72: chaperokine activity of Hsp72. Curr. Immunol. Rev. 2 209-215
    • (2006) Curr. Immunol. Rev , vol.2 , pp. 209-215
    • Asea, A.1
  • 2
    • 23844544016 scopus 로고    scopus 로고
    • Alternative mechanism by which IFN-γ enhances tumor recognition: Active release of heat shock protein 72
    • Bausero, M.A., Gastpar, R., Multhoff, G. and Asea, A. (2005) Alternative mechanism by which IFN-γ enhances tumor recognition: active release of heat shock protein 72. J. Immunol. 175, 2900-2912
    • (2005) J. Immunol , vol.175 , pp. 2900-2912
    • Bausero, M.A.1    Gastpar, R.2    Multhoff, G.3    Asea, A.4
  • 3
    • 2442616009 scopus 로고    scopus 로고
    • Expression of regulated secretory proteins is sufficient to generate granule-like structures in constitutively secreting cells
    • Beuret, N., Stettler, H., Renold, A., Rutishauser, J. and Spiess, M. (2004) Expression of regulated secretory proteins is sufficient to generate granule-like structures in constitutively secreting cells. J. Biol. Chem. 279, 20242-20249
    • (2004) J. Biol. Chem , vol.279 , pp. 20242-20249
    • Beuret, N.1    Stettler, H.2    Renold, A.3    Rutishauser, J.4    Spiess, M.5
  • 4
    • 0028879136 scopus 로고
    • Cysteine string protein, a DnaJ family member, is present on diverse secretory vesicles
    • Braun, J.E.A. and Scheller, R.H. (1995) Cysteine string protein, a DnaJ family member, is present on diverse secretory vesicles. Neuropharmacology 34, 1361-1369
    • (1995) Neuropharmacology , vol.34 , pp. 1361-1369
    • Braun, J.E.A.1    Scheller, R.H.2
  • 5
    • 0026699473 scopus 로고
    • Secretory granule autoantigen in insulin-dependent diabetes mellitus is related to 62 kDa heat-shock protein (hsp60)
    • Brudzynski, K., Martinez, V. and Gupta, R.S. (1992) Secretory granule autoantigen in insulin-dependent diabetes mellitus is related to 62 kDa heat-shock protein (hsp60). J. Autoimmun. 5, 453-463
    • (1992) J. Autoimmun , vol.5 , pp. 453-463
    • Brudzynski, K.1    Martinez, V.2    Gupta, R.S.3
  • 6
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp72 and Hsp60 chaperone machines
    • Bukau, B. and Horwich, A.L. (1998) The Hsp72 and Hsp60 chaperone machines. Cell 92, 351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 7
    • 38449100535 scopus 로고    scopus 로고
    • Extracellular heat shock proteins in cell signaling and immunity
    • Calderwood, S.K., Mambula, S.S. and Gray, Jr, P.J. (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
  • 8
    • 0033976869 scopus 로고    scopus 로고
    • Localization of mitochondrial 60-kD heat shock chaperonin protein (Hsp60) in pituitary growth hormone secretory granules and pancreatic zymogen granules
    • Cechetto, J.D., Soltys, B.J. and Gupta, R.S. (2000) Localization of mitochondrial 60-kD heat shock chaperonin protein (Hsp60) in pituitary growth hormone secretory granules and pancreatic zymogen granules. J. Histochem. Cytochem. 48, 45-56
    • (2000) J. Histochem. Cytochem , vol.48 , pp. 45-56
    • Cechetto, J.D.1    Soltys, B.J.2    Gupta, R.S.3
  • 9
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability
    • Denizot, F. and Lang, R. (1986) Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability. J. Immunol. Methods 89, 271-277
    • (1986) J. Immunol. Methods , vol.89 , pp. 271-277
    • Denizot, F.1    Lang, R.2
  • 10
    • 34547850676 scopus 로고    scopus 로고
    • Phospholipase C β3 is a key component in the Gβγ/PKCη/PKD-mediated regulation of trans-Golgi network to plasma membrane transport
    • Diaz Anel, A.M. (2007) Phospholipase C β3 is a key component in the Gβγ/PKCη/PKD-mediated regulation of trans-Golgi network to plasma membrane transport. Biochem. J. 406, 157-165
    • (2007) Biochem. J , vol.406 , pp. 157-165
    • Diaz Anel, A.M.1
  • 11
    • 2942551229 scopus 로고    scopus 로고
    • Phospholipase C inhibitor, U73122, stimulates release of hsp-70 stress protein from A431 human carcinoma cells
    • Evdonin, A.L., Guzhova, I.V., Margulis, B.A. and Medvedeva, N.D. (2004) Phospholipase C inhibitor, U73122, stimulates release of hsp-70 stress protein from A431 human carcinoma cells. Cancer Cell Int. 4, 2
    • (2004) Cancer Cell Int , vol.4 , pp. 2
    • Evdonin, A.L.1    Guzhova, I.V.2    Margulis, B.A.3    Medvedeva, N.D.4
  • 13
    • 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. and Medvedeva, N.D. (2006b) 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
  • 15
    • 34548259088 scopus 로고    scopus 로고
    • Hsp72 chaperone as a survival factor in cell pathology
    • Guzhova, I. and Margulis, B. (2006) Hsp72 chaperone as a survival factor in cell pathology. Int. Rev. Cytol. 254, 101-149
    • (2006) Int. Rev. Cytol , vol.254 , pp. 101-149
    • Guzhova, I.1    Margulis, B.2
  • 16
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp72 can be released by glia and that exogenous Hsp72 can enhance neuronal stress tolerance
    • Guzhova, I., Kislyakova, K., Moskaliova, O., Fridlanskaya, I., Tytell, M., Cheetham, M. and Margulis, B. (2001) In vitro studies show that Hsp72 can be released by glia and that exogenous Hsp72 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
  • 17
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. and Hayer-Hartl, M. (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, M.2
  • 20
    • 33646088155 scopus 로고    scopus 로고
    • Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
    • Johnson, J.D. and 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
  • 21
    • 0037032470 scopus 로고    scopus 로고
    • HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor
    • Kabani, M., McLellan, C., Raynes, D.A., Guerriero, V. and Brodsky, J.L. (2002) HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. FEBS Lett. 531, 339-342
    • (2002) FEBS Lett , vol.531 , pp. 339-342
    • Kabani, M.1    McLellan, C.2    Raynes, D.A.3    Guerriero, V.4    Brodsky, J.L.5
  • 22
    • 33646348746 scopus 로고    scopus 로고
    • Mechanisms of stress-induced cellular HSP72 release: Implications for exercise-induced increases in extracellular HSP72
    • Lancaster, G.I. and 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
  • 23
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • Mambula, S.S. and Calderwood, S.K. (2006) Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes J. Immunol. 177, 7849-7857
    • (2006) J. Immunol , vol.177 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 24
    • 0038482018 scopus 로고    scopus 로고
    • HspBP1, an Hsp72 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp72 ATPase domain
    • McLellan, C.A., Raynes, D.A. and Guerriero, V. (2003) HspBP1, an Hsp72 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp72 ATPase domain. J. Biol. Chem. 278, 19017-19022
    • (2003) J. Biol. Chem , vol.278 , pp. 19017-19022
    • McLellan, C.A.1    Raynes, D.A.2    Guerriero, V.3
  • 25
    • 0030998836 scopus 로고    scopus 로고
    • 2+ release and directly activates ion channels in mouse pancreatic acinar cells
    • 2+ release and directly activates ion channels in mouse pancreatic acinar cells. Biochem. J. 324, 645-651
    • (1997) Biochem. J , vol.324 , pp. 645-651
    • Mogami, H.1    Lloyd Mills, C.2    Gallacher, D.V.3
  • 26
    • 0032483996 scopus 로고    scopus 로고
    • Inhibition of Hsp72 ATPase activity and protein renaturation by a novel Hsp72-binding protein
    • Raynes, D.A. and Guerriero, Jr, V. (1998) Inhibition of Hsp72 ATPase activity and protein renaturation by a novel Hsp72-binding protein. J. Biol. Chem. 273, 32883-32888
    • (1998) J. Biol. Chem , vol.273 , pp. 32883-32888
    • Raynes, D.A.1    Guerriero Jr, V.2
  • 27
    • 33744995563 scopus 로고    scopus 로고
    • Human serum contains detectable levels of the Hsp72 cochaperone HspBP1 and antibodies bound to HspBP1
    • Raynes, D.A., Thomson, C.A., Stroster, J., Newton, T., Cuneo, P. and Guerriero, V. (2006) Human serum contains detectable levels of the Hsp72 cochaperone HspBP1 and antibodies bound to HspBP1. J. Immunoassay Immunochem. 27, 251-264
    • (2006) J. Immunoassay Immunochem , vol.27 , pp. 251-264
    • Raynes, D.A.1    Thomson, C.A.2    Stroster, J.3    Newton, T.4    Cuneo, P.5    Guerriero, V.6
  • 28
    • 0026702863 scopus 로고
    • U-73122, an aminosteroid phospholipase C antagonist, noncompetitively inhibits thyrotropin-releasing hormone effects in GH3 rat pituitary cells
    • Smallridge, R.C., Kiang, J.G., Gist, I.D., Fein, H.G. and Galloway, R.J. (1992) U-73122, an aminosteroid phospholipase C antagonist, noncompetitively inhibits thyrotropin-releasing hormone effects in GH3 rat pituitary cells. Endocrinology 131, 1883-1888
    • (1992) Endocrinology , vol.131 , pp. 1883-1888
    • Smallridge, R.C.1    Kiang, J.G.2    Gist, I.D.3    Fein, H.G.4    Galloway, R.J.5
  • 29
    • 0035958913 scopus 로고    scopus 로고
    • Oxidative stress-induced phospholipase C-γ1 activation enhances cell survival
    • Wang, X., McCullough, K.D., Wang, X., Carpenter, G. and Holbrook, N.J. (2001) Oxidative stress-induced phospholipase C-γ1 activation enhances cell survival. J. Biol. Chem. 276, 28364-28371
    • (2001) J. Biol. Chem , vol.276 , pp. 28364-28371
    • Wang, X.1    McCullough, K.D.2    Wang, X.3    Carpenter, G.4    Holbrook, N.J.5
  • 30
    • 0034007505 scopus 로고    scopus 로고
    • Elevated serum chromogranin A is detectable in patients with carcinomas at advanced disease stages
    • Wu, J.T., Erickson, A.J., Tsao, K.C., Wu, T.L. and Sun, C.F. (2000) Elevated serum chromogranin A is detectable in patients with carcinomas at advanced disease stages. Ann. Clin. Lab. Sci. 30, 175-178
    • (2000) Ann. Clin. Lab. Sci , vol.30 , pp. 175-178
    • Wu, J.T.1    Erickson, A.J.2    Tsao, K.C.3    Wu, T.L.4    Sun, C.F.5
  • 32
    • 0028842290 scopus 로고
    • Effects of the phospholipase-C inhibitor, U73122, on signaling and secretion in pituitary gonadotrophs
    • Zheng, L., Paik, W.Y., Cesnjaj, M., Balla, T., Tomic, M., Catt, K.J. and Stojilkovic, S.S. (1995) Effects of the phospholipase-C inhibitor, U73122, on signaling and secretion in pituitary gonadotrophs. Endocrinology 136, 1079-1088
    • (1995) Endocrinology , vol.136 , pp. 1079-1088
    • Zheng, L.1    Paik, W.Y.2    Cesnjaj, M.3    Balla, T.4    Tomic, M.5    Catt, K.J.6    Stojilkovic, S.S.7


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