메뉴 건너뛰기




Volumn 23, Issue 4, 2011, Pages 223-237

Extracellular heat shock protein 90 plays a role in translocating chaperoned antigen from endosome to proteasome for generating antigenic peptide to be cross-presented by dendritic cells

Author keywords

Antigen presentation processing; Cytotoxic T cell; Tumor immunity

Indexed keywords

ANTIGEN; HEAT SHOCK PROTEIN 90; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MONOCLONAL ANTIBODY; OVALBUMIN; PROTEASOME;

EID: 79953326945     PISSN: 09538178     EISSN: 14602377     Source Type: Journal    
DOI: 10.1093/intimm/dxq475     Document Type: Article
Times cited : (61)

References (30)
  • 1
    • 4143146210 scopus 로고    scopus 로고
    • Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo
    • Shen, L., Sigal, L. J., Boes, M. and Rock, K. L. 2004. Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo. Immunity 21:155.
    • (2004) Immunity , vol.21 , pp. 155
    • Shen, L.1    Sigal, L.J.2    Boes, M.3    Rock, K.L.4
  • 2
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses
    • Srivastava, P. 2002. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu. Rev. Immunol. 20:395.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 395
    • Srivastava, P.1
  • 3
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto, R. and Srivastava, P. K. 1995. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269:1585.
    • (1995) Science , vol.269 , pp. 1585
    • Suto, R.1    Srivastava, P.K.2
  • 4
    • 0033120990 scopus 로고    scopus 로고
    • Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells
    • Arnold-Schild, D., Hanau, D., Spehner, D. et al. 1999. Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells. J. Immunol. 162:3757.
    • (1999) J. Immunol. , vol.162 , pp. 3757
    • Arnold-Schild, D.1    Hanau, D.2    Spehner, D.3
  • 5
    • 0034608370 scopus 로고    scopus 로고
    • Receptormediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways
    • Castellino, F., Boucher, P. E., Eichelberg, K. et al. 2000. Receptormediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways. J. Exp. Med. 191:1957.
    • (2000) J. Exp. Med. , vol.191 , pp. 1957
    • Castellino, F.1    Boucher, P.E.2    Eichelberg, K.3
  • 6
    • 0034724336 scopus 로고    scopus 로고
    • Induction of cellular immunity by immunization with novel hybrid peptides complexed to heat shock protein 70
    • Moroi, Y., Mayhew, M., Trcka, J. et al. 2000. Induction of cellular immunity by immunization with novel hybrid peptides complexed to heat shock protein 70. Proc. Natl. Acad. Sci. USA 97:3485.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3485
    • Moroi, Y.1    Mayhew, M.2    Trcka, J.3
  • 7
    • 0034608387 scopus 로고    scopus 로고
    • Crosspresentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptormediated endocytosis
    • Singh-Jasuja, H., Toes, R. E., Spee, P. et al. 2000. Crosspresentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptormediated endocytosis. J. Exp. Med. 191:1965.
    • (2000) J. Exp. Med. , vol.191 , pp. 1965
    • Singh-Jasuja, H.1    Toes, R.E.2    Spee, P.3
  • 8
    • 0036237529 scopus 로고    scopus 로고
    • Transfer of GRP94(Gp96)-associated peptides onto endosomal MHC class I molecules
    • Berwin, B., Rosser, M. F., Brinker, K. G. and Nicchitta, C. V. 2002. Transfer of GRP94(Gp96)-associated peptides onto endosomal MHC class I molecules. Traffic 3:358.
    • (2002) Traffic , vol.3 , pp. 358
    • Berwin, B.1    Rosser, M.F.2    Brinker, K.G.3    Nicchitta, C.V.4
  • 9
    • 0028301079 scopus 로고
    • Comparison of tumorspecific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70
    • Udono, H. and Srivastava, P. K. 1994. Comparison of tumorspecific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70. J. Immunol. 152:5398.
    • (1994) J. Immunol. , vol.152 , pp. 5398
    • Udono, H.1    Srivastava, P.K.2
  • 10
    • 33646575879 scopus 로고    scopus 로고
    • Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway
    • Kunisawa, J. and Shastri, N. 2006. Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway. Immunity 24:523.
    • (2006) Immunity , vol.24 , pp. 523
    • Kunisawa, J.1    Shastri, N.2
  • 11
    • 40349088739 scopus 로고    scopus 로고
    • Heat-shock protein 90 associates with N-terminal extended peptides and is required for direct and indirect antigen presentation
    • Callahan, M. K., Garg, M. and Srivastava, P. K. 2008. Heat-shock protein 90 associates with N-terminal extended peptides and is required for direct and indirect antigen presentation. Proc. Natl. Acad. Sci. USA 105:1662.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1662
    • Callahan, M.K.1    Garg, M.2    Srivastava, P.K.3
  • 12
    • 34548654412 scopus 로고    scopus 로고
    • Efficient crosspresentation by heat shock protein 90-peptide complex-loaded dendritic cells via an endosomal pathway
    • Kurotaki, T., Tamura, Y., Ueda, G. et al. 2007. Efficient crosspresentation by heat shock protein 90-peptide complex-loaded dendritic cells via an endosomal pathway. J. Immunol. 179:1803.
    • (2007) J. Immunol. , vol.179 , pp. 1803
    • Kurotaki, T.1    Tamura, Y.2    Ueda, G.3
  • 13
    • 2442517310 scopus 로고    scopus 로고
    • Glycoprotein 96 can chaperone both MHC class I- and class II-restricted epitopes for in vivo presentation, but selectively primes CD8+ T cell effector function
    • Doody, A. D., Kovalchin, J. T., Mihalyo, M. A., Hagymasi, A. T., Drake, C. G. and Adler, A. J. 2004. Glycoprotein 96 can chaperone both MHC class I- and class II-restricted epitopes for in vivo presentation, but selectively primes CD8+ T cell effector function. J. Immunol. 172:6087.
    • (2004) J. Immunol. , vol.172 , pp. 6087
    • Doody, A.D.1    Kovalchin, J.T.2    Mihalyo, M.A.3    Hagymasi, A.T.4    Drake, C.G.5    Adler, A.J.6
  • 14
    • 3242811091 scopus 로고    scopus 로고
    • Heat shock protein-mediated cross-presentation of exogenous HIV antigen on HLA class I and class II
    • SenGupta, D., Norris, P. J., Suscovich, T. J. et al. 2004. Heat shock protein-mediated cross-presentation of exogenous HIV antigen on HLA class I and class II.. J. Immunol. 173:1987.
    • (2004) J. Immunol. , vol.173 , pp. 1987
    • SenGupta, D.1    Norris, P.J.2    Suscovich, T.J.3
  • 15
    • 27944442354 scopus 로고    scopus 로고
    • The heat shock protein Hsp70 enhances antigen-specific proliferation of human CD4+ memory T cells
    • Haug, M., Dannecker, L., Schepp, C. P. et al. 2005. The heat shock protein Hsp70 enhances antigen-specific proliferation of human CD4+ memory T cells. Eur. J. Immunol. 35:3163.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 3163
    • Haug, M.1    Dannecker, L.2    Schepp, C.P.3
  • 16
    • 78049397567 scopus 로고    scopus 로고
    • Heat shock protein 90 mediates efficient antigen cross presentation through the scavenger receptor expressed by endothelial cells-I
    • Murshid, A., Gong, J. and Calderwood, S. K. 2010. Heat shock protein 90 mediates efficient antigen cross presentation through the scavenger receptor expressed by endothelial cells-I. J. Immunol. 185:2903.
    • (2010) J. Immunol. , vol.185 , pp. 2903
    • Murshid, A.1    Gong, J.2    Calderwood, S.K.3
  • 17
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • Lakadamyali, M., Rust, M. J. and Zhuang, X. 2006. Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 124:997.
    • (2006) Cell , vol.124 , pp. 997
    • Lakadamyali, M.1    Rust, M.J.2    Zhuang, X.3
  • 18
    • 33646891148 scopus 로고    scopus 로고
    • The mannose receptor mediates uptake of soluble but not of cell-associated antigen for cross-presentation
    • Burgdorf, S., Lukacs-Kornek, V. and Kurts, C. 2006. The mannose receptor mediates uptake of soluble but not of cell-associated antigen for cross-presentation. J. Immunol. 176:6770.
    • (2006) J. Immunol. , vol.176 , pp. 6770
    • Burgdorf, S.1    Lukacs-Kornek, V.2    Kurts, C.3
  • 19
    • 33749512465 scopus 로고    scopus 로고
    • Exiting the outside world for cross-presentation
    • Rock, K. L. 2006. Exiting the outside world for cross-presentation. Immunity 25:523.
    • (2006) Immunity , vol.25 , pp. 523
    • Rock, K.L.1
  • 20
    • 78049374392 scopus 로고    scopus 로고
    • Essential role of endogenous heat shock protein 90 of dendritic cells in antigen cross-presentation
    • Ichiyanagi, T., Imai, T., Kajiwara, C. et al. 2010. Essential role of endogenous heat shock protein 90 of dendritic cells in antigen cross-presentation. J. Immunol. 185:2693.
    • (2010) J. Immunol. , vol.185 , pp. 2693
    • Ichiyanagi, T.1    Imai, T.2    Kajiwara, C.3
  • 21
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • Ratts, R., Zeng, H., Berg, E. A. et al. 2003. The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex. J. Cell. Biol. 160:1139.
    • (2003) J. Cell. Biol. , vol.160 , pp. 1139
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3
  • 22
    • 0346333312 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin: membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain
    • Haug, G., Wilde, C., Leemhuis, J., Meyer, D. K., Aktories, K. and Barth, H. 2003. Cellular uptake of Clostridium botulinum C2 toxin: membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain. Biochemistry 42:15284.
    • (2003) Biochemistry , vol.42 , pp. 15284
    • Haug, G.1    Wilde, C.2    Leemhuis, J.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6
  • 23
    • 33744961514 scopus 로고    scopus 로고
    • FGF-1 and FGF-2 require the cytosolic chaperone Hsp90 for translocation into the cytosol and the cell nucleus
    • Wesche, J., Malecki, J., Wiedlocha, A., Skjerpen, C. S., Claus, P. and Olsnes, S. 2006. FGF-1 and FGF-2 require the cytosolic chaperone Hsp90 for translocation into the cytosol and the cell nucleus. J. Biol. Chem. 281:11405.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11405
    • Wesche, J.1    Malecki, J.2    Wiedlocha, A.3    Skjerpen, C.S.4    Claus, P.5    Olsnes, S.6
  • 24
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes, F. A. and Dice, J. F. 2001. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J. Cell. Sci. 114:2491.
    • (2001) J. Cell. Sci. , vol.114 , pp. 2491
    • Agarraberes, F.A.1    Dice, J.F.2
  • 25
    • 19344373577 scopus 로고    scopus 로고
    • Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens
    • Zhou, D., Li, P., Lin, Y. et al. 2005. Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens. Immunity 22:571.
    • (2005) Immunity , vol.22 , pp. 571
    • Zhou, D.1    Li, P.2    Lin, Y.3
  • 26
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W. B. and Toft, D. O. 2003. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228:111.
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111
    • Pratt, W.B.1    Toft, D.O.2
  • 27
    • 12444339508 scopus 로고    scopus 로고
    • Exogenous antigens are processed through the endoplasmic reticulum-associated degradation (ERAD) in cross-presentation by dendritic cells
    • Imai, J., Hasegawa, H., Maruya, M., Koyasu, S. and Yahara, I. 2005. Exogenous antigens are processed through the endoplasmic reticulum-associated degradation (ERAD) in cross-presentation by dendritic cells. Int. Immunol. 17:45.
    • (2005) Int. Immunol. , vol.17 , pp. 45
    • Imai, J.1    Hasegawa, H.2    Maruya, M.3    Koyasu, S.4    Yahara, I.5
  • 28
    • 33749522738 scopus 로고    scopus 로고
    • A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells
    • Ackerman, A. L., Giodini, A. and Cresswell, P. 2006. A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells. Immunity 25:607.
    • (2006) Immunity , vol.25 , pp. 607
    • Ackerman, A.L.1    Giodini, A.2    Cresswell, P.3
  • 29
    • 0028352980 scopus 로고
    • Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90
    • Tsubuki, S., Saito, Y. and Kawashima, S. 1994. Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90. FEBS Lett. 344:229.
    • (1994) FEBS Lett , vol.344 , pp. 229
    • Tsubuki, S.1    Saito, Y.2    Kawashima, S.3
  • 30
    • 0037099735 scopus 로고    scopus 로고
    • Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing
    • Yamano, T., Murata, S., Shimbara, N. et al. 2002. Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing. J. Exp. Med. 196:185.
    • (2002) J. Exp. Med. , vol.196 , pp. 185
    • Yamano, T.1    Murata, S.2    Shimbara, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.