메뉴 건너뛰기




Volumn 44, Issue 6, 2007, Pages 1262-1273

Mouse CD40-transfected cell lines cannot exhibit the binding and RANTES-stimulating activity of exogenous heat shock protein 70

Author keywords

Ba F3; CD40; Heat shock protein 70; HEK 293; RANTES; Transfectant

Indexed keywords

CD40 ANTIGEN; CD40 LIGAND; CHEMOKINE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 72; PROTEIN DNAK; RANTES; RECOMBINANT PROTEIN;

EID: 33748791472     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2006.06.002     Document Type: Article
Times cited : (4)

References (43)
  • 2
    • 0034113617 scopus 로고    scopus 로고
    • Hsp70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A., Kraeft S.-K., Kurt-Jones E., Stevenson M.A., Chen L.B., Finberg R.W., Koo G.C., and Calderwood S.K. Hsp70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6 (2000) 435-442
    • (2000) Nat. Med. , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.-K.2    Kurt-Jones, E.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 3
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4
    • Asea A., Rehli M., Kabingu E., Boch J.A., Bare O., Auron P.E., Stevenson M.A., and Calderwood S.K. Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. J. Biol. Chem. 277 (2002) 15028-15034
    • (2002) J. Biol. Chem. , vol.277 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3    Boch, J.A.4    Bare, O.5    Auron, P.E.6    Stevenson, M.A.7    Calderwood, S.K.8
  • 5
    • 0037144808 scopus 로고    scopus 로고
    • CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes
    • Becker T., Hartl F.-U., and Wialand F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J. Cell Biol. 158 (2002) 1277-1285
    • (2002) J. Cell Biol. , vol.158 , pp. 1277-1285
    • Becker, T.1    Hartl, F.-U.2    Wialand, F.3
  • 6
    • 0345305789 scopus 로고    scopus 로고
    • Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells
    • Berwin B., Hart J.P., Rice S., Gass C., Pizzo S.V., Post S.R., and Nicchitta C. Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J. 22 (2003) 6127-6136
    • (2003) EMBO J. , vol.22 , pp. 6127-6136
    • Berwin, B.1    Hart, J.P.2    Rice, S.3    Gass, C.4    Pizzo, S.V.5    Post, S.R.6    Nicchitta, C.7
  • 7
    • 10944228434 scopus 로고    scopus 로고
    • SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin
    • Berwin B., Delneste Y., Lovingood R.V., Post S.R., and Pizzo S.V. SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. J. Biol. Chem. 279 (2004) 51250-51257
    • (2004) J. Biol. Chem. , vol.279 , pp. 51250-51257
    • Berwin, B.1    Delneste, Y.2    Lovingood, R.V.3    Post, S.R.4    Pizzo, S.V.5
  • 8
    • 0034252620 scopus 로고    scopus 로고
    • CD91: a receptor for heat shock protein gp96
    • Binder R.J., Han D.K., and Srivastava P.K. CD91: a receptor for heat shock protein gp96. Nat. Immunol. 1 (2000) 151-155
    • (2000) Nat. Immunol. , vol.1 , pp. 151-155
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 9
    • 4744371115 scopus 로고    scopus 로고
    • The heat-shock protein receptors: some answer and more questions
    • Binder R.J., Vatner R., and Srivastava P. The heat-shock protein receptors: some answer and more questions. Tissue Antigens 64 (2004) 442-451
    • (2004) Tissue Antigens , vol.64 , pp. 442-451
    • Binder, R.J.1    Vatner, R.2    Srivastava, P.3
  • 10
    • 0037072758 scopus 로고    scopus 로고
    • Differential acquisition of antigenic peptides by Hsp70 and Hsc70 under oxidative conditions
    • Callahan M.K., Chaillot D., Jacquin C., Clark P.R., and Menoret A. Differential acquisition of antigenic peptides by Hsp70 and Hsc70 under oxidative conditions. J. Biol. Chem. 277 (2002) 33604-33609
    • (2002) J. Biol. Chem. , vol.277 , pp. 33604-33609
    • Callahan, M.K.1    Chaillot, D.2    Jacquin, C.3    Clark, P.R.4    Menoret, A.5
  • 11
    • 0034608370 scopus 로고    scopus 로고
    • Receptor-mediated 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., Mayhew M., Rothman J.E., Houghton A.N., and Germain R.N. Receptor-mediated 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 (2000) 1957-1964
    • (2000) J. Exp. Med. , vol.191 , pp. 1957-1964
    • Castellino, F.1    Boucher, P.E.2    Eichelberg, K.3    Mayhew, M.4    Rothman, J.E.5    Houghton, A.N.6    Germain, R.N.7
  • 12
    • 0029812593 scopus 로고    scopus 로고
    • Ligation of CD40 on dendritic cells triggers production of high levels of IL-12 and enhances T cell stimulatory capacity: T-T help via APC activation
    • Cella M., Scheidegger D., Palmer-Lehmann K., Lane P., Lanzavecchia A., and Alber G. Ligation of CD40 on dendritic cells triggers production of high levels of IL-12 and enhances T cell stimulatory capacity: T-T help via APC activation. J. Exp. Med. 184 (1996) 747-752
    • (1996) J. Exp. Med. , vol.184 , pp. 747-752
    • Cella, M.1    Scheidegger, D.2    Palmer-Lehmann, K.3    Lane, P.4    Lanzavecchia, A.5    Alber, G.6
  • 13
    • 0033559496 scopus 로고    scopus 로고
    • Human 60-kDa heat-shock protein: a danger signal to the innate immune system
    • Chen W., Syldath U., Bellmann K., Burkart V., and Kolb H. Human 60-kDa heat-shock protein: a danger signal to the innate immune system. J. Immunol. 162 (1999) 3212-3219
    • (1999) J. Immunol. , vol.162 , pp. 3212-3219
    • Chen, W.1    Syldath, U.2    Bellmann, K.3    Burkart, V.4    Kolb, H.5
  • 16
    • 0037298742 scopus 로고    scopus 로고
    • Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94
    • Gross C., Hansch D., Gastpar R., and Multhoff G. Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94. Biol. Chem. 384 (2003) 267-279
    • (2003) Biol. Chem. , vol.384 , pp. 267-279
    • Gross, C.1    Hansch, D.2    Gastpar, R.3    Multhoff, G.4
  • 17
    • 0035525290 scopus 로고    scopus 로고
    • Cross-presentation in viral immunity and self-tolerance
    • Heath W.R., and Carbone F.R. Cross-presentation in viral immunity and self-tolerance. Nat. Rev. Immunol. 1 (2001) 126-134
    • (2001) Nat. Rev. Immunol. , vol.1 , pp. 126-134
    • Heath, W.R.1    Carbone, F.R.2
  • 18
    • 0028858649 scopus 로고
    • Stimulation of CD40 with purified soluble gp39 induces proinflammatory responses in human monocytes
    • Kiener P.A., Moran-Davis P., Rankin B.M., Wahl A.F., Aruffo A., and Hollengaugh D. Stimulation of CD40 with purified soluble gp39 induces proinflammatory responses in human monocytes. J. Immunol. 155 (1995) 4917-4925
    • (1995) J. Immunol. , vol.155 , pp. 4917-4925
    • Kiener, P.A.1    Moran-Davis, P.2    Rankin, B.M.3    Wahl, A.F.4    Aruffo, A.5    Hollengaugh, D.6
  • 19
    • 0033557202 scopus 로고    scopus 로고
    • Chlamydail and human heat shock protein 60s active human vascular endothelium, smooth muscle cells, and macrophages
    • Kol A., Bourcier T., Lichtman A.H., and Libby P. Chlamydail and human heat shock protein 60s active human vascular endothelium, smooth muscle cells, and macrophages. J. Clin. Invest. 103 (1999) 571-577
    • (1999) J. Clin. Invest. , vol.103 , pp. 571-577
    • Kol, A.1    Bourcier, T.2    Lichtman, A.H.3    Libby, P.4
  • 20
    • 0346849665 scopus 로고    scopus 로고
    • CD40, but not CD40L, is required for the optimal priming of T cells and control of aerosol M. tuberculosis infection
    • Lazarevic V., Myers A.J., Scanga C.A., and Flynn J.L. CD40, but not CD40L, is required for the optimal priming of T cells and control of aerosol M. tuberculosis infection. Immunity 19 (2003) 823-835
    • (2003) Immunity , vol.19 , pp. 823-835
    • Lazarevic, V.1    Myers, A.J.2    Scanga, C.A.3    Flynn, J.L.4
  • 21
    • 14844347510 scopus 로고    scopus 로고
    • Heat shock protein receptors, functions and their effect on monocytes and dendritic cells. van Eden W. (Ed), Birkhäuser Verlag, Basel, Switzerland
    • Lehner T., Wang Y., and Kelly C. Heat shock protein receptors, functions and their effect on monocytes and dendritic cells. In: van Eden W. (Ed). Heat Shock Proteins and Inflammation (2002), Birkhäuser Verlag, Basel, Switzerland 193-216
    • (2002) Heat Shock Proteins and Inflammation , pp. 193-216
    • Lehner, T.1    Wang, Y.2    Kelly, C.3
  • 22
    • 0347122087 scopus 로고    scopus 로고
    • Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo
    • Millar D.G., Garza K.M., Odermatt B., Elford A.R., Ono N., Li Z., and Ohashi P.S. Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo. Nat. Med. 9 (2003) 1469-1476
    • (2003) Nat. Med. , vol.9 , pp. 1469-1476
    • Millar, D.G.1    Garza, K.M.2    Odermatt, B.3    Elford, A.R.4    Ono, N.5    Li, Z.6    Ohashi, P.S.7
  • 23
    • 6344241182 scopus 로고    scopus 로고
    • Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity
    • Ohno M., Kitabatake N., and Tani F. Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity. FEBS Lett. 576 (2004) 381-386
    • (2004) FEBS Lett. , vol.576 , pp. 381-386
    • Ohno, M.1    Kitabatake, N.2    Tani, F.3
  • 24
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding
    • Palleros D.R., Welch W.J., and Fink A.L. Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 5719-5723
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 28
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • Srivastava P.K., Udono H., Blachere N.E., and Li Z. Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics 39 (1994) 93-98
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 29
    • 0032101221 scopus 로고    scopus 로고
    • Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world
    • Srivastava P.K., Menoret A., Basu S., Binder R.J., and McQuade K.L. Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world. Immunity 8 (1998) 657-665
    • (1998) Immunity , vol.8 , pp. 657-665
    • Srivastava, P.K.1    Menoret, A.2    Basu, S.3    Binder, R.J.4    McQuade, K.L.5
  • 30
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • Srivastava P.K. Roles of heat-shock proteins in innate and adaptive immunity. Nat. Rev. Immunol. 2 (2002) 185-194
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 185-194
    • Srivastava, P.K.1
  • 31
    • 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. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu. Rev. Immunol. 20 (2002) 395-425
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 32
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto R., and Srivasatava P.K. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269 (1995) 1585-1588
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivasatava, P.K.2
  • 33
    • 15544373100 scopus 로고    scopus 로고
    • Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells
    • Thériault J.R., Mambula S.S., Sawamura T., Stevenson M.A., and Calderwood S.K. Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells. FEBS Lett. 579 (2005) 1951-1960
    • (2005) FEBS Lett. , vol.579 , pp. 1951-1960
    • Thériault, J.R.1    Mambula, S.S.2    Sawamura, T.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 34
    • 0033179274 scopus 로고    scopus 로고
    • Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake
    • Todryk S., Melcher A.A., Hardwick N., Linardakis E., Bateman A., Colombo M.P., Stoppaciaro A., and Vile R.G. Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake. J. Immunol. 163 (1999) 1398-1408
    • (1999) J. Immunol. , vol.163 , pp. 1398-1408
    • Todryk, S.1    Melcher, A.A.2    Hardwick, N.3    Linardakis, E.4    Bateman, A.5    Colombo, M.P.6    Stoppaciaro, A.7    Vile, R.G.8
  • 35
  • 36
    • 0027260585 scopus 로고
    • Heat shock protein 70-associated peptides elicit specific cancer immunity
    • Udono H., and Srivastava P.K. Heat shock protein 70-associated peptides elicit specific cancer immunity. J. Exp. Med. 178 (1993) 1391-1396
    • (1993) J. Exp. Med. , vol.178 , pp. 1391-1396
    • Udono, H.1    Srivastava, P.K.2
  • 38
    • 0036721692 scopus 로고    scopus 로고
    • Stimulation of Th1-polarizing cytokines, C-C chemokines, maturation of dendritic cells, and adjuvant function by the peptide binding fragment of heat shock protein 70
    • Wang Y., Kelly C.G., Singh M., McGowan E.G., Carrara A.-S., Bergmeier L.A., and Lehner T. Stimulation of Th1-polarizing cytokines, C-C chemokines, maturation of dendritic cells, and adjuvant function by the peptide binding fragment of heat shock protein 70. J. Immunol. 169 (2002) 2422-2429
    • (2002) J. Immunol. , vol.169 , pp. 2422-2429
    • Wang, Y.1    Kelly, C.G.2    Singh, M.3    McGowan, E.G.4    Carrara, A.-S.5    Bergmeier, L.A.6    Lehner, T.7
  • 39
    • 14844355875 scopus 로고    scopus 로고
    • Identification of stimulating and inhibitory epitopes within the heat shock protein 70 molecule that modulate cytokine production and maturation of dendritic cells
    • Wang Y., Whittall T., McGowan E., Younson J., Kelly C., Bergmeier L.A., Singh M., and Lehner T. Identification of stimulating and inhibitory epitopes within the heat shock protein 70 molecule that modulate cytokine production and maturation of dendritic cells. J. Immunol. 174 (2005) 3306-3316
    • (2005) J. Immunol. , vol.174 , pp. 3306-3316
    • Wang, Y.1    Whittall, T.2    McGowan, E.3    Younson, J.4    Kelly, C.5    Bergmeier, L.A.6    Singh, M.7    Lehner, T.8
  • 40
    • 0032856673 scopus 로고    scopus 로고
    • Receptor mediated and fluid phase pathways for internalization of the ER Hsp90 chaperone GRP94 in murine macrophages
    • Wassenberg J.J., Dezfulian C., and Nicchitta C.V. Receptor mediated and fluid phase pathways for internalization of the ER Hsp90 chaperone GRP94 in murine macrophages. J. Cell Sci. 112 (1999) 2167-2175
    • (1999) J. Cell Sci. , vol.112 , pp. 2167-2175
    • Wassenberg, J.J.1    Dezfulian, C.2    Nicchitta, C.V.3
  • 41
    • 13244279524 scopus 로고    scopus 로고
    • Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33
    • Winter J., Linke K., Jatzek A., and Jakob U. Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33. Mol. Cell 17 (2005) 381-392
    • (2005) Mol. Cell , vol.17 , pp. 381-392
    • Winter, J.1    Linke, K.2    Jatzek, A.3    Jakob, U.4
  • 42
    • 0033062377 scopus 로고    scopus 로고
    • + T cell responses to infectious agents, tumors, transplants, and vaccines
    • + T cell responses to infectious agents, tumors, transplants, and vaccines. Adv. Immunol. 73 (1999) 1-77
    • (1999) Adv. Immunol. , vol.73 , pp. 1-77
    • Yewdell, J.W.1    Norbury, C.C.2    Bennink, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.