메뉴 건너뛰기




Volumn 194, Issue 11, 2015, Pages 5103-5109

A humanized monoclonal antibody against heat shock protein 60 suppresses murine arthritis and colitis and skews the cytokine balance toward an anti-inflammatory response

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFLAMMATORY AGENT; ANTIRHEUMATIC AGENT; BEVACIZUMAB; CD3 ANTIBODY; CHAPERONIN 60; ETANERCEPT; GAMMA INTERFERON; INTERLEUKIN 1; INTERLEUKIN 10; INTERLEUKIN 17; INTERLEUKIN 4; INTERLEUKIN 6; METHYLPREDNISOLONE SODIUM SUCCINATE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY CD28; PROZUMAB; RITUXIMAB; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; HEAT-SHOCK PROTEIN 65, MYCOBACTERIUM; IL10 PROTEIN, HUMAN; IL6 PROTEIN, HUMAN; PROTEIN BINDING;

EID: 84929630175     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1500023     Document Type: Article
Times cited : (20)

References (26)
  • 1
    • 0028905901 scopus 로고
    • Immunoglobulins from rats that are resistant to adjuvant arthritis suppress the disease in arthritis-susceptible rats
    • Ulmansky, R., and Y. Naparstek. 1995. Immunoglobulins from rats that are resistant to adjuvant arthritis suppress the disease in arthritis-susceptible rats. Eur. J. Immunol. 25: 952-957.
    • (1995) Eur. J. Immunol , vol.25 , pp. 952-957
    • Ulmansky, R.1    Naparstek, Y.2
  • 2
    • 0037097641 scopus 로고    scopus 로고
    • Resistance to adjuvant arthritis is due to protective antibodies against heat shock protein surface epitopes and the induction of IL-10 secretion
    • Ulmansky, R., C. J. Cohen, F. Szafer, E. Moallem, Z. G. Fridlender, Y. Kashi, and Y. Naparstek. 2002. Resistance to adjuvant arthritis is due to protective antibodies against heat shock protein surface epitopes and the induction of IL-10 secretion. J. Immunol. 168: 6463-6469.
    • (2002) J. Immunol , vol.168 , pp. 6463-6469
    • Ulmansky, R.1    Cohen, C.J.2    Szafer, F.3    Moallem, E.4    Fridlender, Z.G.5    Kashi, Y.6    Naparstek, Y.7
  • 5
    • 14644439827 scopus 로고    scopus 로고
    • Illuminating the role of type i IFNs in colitis
    • Wirtz, S., and M. F. Neurath. 2005. Illuminating the role of type I IFNs in colitis. J. Clin. Invest. 115: 586-588.
    • (2005) J. Clin. Invest , vol.115 , pp. 586-588
    • Wirtz, S.1    Neurath, M.F.2
  • 7
    • 34548190038 scopus 로고    scopus 로고
    • Il-6 signaling in inflammatory bowel disease: Pathophysiological role and clinical relevance
    • Mudter, J., and M. F. Neurath. 2007. Il-6 signaling in inflammatory bowel disease: pathophysiological role and clinical relevance. Inflamm. Bowel Dis. 13: 1016-1023.
    • (2007) Inflamm. Bowel Dis , vol.13 , pp. 1016-1023
    • Mudter, J.1    Neurath, M.F.2
  • 8
    • 0036218221 scopus 로고    scopus 로고
    • The immunology of mucosal models of inflammation
    • Strober, W., I. J. Fuss, and R. S. Blumberg. 2002. The immunology of mucosal models of inflammation. Annu. Rev. Immunol. 20: 495-549.
    • (2002) Annu. Rev. Immunol , vol.20 , pp. 495-549
    • Strober, W.1    Fuss, I.J.2    Blumberg, R.S.3
  • 9
    • 33749343778 scopus 로고    scopus 로고
    • Critical appraisal of the current practice in murine TNBS-induced colitis
    • te Velde, A. A., M. I. Verstege, and D. W. Hommes. 2006. Critical appraisal of the current practice in murine TNBS-induced colitis. Inflamm. Bowel Dis. 12: 995-999.
    • (2006) Inflamm. Bowel Dis , vol.12 , pp. 995-999
    • Te Velde, A.A.1    Verstege, M.I.2    Hommes, D.W.3
  • 10
    • 0031147756 scopus 로고    scopus 로고
    • Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells
    • Soltys, B. J., and R. S. Gupta. 1997. Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol. Int. 21: 315-320.
    • (1997) Cell Biol. Int , vol.21 , pp. 315-320
    • Soltys, B.J.1    Gupta, R.S.2
  • 12
    • 74049129476 scopus 로고    scopus 로고
    • Integrating the cell stress response: A new view of molecular chaperones as immunological and physiological homeostatic regulators
    • Henderson, B. 2010. Integrating the cell stress response: a new view of molecular chaperones as immunological and physiological homeostatic regulators. Cell Biochem. Funct. 28: 1-14.
    • (2010) Cell Biochem. Funct , vol.28 , pp. 1-14
    • Henderson, B.1
  • 13
    • 17144417382 scopus 로고    scopus 로고
    • Heat-shock proteins induce T-cell regulation of chronic inflammation
    • van Eden, W., R. van der Zee, and B. Prakken. 2005. Heat-shock proteins induce T-cell regulation of chronic inflammation. Nat. Rev. Immunol. 5: 318-330.
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 318-330
    • Van Eden, W.1    Zee Der R.Van2    Prakken, B.3
  • 14
    • 0025978905 scopus 로고
    • A monoclonal antibody to the mycobacterial 65 kDa heat shock protein (ML 30) binds to cells in normal and arthritic joints of rats
    • Kleinau, S., K. Söderström, R. Kiessling, and L. Klareskog. 1991. A monoclonal antibody to the mycobacterial 65 kDa heat shock protein (ML 30) binds to cells in normal and arthritic joints of rats. Scand. J. Immunol. 33: 195-202.
    • (1991) Scand. J. Immunol , vol.33 , pp. 195-202
    • Kleinau, S.1    Söderström, K.2    Kiessling, R.3    Klareskog, L.4
  • 17
    • 79751531096 scopus 로고    scopus 로고
    • The HSP60 immune system network
    • Quintana, F. J., and I. R. Cohen. 2011. The HSP60 immune system network. Trends Immunol. 32: 89-95.
    • (2011) Trends Immunol , vol.32 , pp. 89-95
    • Quintana, F.J.1    Cohen, I.R.2
  • 18
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex
    • Ohashi, K., V. Burkart, S. Flohé, and H. Kolb. 2000. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex. J. Immunol. 164: 558-561.
    • (2000) J. Immunol , vol.164 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohé, S.3    Kolb, H.4
  • 20
    • 0043205830 scopus 로고    scopus 로고
    • T cells respond to heat shock protein 60 via TLR2: Activation of adhesion and inhibition of chemokine receptors
    • Zanin-Zhorov, A., G. Nussbaum, S. Franitza, I. R. Cohen, and O. Lider. 2003. T cells respond to heat shock protein 60 via TLR2: activation of adhesion and inhibition of chemokine receptors. FASEB J. 17: 1567-1569.
    • (2003) FASEB J , vol.17 , pp. 1567-1569
    • Zanin-Zhorov, A.1    Nussbaum, G.2    Franitza, S.3    Cohen, I.R.4    Lider, O.5
  • 21
    • 0034937409 scopus 로고    scopus 로고
    • Heat shock proteins as "danger signals": Eukaryotic Hsp60 enhances and accelerates antigen-specific IFN-g production in T cells
    • Breloer, M., B. Dorner, S. H. Moré, T. Roderian, B. Fleischer, and A. von Bonin. 2001. Heat shock proteins as "danger signals": eukaryotic Hsp60 enhances and accelerates antigen-specific IFN-g production in T cells. Eur. J. Immunol. 31: 2051-2059.
    • (2001) Eur. J. Immunol , vol.31 , pp. 2051-2059
    • Breloer, M.1    Dorner, B.2    Moré, S.H.3    Roderian, T.4    Fleischer, B.5    Von Bonin, A.6
  • 22
    • 33947510303 scopus 로고    scopus 로고
    • Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide
    • Osterloh, A., U. Kalinke, S. Weiss, B. Fleischer, and M. Breloer. 2007. Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide. J. Biol. Chem. 282: 4669-4680.
    • (2007) J. Biol. Chem , vol.282 , pp. 4669-4680
    • Osterloh, A.1    Kalinke, U.2    Weiss, S.3    Fleischer, B.4    Breloer, M.5
  • 23
    • 0035944844 scopus 로고    scopus 로고
    • B-Cell function in new-onset type 1 diabetes and immunomodulation with a heat-shock protein peptide (DiaPep277): A randomised, double-blind, phase II trial
    • Raz, I., D. Elias, A. Avron, M. Tamir, M. Metzger, and I. R. Cohen. 2001. b-Cell function in new-onset type 1 diabetes and immunomodulation with a heat-shock protein peptide (DiaPep277): a randomised, double-blind, phase II trial. Lancet 358: 1749-1753.
    • (2001) Lancet , vol.358 , pp. 1749-1753
    • Raz, I.1    Elias, D.2    Avron, A.3    Tamir, M.4    Metzger, M.5    Cohen, I.R.6
  • 25
    • 0036065042 scopus 로고    scopus 로고
    • Inhibition of adjuvant-induced arthritis by interleukin-10-driven regulatory cells induced via nasal administration of a peptide analog of an arthritis-related heat-shock protein 60 T cell epitope
    • Prakken, B. J., S. Roord, P. J. van Kooten, J. P. Wagenaar, W. van Eden, S. Albani, and M. H. Wauben. 2002. Inhibition of adjuvant-induced arthritis by interleukin-10-driven regulatory cells induced via nasal administration of a peptide analog of an arthritis-related heat-shock protein 60 T cell epitope. Arthritis Rheum. 46: 1937-1946.
    • (2002) Arthritis Rheum , vol.46 , pp. 1937-1946
    • Prakken, B.J.1    Roord, S.2    Van Kooten, P.J.3    Wagenaar, J.P.4    Van Eden, W.5    Albani, S.6    Wauben, M.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.