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Volumn 180, Issue 12, 2008, Pages 7989-8003

Inhibition of invariant chain processing, antigen-induced proliferative responses, and the development of collagen-induced arthritis and experimental autoimmune encephalomyelitis by a small molecule cysteine protease inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; COLLAGEN; CYSTEINE PROTEINASE INHIBITOR; INTERLEUKIN 1BETA; MYELIN BASIC PROTEIN; SB 33170; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; 5 (2 MORPHOLIN 4 YLETHOXY)BENZOFURAN 2 CARBOXYLIC ACID (3 METHYL 1 (3 OXO 1 (2 (3 PYRIDIN 2 YLPHENYL)ACETYL)AZEPAN 4 YLCARBAMOYL)BUTYL)AMIDE; 5-(2-MORPHOLIN-4-YLETHOXY)BENZOFURAN-2-CARBOXYLIC ACID (3-METHYL-1-(3-OXO-1-(2-(3-PYRIDIN-2-YLPHENYL)ACETYL)AZEPAN-4-YLCARBAMOYL)BUTYL)AMIDE; AZEPINE DERIVATIVE; B LYMPHOCYTE ANTIGEN; BENZOFURAN DERIVATIVE; CATHEPSIN; COLLAGEN TYPE 2; DRUG DERIVATIVE; HLA ANTIGEN CLASS 2; LEUCINE; PYRIDINE DERIVATIVE; SB 331750;

EID: 50949122918     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.180.12.7989     Document Type: Article
Times cited : (16)

References (65)
  • 1
    • 0022326904 scopus 로고
    • T-lymphocyte recognition of antigen in association with gene products of the major hislocompatibilily complex
    • Schwartz, R. H. 1985. T-lymphocyte recognition of antigen in association with gene products of the major hislocompatibilily complex. Annu. Rev. Immunol. 3: 237-261.
    • (1985) Annu. Rev. Immunol , vol.3 , pp. 237-261
    • Schwartz, R.H.1
  • 3
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey, K., and A. Y. Rudensky. 2003. Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol. 3: 472-482.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 4
    • 3242743087 scopus 로고    scopus 로고
    • The exogenous pathway for antigen presentation on major his-tocompatibility complex class II and CD1 molecules
    • Watts, C. 2004. The exogenous pathway for antigen presentation on major his-tocompatibility complex class II and CD1 molecules. Nat. Immunol. 5: 685-692.
    • (2004) Nat. Immunol , vol.5 , pp. 685-692
    • Watts, C.1
  • 5
    • 0030458137 scopus 로고    scopus 로고
    • HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules
    • Denzin, L. K., C. Hammond, and P. Cresswell. 1996. HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules. J. Exp. hied. 184: 2153-2165.
    • (1996) J. Exp. hied , vol.184 , pp. 2153-2165
    • Denzin, L.K.1    Hammond, C.2    Cresswell, P.3
  • 9
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • Shi, G.-P., R. A. R. Bryant, R. Riese, S. Verhelst, C. Driessen, Z. Li, D. Bromme, H. L. Ploegh, and H. A. Chapman. 2000. Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med. 191: 1177-1185.
    • (2000) J. Exp. Med , vol.191 , pp. 1177-1185
    • Shi, G.-P.1    Bryant, R.A.R.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6    Bromme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 12
    • 0038651151 scopus 로고    scopus 로고
    • Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs
    • Bania, J., E. Gatti, H. Lelouard, A. David, F. Cappello, E. Weber, V. Camosseto, and P. Pierre. 2003. Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs. Proc. Natl. Acad. Sci. USA 100: 6664-6669.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6664-6669
    • Bania, J.1    Gatti, E.2    Lelouard, H.3    David, A.4    Cappello, F.5    Weber, E.6    Camosseto, V.7    Pierre, P.8
  • 13
    • 12444288446 scopus 로고    scopus 로고
    • Cathepsin S controls MHC class II-mediated antigen presentation by epithelial cells in vivo
    • Beers, C, A. Burich, M. J. Kleijmeer, J. M. Griffith, P. Wong, and A. Y. Rudensky. 2005. Cathepsin S controls MHC class II-mediated antigen presentation by epithelial cells in vivo. J. Immunol. 174: 1205-1212.
    • (2005) J. Immunol , vol.174 , pp. 1205-1212
    • Beers, C.1    Burich, A.2    Kleijmeer, M.J.3    Griffith, J.M.4    Wong, P.5    Rudensky, A.Y.6
  • 14
    • 0030631403 scopus 로고    scopus 로고
    • Collagen-induced arthritis, an animal model of autoimmunity
    • Myers, L. K., E. F. Rosloniec, M. A. Cremer, and A. H. Kang. 1997. Collagen-induced arthritis, an animal model of autoimmunity. Life Sci. 61: 1861-1878.
    • (1997) Life Sci , vol.61 , pp. 1861-1878
    • Myers, L.K.1    Rosloniec, E.F.2    Cremer, M.A.3    Kang, A.H.4
  • 15
    • 0022361703 scopus 로고
    • Prevention of type II collagen-induced arthritis by in vivo treatment with anti-L3T4
    • Ranges, G. E., S. Sriram, and S. M. Cooper. 1985. Prevention of type II collagen-induced arthritis by in vivo treatment with anti-L3T4. J. Exp. Med. 162: 1105-1110.
    • (1985) J. Exp. Med , vol.162 , pp. 1105-1110
    • Ranges, G.E.1    Sriram, S.2    Cooper, S.M.3
  • 16
    • 15444369239 scopus 로고    scopus 로고
    • Ex vivo characterization of the autoimmune T cell response in the HLA-DR1 mouse model of collagen-induced arthritis reveals long-term activation of type II collagen-specific cells and their presence in arthritic joints
    • Latham, K. A., K. B. Whittington, R. Zhou, Z. Qian, and E. F. Rosloniec. 2005. Ex vivo characterization of the autoimmune T cell response in the HLA-DR1 mouse model of collagen-induced arthritis reveals long-term activation of type II collagen-specific cells and their presence in arthritic joints. J. Immunol. 174: 3978-3985.
    • (2005) J. Immunol , vol.174 , pp. 3978-3985
    • Latham, K.A.1    Whittington, K.B.2    Zhou, R.3    Qian, Z.4    Rosloniec, E.F.5
  • 17
    • 0019512029 scopus 로고
    • Type II collagen-induced arthritis in mice: I. Major histocompatibility complex (I region) linkage and antibody correlates
    • Wooley, P. H., H. S. Luthra, J. M. Stuart, and C. S. David. 1981. Type II collagen-induced arthritis in mice: I. Major histocompatibility complex (I region) linkage and antibody correlates. J. Exp. Med. 154: 688-700.
    • (1981) J. Exp. Med , vol.154 , pp. 688-700
    • Wooley, P.H.1    Luthra, H.S.2    Stuart, J.M.3    David, C.S.4
  • 18
    • 0022358989 scopus 로고
    • Type II collagen-induced arthritis in mice: IV. Variations in immunogenetic regulation provide evidence for multiple arthritogenic epitopes on the collagen molecule
    • Wooley, P. H., H. S. Luthra, M. M. Griffiths, J. M. Stuart, A. Huse, and C. S. David. 1985. Type II collagen-induced arthritis in mice: IV. Variations in immunogenetic regulation provide evidence for multiple arthritogenic epitopes on the collagen molecule. J. Immunol. 135: 2443-2451.
    • (1985) J. Immunol , vol.135 , pp. 2443-2451
    • Wooley, P.H.1    Luthra, H.S.2    Griffiths, M.M.3    Stuart, J.M.4    Huse, A.5    David, C.S.6
  • 19
    • 0028990462 scopus 로고
    • Immunologic mechanisms and therapy in multiple sclerosis
    • Hafler, D. A., and H. L. Weiner. 1995. Immunologic mechanisms and therapy in multiple sclerosis. Immunol. Rev. 144: 75-107.
    • (1995) Immunol. Rev , vol.144 , pp. 75-107
    • Hafler, D.A.1    Weiner, H.L.2
  • 20
    • 0028840828 scopus 로고
    • Experimental autoimmune encephalomyelitis in rodents as a model for human demyelinating disease
    • Swanborg, R. H. 1995. Experimental autoimmune encephalomyelitis in rodents as a model for human demyelinating disease. Clin. Immunol. Immunopathol. 77: 4-13.
    • (1995) Clin. Immunol. Immunopathol , vol.77 , pp. 4-13
    • Swanborg, R.H.1
  • 21
    • 0032209152 scopus 로고    scopus 로고
    • Antigen-driven regulation of experimental autoimmune encephalomyelitis
    • Kuchroo, V. K., and H. L. Weiner. 1998. Antigen-driven regulation of experimental autoimmune encephalomyelitis. Res. Immunol. 149: 759-771.
    • (1998) Res. Immunol , vol.149 , pp. 759-771
    • Kuchroo, V.K.1    Weiner, H.L.2
  • 22
    • 0021924965 scopus 로고
    • Major histocompatibility complex-linked control of the murine immune response to myelin basic protein
    • Fritz, R. B., M. J. Skeen, C.-H. Jen Chou, M. Garcia, and I. K. Egorov. 1985. Major histocompatibility complex-linked control of the murine immune response to myelin basic protein. J. Immunol. 134: 2328-2332.
    • (1985) J. Immunol , vol.134 , pp. 2328-2332
    • Fritz, R.B.1    Skeen, M.J.2    Jen Chou, C.-H.3    Garcia, M.4    Egorov, I.K.5
  • 23
    • 0025037062 scopus 로고
    • Inhibition of experimental autoimmune encephalomyelitis induction in SJL/J mice by using a peptide with high affinity for IAs molecules
    • Lamont, A. G., A. Sette, R. Fujinami, S. M. Colon, C. Miles, and H. M. Grey. 1990. Inhibition of experimental autoimmune encephalomyelitis induction in SJL/J mice by using a peptide with high affinity for IAs molecules. J. Immunol. 145: 1687-1693:
    • (1990) J. Immunol , vol.145 , pp. 1687-1693
    • Lamont, A.G.1    Sette, A.2    Fujinami, R.3    Colon, S.M.4    Miles, C.5    Grey, H.M.6
  • 25
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer, J. T., D. Rasnick, J. L. Klaus, and D. Bromme. 1995. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem. 38: 3193-3196.
    • (1995) J. Med. Chem , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Bromme, D.4
  • 28
    • 0038687865 scopus 로고    scopus 로고
    • Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
    • Bromme, D., Z. Li, M. Barnes, and E. Mehler. 1999. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry 38: 2377-2385.
    • (1999) Biochemistry , vol.38 , pp. 2377-2385
    • Bromme, D.1    Li, Z.2    Barnes, M.3    Mehler, E.4
  • 31
    • 0025083334 scopus 로고
    • Invariant chain trimers are sequestered in the rough endoplxsmic reticulum in the absence of association with HLA class II antigens
    • Marks, M. S., J. S. Blum, and P. Cresswell. 1990. Invariant chain trimers are sequestered in the rough endoplxsmic reticulum in the absence of association with HLA class II antigens. J. Cell Biol. 111: 839-855.
    • (1990) J. Cell Biol , vol.111 , pp. 839-855
    • Marks, M.S.1    Blum, J.S.2    Cresswell, P.3
  • 35
    • 0032989434 scopus 로고    scopus 로고
    • Converting enzyme-independent release of tumor necrosis factor-a and IL-1β from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3
    • Coeshott, C., C. Ohnemus, A. Pilyavskaya, S. Ross, M. Wieczorek, H. Kroona, A. H. Leimer, and J. Cheronis. 1999. Converting enzyme-independent release of tumor necrosis factor-a and IL-1β from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3. Proc. Natl. Acad Sci. USA 96: 6261-6266.
    • (1999) Proc. Natl. Acad Sci. USA , vol.96 , pp. 6261-6266
    • Coeshott, C.1    Ohnemus, C.2    Pilyavskaya, A.3    Ross, S.4    Wieczorek, M.5    Kroona, H.6    Leimer, A.H.7    Cheronis, J.8
  • 36
    • 12444250686 scopus 로고    scopus 로고
    • Cathepsin S is required for murine autoimmune myasthenia gravis pathogenesis
    • Yang, H., M. Kala, B. G. Scott, E. Goluszko, H. A. Chapman, and P. Christadoss. 2005. Cathepsin S is required for murine autoimmune myasthenia gravis pathogenesis. J. Immunol. 174: 1729-1737.
    • (2005) J. Immunol , vol.174 , pp. 1729-1737
    • Yang, H.1    Kala, M.2    Scott, B.G.3    Goluszko, E.4    Chapman, H.A.5    Christadoss, P.6
  • 37
    • 0035079963 scopus 로고    scopus 로고
    • Cysteine protease activity is up-regulated in inflamed ankle joints of rats with adjuvant-induced arthritis and decreases with in vivo administration of a vinyl sulfone cysteine protease inhibitor
    • Biroc, S. L., S. Gay, K. Hummel, C. Magill, J. T. Palmer, D. R. Spencer, S. Sa, J. L. Klaus, B. A. Michel, D. Rasnick, and R. E. Gay. 2001. Cysteine protease activity is up-regulated in inflamed ankle joints of rats with adjuvant-induced arthritis and decreases with in vivo administration of a vinyl sulfone cysteine protease inhibitor. Arthritis Rheum. 44: 703-711.
    • (2001) Arthritis Rheum , vol.44 , pp. 703-711
    • Biroc, S.L.1    Gay, S.2    Hummel, K.3    Magill, C.4    Palmer, J.T.5    Spencer, D.R.6    Sa, S.7    Klaus, J.L.8    Michel, B.A.9    Rasnick, D.10    Gay, R.E.11
  • 39
    • 0028921633 scopus 로고
    • Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II
    • Sette, A., S. Southwood, J. Miller, and E. Appella. 1995. Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II. J. Exp. Med. 181: 677-683.
    • (1995) J. Exp. Med , vol.181 , pp. 677-683
    • Sette, A.1    Southwood, S.2    Miller, J.3    Appella, E.4
  • 40
    • 0028676010 scopus 로고
    • In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides
    • Avva, R. R., and P. Cresswell. 1994. In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides. Immunity 1: 763-774.
    • (1994) Immunity , vol.1 , pp. 763-774
    • Avva, R.R.1    Cresswell, P.2
  • 41
    • 0030790341 scopus 로고    scopus 로고
    • Degradation of mouse invariant chain: Roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism
    • Villadangos, J. A., R. J. Riese, C. Peters, H. A. Chapman, and H. L. Ploegh. 1997. Degradation of mouse invariant chain: roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism. J. Exp. Med. 186: 549-560.
    • (1997) J. Exp. Med , vol.186 , pp. 549-560
    • Villadangos, J.A.1    Riese, R.J.2    Peters, C.3    Chapman, H.A.4    Ploegh, H.L.5
  • 42
    • 0035892760 scopus 로고    scopus 로고
    • Rheumatoid arthritis (RA)-associated HLA-DR alleles form less stable complexes with class II-associated invariant chain peptide than non-RA-associated HLA-DR alleles
    • Patil, N. S., A. Pashine, M. P. Belmares, W. Liu, B. Kaneshiro, J. Rabinowitz, H. McConnell, and E. D. Mellins. 2001. Rheumatoid arthritis (RA)-associated HLA-DR alleles form less stable complexes with class II-associated invariant chain peptide than non-RA-associated HLA-DR alleles. J. Immunol. 167: 7157-7168.
    • (2001) J. Immunol , vol.167 , pp. 7157-7168
    • Patil, N.S.1    Pashine, A.2    Belmares, M.P.3    Liu, W.4    Kaneshiro, B.5    Rabinowitz, J.6    McConnell, H.7    Mellins, E.D.8
  • 43
    • 0030473602 scopus 로고    scopus 로고
    • Modulation of HLA-DQ binding properties by differences in class II dimer stability and pH-dependent peptide interactions
    • Buckner, J., W. W. Kwok, B. Nepon, and G. T. Nepom. 1996. Modulation of HLA-DQ binding properties by differences in class II dimer stability and pH-dependent peptide interactions. J. Immunol. 157: 4940-4945.
    • (1996) J. Immunol , vol.157 , pp. 4940-4945
    • Buckner, J.1    Kwok, W.W.2    Nepon, B.3    Nepom, G.T.4
  • 44
    • 0033532631 scopus 로고    scopus 로고
    • pH-dependent peptide binding properties of the type 1 diabetes-associated I-As7 molecule: Rapid release of CLIP at an endosomal pH
    • Hausmann, D. H. F., B. Yu, S. Hausmann, and K. W. Wucherpfennig. 1999. pH-dependent peptide binding properties of the type 1 diabetes-associated I-As7 molecule: rapid release of CLIP at an endosomal pH. J. Exp. Med. 189: 1723-1733.
    • (1999) J. Exp. Med , vol.189 , pp. 1723-1733
    • Hausmann, D.H.F.1    Yu, B.2    Hausmann, S.3    Wucherpfennig, K.W.4
  • 46
    • 1642342937 scopus 로고    scopus 로고
    • Effect of decreasing the affinity of the class II-associated invariant chain peptide on the MHC class II peptide repertoire in the presence or absence of H-2M
    • Honey, K., K. Forbush, P. E. Jensen, and A. Y. Rudensky. 2004. Effect of decreasing the affinity of the class II-associated invariant chain peptide on the MHC class II peptide repertoire in the presence or absence of H-2M. J. Immunol. 172: 4142-4150.
    • (2004) J. Immunol , vol.172 , pp. 4142-4150
    • Honey, K.1    Forbush, K.2    Jensen, P.E.3    Rudensky, A.Y.4
  • 47
    • 0026583941 scopus 로고
    • Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistant α β heterodimers in endosomes
    • Neefjes, J. J., and H. L. Ploegh. 1992. Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistant α β heterodimers in endosomes. EMBO J. 11: 411-416.
    • (1992) EMBO J , vol.11 , pp. 411-416
    • Neefjes, J.J.1    Ploegh, H.L.2
  • 48
    • 0027232592 scopus 로고
    • Invariant chain retains MHC class II molecules in the endocytic pathway
    • Loss, G. E., and A. J. Sant. 1993. Invariant chain retains MHC class II molecules in the endocytic pathway. J. Immunol. 150: 3187-3197.
    • (1993) J. Immunol , vol.150 , pp. 3187-3197
    • Loss, G.E.1    Sant, A.J.2
  • 49
    • 0035081835 scopus 로고    scopus 로고
    • The transmembrane segment of invariant chain mediates binding to MHC class II molecules in a CLIP-indepen-dent manner
    • Castellino, F., R. Han, and R. N. Germain. 2001. The transmembrane segment of invariant chain mediates binding to MHC class II molecules in a CLIP-indepen-dent manner. Eur. J. Immunol. 31: 841-850.
    • (2001) Eur. J. Immunol , vol.31 , pp. 841-850
    • Castellino, F.1    Han, R.2    Germain, R.N.3
  • 50
    • 0037087364 scopus 로고    scopus 로고
    • A role for cathepsin L and cathepsin S in peptide generation of MHC class II presentation
    • Hsieh, C.-S., P. deRoos, K. Honey, C. Beers, and A. Y. Rudensky. 2002. A role for cathepsin L and cathepsin S in peptide generation of MHC class II presentation. J. Immunol. 168: 2618-2625.
    • (2002) J. Immunol , vol.168 , pp. 2618-2625
    • Hsieh, C.-S.1    deRoos, P.2    Honey, K.3    Beers, C.4    Rudensky, A.Y.5
  • 53
    • 0035666656 scopus 로고    scopus 로고
    • Cathepsin S and an asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro
    • Beck, H., G. Schwartz, C. J. Schröter, M. Deeg, D. Baier, S. Stevanovic, E. Weber, C. Driessen, and H. Kalbacher. 2001. Cathepsin S and an asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro. Eur. J. Immunol. 31: 3726-3736.
    • (2001) Eur. J. Immunol , vol.31 , pp. 3726-3736
    • Beck, H.1    Schwartz, G.2    Schröter, C.J.3    Deeg, M.4    Baier, D.5    Stevanovic, S.6    Weber, E.7    Driessen, C.8    Kalbacher, H.9
  • 55
    • 14044271507 scopus 로고    scopus 로고
    • The role of macrophages in rheumatoid arthritis
    • Ma, Y., and R. M. Pope. 2005. The role of macrophages in rheumatoid arthritis. Curr. Pharm. Des. 11: 569-580.
    • (2005) Curr. Pharm. Des , vol.11 , pp. 569-580
    • Ma, Y.1    Pope, R.M.2
  • 56
    • 0029979369 scopus 로고    scopus 로고
    • Biological basis for interleukin-1 in disease
    • Dinarello, C. A. 1996. Biological basis for interleukin-1 in disease. Blood 87: 2095-2147.
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 57
    • 85036810675 scopus 로고    scopus 로고
    • Aggarwal, B. B., A. Samanta, and M. Feldmann. 2001. TNFα. In Cytokine Reference. J. J. Oppcnheim and M. Feldmann, eds. Academic Press, San Diego, pp. 413-434.
    • Aggarwal, B. B., A. Samanta, and M. Feldmann. 2001. TNFα. In Cytokine Reference. J. J. Oppcnheim and M. Feldmann, eds. Academic Press, San Diego, pp. 413-434.
  • 58
    • 0034778328 scopus 로고    scopus 로고
    • Requirement for endocytic antigen processing and influence of invariant chain and H-2M deficiencies in CNS autoim-munity
    • Slavin, A. J., J. M. Soos, O. Stuve, J. C. Patarroyo, H. L. Weiner, A. Fontana, E. K. Bikoff, and S. S. Zamvil. 2001. Requirement for endocytic antigen processing and influence of invariant chain and H-2M deficiencies in CNS autoim-munity. J. Clin. Invest. 108: 1133-1139.
    • (2001) J. Clin. Invest , vol.108 , pp. 1133-1139
    • Slavin, A.J.1    Soos, J.M.2    Stuve, O.3    Patarroyo, J.C.4    Weiner, H.L.5    Fontana, A.6    Bikoff, E.K.7    Zamvil, S.S.8
  • 59
    • 0037090253 scopus 로고    scopus 로고
    • De novo central nervous system processing of myelin antigen is required for the initiation of experimental autoimmune encephalomyelitis
    • Tompkins, S. M., J. Padilla, M. C. Dal Canto, J. P. Y. Ting, L. Van Kaer, and S. D. Miller. 2002. De novo central nervous system processing of myelin antigen is required for the initiation of experimental autoimmune encephalomyelitis. J. Immunol. 168: 4173-4183.
    • (2002) J. Immunol , vol.168 , pp. 4173-4183
    • Tompkins, S.M.1    Padilla, J.2    Dal Canto, M.C.3    Ting, J.P.Y.4    Van Kaer, L.5    Miller, S.D.6
  • 61
    • 0034964922 scopus 로고    scopus 로고
    • Immunocompetent astrocytes and microglia display major differences in the processing of the invariant chain and in the expression of active cathepsin L and cathepsin S
    • Gresser, O., E. Weber, A. Hellwig, S. Riese, and A. Régnier- Vigouroux. 2001. Immunocompetent astrocytes and microglia display major differences in the processing of the invariant chain and in the expression of active cathepsin L and cathepsin S. Eur. J. Immunol. 31: 1813-1824.
    • (2001) Eur. J. Immunol , vol.31 , pp. 1813-1824
    • Gresser, O.1    Weber, E.2    Hellwig, A.3    Riese, S.4    Régnier- Vigouroux, A.5
  • 62
    • 0026628844 scopus 로고
    • Immune regulation by brain cells in the central nervous system: Microglia but not astrocytes present myelin basic protein to encephalitogenic T cells under in vivo-mimicking conditions
    • Matsumoto, Y., K. Ohmori, and M. Fujiwara. 1992. Immune regulation by brain cells in the central nervous system: microglia but not astrocytes present myelin basic protein to encephalitogenic T cells under in vivo-mimicking conditions. Immunology 76: 209-216.
    • (1992) Immunology , vol.76 , pp. 209-216
    • Matsumoto, Y.1    Ohmori, K.2    Fujiwara, M.3
  • 63
    • 0028970282 scopus 로고
    • Antigen presentation by human fetal astrocytes with the cooperative effect of microglia or the microglial-derived cytokine IL-1
    • Williams, K. C, N. P. Dooley, E. Ulvestad, A. Waage, M. Blain, V. W. Yong, and J. P. Antel. 1995. Antigen presentation by human fetal astrocytes with the cooperative effect of microglia or the microglial-derived cytokine IL-1. J. Neurosci. 15: 1869-1878.
    • (1995) J. Neurosci , vol.15 , pp. 1869-1878
    • Williams, K.C.1    Dooley, N.P.2    Ulvestad, E.3    Waage, A.4    Blain, M.5    Yong, V.W.6    Antel, J.P.7
  • 64
    • 0031568084 scopus 로고    scopus 로고
    • IFN-γ-activated primary murine astrocytes express B7 costimulatory molecules and prime naive antigen-specific T cells
    • Nikcevich, K. M., K. B. Gordon, L. Tan, S. D. Hurst, J. Kroepfl, M. Gardinier, T. A. Barrett, and S. D. Miller. 1997. IFN-γ-activated primary murine astrocytes express B7 costimulatory molecules and prime naive antigen-specific T cells. J. Immunol. 158: 614-621.
    • (1997) J. Immunol , vol.158 , pp. 614-621
    • Nikcevich, K.M.1    Gordon, K.B.2    Tan, L.3    Hurst, S.D.4    Kroepfl, J.5    Gardinier, M.6    Barrett, T.A.7    Miller, S.D.8
  • 65
    • 0032524997 scopus 로고    scopus 로고
    • Microglia are more efficient than astrocytes in antigen processing and in Th1 but not Th2 cell activation
    • Aloisi, F., F. Ria, G. Penna, and L. Adorini. 1998. Microglia are more efficient than astrocytes in antigen processing and in Th1 but not Th2 cell activation. J. Immunol. 160: 4671-4680.
    • (1998) J. Immunol , vol.160 , pp. 4671-4680
    • Aloisi, F.1    Ria, F.2    Penna, G.3    Adorini, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.