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Volumn 6, Issue 6, 2000, Pages 224-230

HLA-B27 misfolding: A solution to the spondyloarthropathy conundrum?

Author keywords

[No Author keywords available]

Indexed keywords

HLA B27 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

EID: 0034214169     PISSN: 13574310     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-4310(00)01699-3     Document Type: Note
Times cited : (108)

References (46)
  • 1
    • 0001458101 scopus 로고    scopus 로고
    • Ankylosing spondylitis: Clinical aspects
    • A. Calin, & J.D. Taurog. Oxford University Press
    • Khan A. Ankylosing spondylitis: clinical aspects. Calin A., Taurog J.D. The Spondyloarthritides. 1998;27-40 Oxford University Press.
    • (1998) The Spondyloarthritides , pp. 27-40
    • Khan, A.1
  • 2
    • 0031726849 scopus 로고    scopus 로고
    • Genes in the spondyloarthropathies
    • Wordsworth P. Genes in the spondyloarthropathies. Rheum. Dis. Clin. North Am. 24:1998;845-863.
    • (1998) Rheum. Dis. Clin. North Am. , vol.24 , pp. 845-863
    • Wordsworth, P.1
  • 3
    • 0015938046 scopus 로고
    • Ankylosing spondylitis and HL-A 27
    • Brewerton D.A.et al. Ankylosing spondylitis and HL-A 27. Lancet. 1:1973;904-907.
    • (1973) Lancet , vol.1 , pp. 904-907
    • Brewerton, D.A.1
  • 4
    • 0015914854 scopus 로고
    • High association of an HL-A antigen, W27, with ankylosing spondylitis
    • Schlosstein L.et al. High association of an HL-A antigen, W27, with ankylosing spondylitis. New Engl. J. Med. 288:1973;704-706.
    • (1973) New Engl. J. Med. , vol.288 , pp. 704-706
    • Schlosstein, L.1
  • 5
    • 0344835943 scopus 로고    scopus 로고
    • The role of HLA-B27 polymorphism and molecular mimicry in spondyloarthropathy
    • Lopez-Larrea C.et al. The role of HLA-B27 polymorphism and molecular mimicry in spondyloarthropathy. Mol. Med. Today. 4:1998;540-549.
    • (1998) Mol. Med. Today , vol.4 , pp. 540-549
    • Lopez-Larrea, C.1
  • 6
    • 0032833157 scopus 로고    scopus 로고
    • HLA-B27 associated spondyloarthropathy, an autoimmune disease based on crossreactivity between bacteria and HLA-B27?
    • Ringrose J.H. HLA-B27 associated spondyloarthropathy, an autoimmune disease based on crossreactivity between bacteria and HLA-B27? Ann. Rheum. Dis. 58:1999;598-610.
    • (1999) Ann. Rheum. Dis. , vol.58 , pp. 598-610
    • Ringrose, J.H.1
  • 7
    • 0030299910 scopus 로고    scopus 로고
    • Presentation of HLA class I-derived peptides: Potential involvement in allorecognition and HLA-B27-associated arthritis
    • Parham P. Presentation of HLA class I-derived peptides: potential involvement in allorecognition and HLA-B27-associated arthritis. Immunol. Rev. 154:1996;137-154.
    • (1996) Immunol. Rev. , vol.154 , pp. 137-154
    • Parham, P.1
  • 8
    • 0027362510 scopus 로고
    • Chemical reactivity of an HLA-B27 thiol group
    • Whelan M.A., Archer J.R. Chemical reactivity of an HLA-B27 thiol group. Eur. J. Immunol. 23:1993;3278-3285.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 3278-3285
    • Whelan, M.A.1    Archer, J.R.2
  • 9
    • 0030942755 scopus 로고    scopus 로고
    • HLA-B27 modulates intracellular survival of Salmonella enteritidis in human monocytic cells
    • Laitio P.et al. HLA-B27 modulates intracellular survival of Salmonella enteritidis in human monocytic cells. Eur. J. Immunol. 27:1997;1331-1338.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1331-1338
    • Laitio, P.1
  • 10
    • 0031975660 scopus 로고    scopus 로고
    • Expression of arthritis-causing HLA-B27 on Hela cells promotes induction of c-fos in response to in vitro invasion by Salmonella typhimurium
    • Ikawa T.et al. Expression of arthritis-causing HLA-B27 on Hela cells promotes induction of c-fos in response to in vitro invasion by Salmonella typhimurium. J. Clin. Invest. 101:1998;263-272.
    • (1998) J. Clin. Invest. , vol.101 , pp. 263-272
    • Ikawa, T.1
  • 11
    • 0032742012 scopus 로고    scopus 로고
    • Misfolding of HLA-B27 as a result of its B pocket suggests a novel mechanism for its role in susceptibility to spondyloarthropathies
    • Mear J.P.et al. Misfolding of HLA-B27 as a result of its B pocket suggests a novel mechanism for its role in susceptibility to spondyloarthropathies. J. Immunol. 163:1999;6665-6670.
    • (1999) J. Immunol. , vol.163 , pp. 6665-6670
    • Mear, J.P.1
  • 12
    • 0031435103 scopus 로고    scopus 로고
    • HLA class I polymorphism: Structure and function and still questions
    • Kostyu D.D.et al. HLA class I polymorphism: Structure and function and still questions. Hum. Immunol. 57:1997;1-18.
    • (1997) Hum. Immunol. , vol.57 , pp. 1-18
    • Kostyu, D.D.1
  • 13
    • 0027399243 scopus 로고
    • Peptides naturally presented by MHC class I molecules
    • Rammensee H-G.et al. Peptides naturally presented by MHC class I molecules. Ann. Rev. Immunol. 11:1993;213-244.
    • (1993) Ann. Rev. Immunol. , vol.11 , pp. 213-244
    • Rammensee, H.-G.1
  • 14
    • 0034101516 scopus 로고    scopus 로고
    • HLA-B27 polymorphism and association with disease
    • Khan M.A. HLA-B27 polymorphism and association with disease. J. Rheumatol. 27:2000;1110-1114.
    • (2000) J. Rheumatol. , vol.27 , pp. 1110-1114
    • Khan, M.A.1
  • 15
    • 0032838314 scopus 로고    scopus 로고
    • Immunogenetics, HLA-B27 and spondyloarthropathies
    • Gonzalez S.et al. Immunogenetics, HLA-B27 and spondyloarthropathies. Curr. Opin. Rheumatol. 11:1999;257-264.
    • (1999) Curr. Opin. Rheumatol. , vol.11 , pp. 257-264
    • Gonzalez, S.1
  • 16
    • 0027210015 scopus 로고
    • Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide
    • Colbert R.A.et al. Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide. Proc. Natl. Acad. Sci. U. S. A. 90:1993;6879-6883.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 6879-6883
    • Colbert, R.A.1
  • 17
    • 0028426881 scopus 로고
    • Differences in peptide presentation between B27 subtypes: The importance of the P1 side chain in maintaining high affinity peptide binding to B*2703
    • Colbert R.A.et al. Differences in peptide presentation between B27 subtypes: the importance of the P1 side chain in maintaining high affinity peptide binding to B*2703. Immunity. 1:1994;121-130.
    • (1994) Immunity , vol.1 , pp. 121-130
    • Colbert, R.A.1
  • 18
    • 0030455722 scopus 로고    scopus 로고
    • Differences in endogenous peptides presented by HLA-B*2705 and B*2703 allelic variants
    • Boisgerault F.et al. Differences in endogenous peptides presented by HLA-B*2705 and B*2703 allelic variants. J. Clin. Invest. 989:1996;2764-2770.
    • (1996) J. Clin. Invest. , vol.989 , pp. 2764-2770
    • Boisgerault, F.1
  • 19
    • 0031573143 scopus 로고    scopus 로고
    • Naturally occurring A pocket polymorphism in HLA-B*2703 increases the dependence on an accessory anchor residue at P1 for optimal binding of nonamer peptides
    • Griffin T.A.et al. Naturally occurring A pocket polymorphism in HLA-B*2703 increases the dependence on an accessory anchor residue at P1 for optimal binding of nonamer peptides. J. Immunol. 159:1997;4887-4897.
    • (1997) J. Immunol. , vol.159 , pp. 4887-4897
    • Griffin, T.A.1
  • 20
    • 0031051908 scopus 로고    scopus 로고
    • Susceptibility to ankylosing spondylitis correlates with the C-terminal residue of peptides presented by various HLA-B27 subtypes
    • Fiorillo M.T.et al. Susceptibility to ankylosing spondylitis correlates with the C-terminal residue of peptides presented by various HLA-B27 subtypes. Eur. J. Immunol. 27:1997;368-373.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 368-373
    • Fiorillo, M.T.1
  • 21
    • 0032533802 scopus 로고    scopus 로고
    • HLA-B27 subtype polymorphism and CTL epitope choice: Studies with EBV peptides link immunogenicity with stability of the B27:peptide complex
    • Brooks J.M.et al. HLA-B27 subtype polymorphism and CTL epitope choice: studies with EBV peptides link immunogenicity with stability of the B27:peptide complex. J. Immunol. 161:1998;5252-5259.
    • (1998) J. Immunol. , vol.161 , pp. 5252-5259
    • Brooks, J.M.1
  • 22
    • 0033495770 scopus 로고    scopus 로고
    • Modulation at multiple anchor positions of the peptide specificity of HLA-B27 subtypes differentially associated with ankylosing spondylitis
    • Lamas J.R.et al. Modulation at multiple anchor positions of the peptide specificity of HLA-B27 subtypes differentially associated with ankylosing spondylitis. Arthritis Rheum. 42:1999;1975-1985.
    • (1999) Arthritis Rheum. , vol.42 , pp. 1975-1985
    • Lamas, J.R.1
  • 23
    • 0028851885 scopus 로고
    • Association of HLA-B39 with HLA-B27-negative ankylosing spondylitis and pauciarticular juvenile rheumatoid arthritis in Japanese patients: Evidence for a role of the peptide-anchoring B pocket
    • Yamaguchi A.et al. Association of HLA-B39 with HLA-B27-negative ankylosing spondylitis and pauciarticular juvenile rheumatoid arthritis in Japanese patients: Evidence for a role of the peptide-anchoring B pocket. Arthritis Rheum. 38:1995;1672-1677.
    • (1995) Arthritis Rheum. , vol.38 , pp. 1672-1677
    • Yamaguchi, A.1
  • 24
    • 0013579017 scopus 로고    scopus 로고
    • HLA-B27 polymorphism and worldwide susceptibility to ankylosing spondylitis
    • Gonzalez-Roces S.et al. HLA-B27 polymorphism and worldwide susceptibility to ankylosing spondylitis. Tissue Antigens. 49:1997;116-123.
    • (1997) Tissue Antigens , vol.49 , pp. 116-123
    • Gonzalez-Roces, S.1
  • 25
    • 0031019845 scopus 로고    scopus 로고
    • Ankylosing spondylitis in West Africans - Evidence for a non-HLA-B27 protective effect
    • Brown M.A.et al. Ankylosing spondylitis in West Africans - evidence for a non-HLA-B27 protective effect. Ann. Rheum. Dis. 56:1997;68-70.
    • (1997) Ann. Rheum. Dis. , vol.56 , pp. 68-70
    • Brown, M.A.1
  • 26
    • 0032806580 scopus 로고    scopus 로고
    • Inflammatory disease in HLA-B27 transgenic rats
    • Taurog J.D.et al. Inflammatory disease in HLA-B27 transgenic rats. Immunol. Rev. 169:1999;209-223.
    • (1999) Immunol. Rev. , vol.169 , pp. 209-223
    • Taurog, J.D.1
  • 27
    • 4243217491 scopus 로고    scopus 로고
    • 2m-deficient mice occurs in the absence of HLA-B27 and is strain dependent
    • 2m-deficient mice occurs in the absence of HLA-B27 and is strain dependent. Arthritis Rheum. 41:1998;S346.
    • (1998) Arthritis Rheum. , vol.41
    • Kingsbury, D.J.1
  • 28
    • 0031726068 scopus 로고    scopus 로고
    • Animal models of human leukocyte antigen B27-linked arthritides
    • Khare S.D.et al. Animal models of human leukocyte antigen B27-linked arthritides. Rheum. Dis. Clin. North Am. 24:1998;883-894.
    • (1998) Rheum. Dis. Clin. North Am. , vol.24 , pp. 883-894
    • Khare, S.D.1
  • 29
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer E., Cresswell P. Mechanisms of MHC class I-restricted antigen processing. Ann. Rev. Immunol. 16:1998;323-358.
    • (1998) Ann. Rev. Immunol. , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 30
    • 0031051852 scopus 로고    scopus 로고
    • Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome
    • Hughes E.A.et al. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl. Acad. Sci. U. S. A. 94:1997;1896-1901.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1896-1901
    • Hughes, E.A.1
  • 31
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz E.J.H.J.et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature. 384:1996;432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.H.J.1
  • 32
    • 0030152620 scopus 로고    scopus 로고
    • A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL
    • Peace-Brewer A.L.et al. A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL. Immunity. 4:1996;505-514.
    • (1996) Immunity , vol.4 , pp. 505-514
    • Peace-Brewer, A.L.1
  • 33
    • 0030865333 scopus 로고    scopus 로고
    • A critical role for tapasin in the assembly and function of multimeric class I-TAP complexes
    • Ortmann B.et al. A critical role for tapasin in the assembly and function of multimeric class I-TAP complexes. Science. 277:1997;1306-1309.
    • (1997) Science , vol.277 , pp. 1306-1309
    • Ortmann, B.1
  • 34
    • 0345465663 scopus 로고    scopus 로고
    • Integration of endoplasmic reticulum signaling in health and disease
    • Aridor M., Balch W.E. Integration of endoplasmic reticulum signaling in health and disease. Nat. Med. 5:1999;745-751.
    • (1999) Nat. Med. , vol.5 , pp. 745-751
    • Aridor, M.1    Balch, W.E.2
  • 35
    • 0032779694 scopus 로고    scopus 로고
    • Signal transduction from the endoplasmic reticulum to the cell nucleus
    • Pahl H.L. Signal transduction from the endoplasmic reticulum to the cell nucleus. Physiol. Rev. 79:1999;683-701.
    • (1999) Physiol. Rev. , vol.79 , pp. 683-701
    • Pahl, H.L.1
  • 36
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle P.A., Henkel T. Function and activation of NF-κB in the immune system. Ann. Rev. Immunol. 12:1994;141-179.
    • (1994) Ann. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 37
    • 0032587402 scopus 로고    scopus 로고
    • NF-κB-mediated self defense of macrophages faced with bacteria
    • Kitamura M. NF-κB-mediated self defense of macrophages faced with bacteria. Eur. J. Immunol. 29:1999;1647-1655.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1647-1655
    • Kitamura, M.1
  • 38
    • 4243220686 scopus 로고    scopus 로고
    • MHC class I molecules modulate LPS-induced NF-κB activation in U937 human monocytic cells
    • Penttinen M.A.et al. MHC class I molecules modulate LPS-induced NF-κB activation in U937 human monocytic cells. Arthritis Rheum. 42:1999;S385.
    • (1999) Arthritis Rheum. , vol.42
    • Penttinen, M.A.1
  • 39
    • 0033136630 scopus 로고    scopus 로고
    • 2-microglobulin-free heavy chain homodimer structure
    • 2-microglobulin-free heavy chain homodimer structure. J. Immunol. 162:1999;5045-5048.
    • (1999) J. Immunol. , vol.162 , pp. 5045-5048
    • Allen, R.L.1
  • 40
    • 0027219916 scopus 로고
    • 2-microglobulin dissociation
    • 2-microglobulin dissociation. J. Immunol. 151:1993;159-169.
    • (1993) J. Immunol. , vol.151 , pp. 159-169
    • Capps, G.G.1
  • 42
    • 0028917871 scopus 로고
    • HLA-B27 as a relative risk factor in ankylosing enthesopathy in transgenic mice
    • Weinreich S.et al. HLA-B27 as a relative risk factor in ankylosing enthesopathy in transgenic mice. Hum. Immunol. 42:1995;103-115.
    • (1995) Hum. Immunol. , vol.42 , pp. 103-115
    • Weinreich, S.1
  • 43
    • 3543113108 scopus 로고    scopus 로고
    • The specificity of peptides bound to HLA-B27 influences the prevalence of arthritis in HLA-B27 transgenic rats
    • Zhou M.et al. The specificity of peptides bound to HLA-B27 influences the prevalence of arthritis in HLA-B27 transgenic rats. J. Exp. Med. 188:1998;877-886.
    • (1998) J. Exp. Med. , vol.188 , pp. 877-886
    • Zhou, M.1
  • 44
    • 0029083655 scopus 로고
    • 2-microglobulin: A model of human spondyloarthropathies
    • 2-microglobulin: a model of human spondyloarthropathies. J. Exp. Med. 182:1995;1153-1158.
    • (1995) J. Exp. Med. , vol.182 , pp. 1153-1158
    • Khare, S.D.1
  • 45
    • 0031930270 scopus 로고    scopus 로고
    • Spontaneous inflammatory disease in HLA-B27 transgenic mice is independent of MHC class II molecules: A direct role for B27 heavy chains and not B27-derived peptides
    • Khare S.D.et al. Spontaneous inflammatory disease in HLA-B27 transgenic mice is independent of MHC class II molecules: a direct role for B27 heavy chains and not B27-derived peptides. J. Immunol. 160:1998;101-106.
    • (1998) J. Immunol. , vol.160 , pp. 101-106
    • Khare, S.D.1
  • 46
    • 13344293690 scopus 로고    scopus 로고
    • Association of HLA types A1-B8-DR3 and B27 with rapid and slow progression of HIV disease
    • McNeil A.J.et al. Association of HLA types A1-B8-DR3 and B27 with rapid and slow progression of HIV disease. Q. J. Med. 89:1996;177-185.
    • (1996) Q. J. Med. , vol.89 , pp. 177-185
    • McNeil, A.J.1


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