Best Practice & Research Clinical Rheumatology
Volume 20, Issue 3 , Pages 571-591 , June 2006

Pathogenesis of ankylosing spondylitis: Current concepts

References 

  1. Schlosstein L, Terasaki PI, Bluestone R, Pearson CM. High association of an HL-A antigen, W27, with ankylosing spondylitis. The New England Journal of Medicine. 1973;288:704–706
  2. Brewerton DA, Hart FD, Nicholls A, et al. Ankylosing spondylitis and HL-A 27. Lancet. 1973;1:904–907
  3. Sims AM, Wordsworth BP, Brown MA. Genetic susceptibility to ankylosing spondylitis. Current Molecular Medicine. 2004;4:13–20
  4. Francois RJ, Gardner DL, Degrave EJ, Bywaters EG. Histopathologic evidence that sacroiliitis in ankylosing spondylitis is not merely enthesitis. Arthritis and Rheumatism. 2000;43:2011–2024
  5. Braun J, Bollow M, Neure L, et al. Use of immunohistologic and in situ hybridization techniques in the examination of sacroiliac joint biopsy specimens from patients with ankylosing spondylitis. Arthritis and Rheumatism. 1995;38:499–505
  6. Bollow M, Fischer T, Reisshauer H, et al. Quantitative analyses of sacroiliac biopsies in spondyloarthropathies: T-cells and macrophages predominate in early and active sacroiliitis-cellularity correlates with the degree of enhancementdetected by magnetic resonance imaging. Annals of the Rheumatic Diseases. 2000;59:135–140
  7. Baeten D, De Keyser F. The histopathology of spondyloarthropathy. Current Molecular Medicine. 2004;4:1–12
  8. Veale D, Yanni G, Rogers S, et al. Reduced synovial membrane macrophage numbers, ELAM-1 expression, and lining layer hyperplasia in psoriatic arthritis as compared with rheumatoid arthritis. Arthritis and Rheumatism. 1993;36:893–900
  9. Reece RJ, Canete JD, Parsons WJ, et al. Distinct vascular patterns of early synovitis in psoriatic, reactive, and rheumatoid arthritis. Arthritis and Rheumatism. 1999;42:1481–1484
  10. Baeten D, Demetter P, Cuvelier C, et al. Comparative study of the synovial histology in rheumatoid arthritis, spondyloarthropathy, and osteoarthritis: influence of disease duration and activity. Annals of the Rheumatic Diseases. 2000;59:945–953
  11. Baeten D, Demetter P, Cuvelier CA, et al. Macrophages expressing the scavenger receptor CD163: a link between immune alterations of the gut and synovial inflammation in spondyloarthropathy. The Journal of Pathology. 2002;196:343–350
  12. Smeets TJ, Dolhain RJ, Breedveld FC, Tak PP. Analysis of the cellular infiltrates and expression of cytokines in synovial tissue from patients with rheumatoid arthritis and reactive arthritis. The Journal of Pathology. 1998;186:75–81
  13. Kraan MC, Haringman JJ, Post WJ, et al. Immunohistological analysis of synovial tissue for differential diagnosis in early arthritis. Rheumatology (Oxford, England). 1999;38:1074–1080
  14. Baeten D, Moller HJ, Delanghe J, et al. Association of CD163+ macrophages and local production of soluble CD163 with decreased lymphocyte activation in spondylarthropathy synovitis. Arthritis and Rheumatism. 2004;50:1611–1623
  15. Seta N, Granfors K, Sahly H, et al. Expression of host defense scavenger receptors in spondylarthropathy. Arthritis and Rheumatism. 2001;44:931–939
  16. Laloux L, Voisin MC, Allain J, et al. Immunohistological study of entheses in spondyloarthropathies: comparison in rheumatoid arthritis and osteoarthritis. Annals of the Rheumatic Diseases. 2001;60:316–321
  17. McGonagle D, Marzo-Ortega H, O'Connor P, et al. Histological assessment of the early enthesitis lesion in spondyloarthropathy. Annals of the Rheumatic Diseases. 2002;61:534–537
  18. Kievits F, Ivanyi P, Krimpenfort P, et al. HLA-restricted recognition of viral antigens in HLA transgenic mice. Nature. 1987;329:447–449
  19. Krimpenfort P, Rudenko G, Hochstenbach F, et al. Crosses of two independently derived transgenic mice demonstrate functional complementation of the genes encoding heavy (HLA-B27) and light (β2-microglobulin) chains of HLA class I antigens. The EMBO Journal. 1987;6:1673–1676
  20. Weinreich S, Hoebe-Hewryk B, van der Horst AR, et al. The role of MHC class I heterodimer expression in mouse ankylosing enthesopathy. Immunogenetics. 1997;46:35–40
  21. Rehakova Z, Capkova J, Stepankova R, et al. Germ-free mice do not develop ankylosing enthesopathy, a spontaneous joint disease. Human Immunology. 2000;61:555–558
  22. Khare SD, Luthra HS, David CS. Spontaneous inflammatory arthritis in HLA-B27 transgenic mice lacking β2-microglobulin: a model of human spondyloarthropathies. The Journal of Experimental Medicine. 1995;182:1153–1158
  23. Hammer RE, Maika SD, Richardson JA, et al. Spontaneous inflammatory disease in transgenic rats expressing HLA-B27 and human β2-m: an animal model of HLA-B27-associated human disorders. Cell. 1990;63:1099–1112
  24. Taurog JD, Maika SD, Satumtira N, et al. Inflammatory disease in HLA-B27 transgenic rats. Immunological Reviews. 1999;169:209–223
  25. Breban M, Hammer RE, Richardson JA, Taurog JD. Transfer of the inflammatory disease of HLA-B27 transgenic rats by bone marrow engraftment. The Journal of Experimental Medicine. 1993;178:1607–1616
  26. Breban M, Fernandez-Sueiro JL, Richardson JA, et al. T-cells, but not thymic exposure to HLA-B27, are required for the inflammatory disease of HLA-B27 transgenic rats. Journal of Immunology. 1996;156:794–803
  27. May E, Dorris ML, Satumtira N, et al. CD8αβ T-cells are not essential to the pathogenesis of arthritis or colitis in HLA-B27 transgenic rats. Journal of Immunology. 2003;170:1099–1105
  28. Taurog JD, Richardson JA, Croft JT, et al. The germfree state prevents development of gut and joint inflammatory disease in HLA-B27 transgenic rats. The Journal of Experimental Medicine. 1994;180:2359–2364
  29. Rath HC, Herfarth HH, Ikeda JS, et al. Normal luminal bacteria, especially bacteroides species, mediate chronic colitis, gastritis, and arthritis in HLA-B27/human β2 microglobulin transgenic rats. The Journal of Clinical Investigation. 1996;98:945–953
  30. Rath HC, Wilson KH, Sartor RB. Differential induction of colitis and gastritis in HLA-B27 transgenic rats selectively colonized with Bacteroides vulgatus or Escherichia coli. Infection and Immunity. 1999;67:2969–2974
  31. Sartor RB. Colitis in HLA-B27/beta 2 microglobulin transgenic rats. International Reviews of Immunology. 2000;19:39–50
  32. Dieleman LA, Hoentjen F, Qian BF, et al. Reduced ratio of protective versus proinflammatory cytokine responses to commensal bacteria in HLA-B27 transgenic rats. Clinical and Experimental Immunology. 2004;136:30–39
  33. Colmegna I, Cuchacovich R, Espinoza LR. HLA-B27-associated reactive arthritis: pathogenetic and clinical considerations. Clinical Microbiology Reviews. 2004;17:348–369
  34. De Keyser F, Elewaut D, De Vos M, et al. Bowel inflammation and the spondyloarthropathies. Rheumatic Diseases Clinics of North America. 1998;24:785–813
  35. Lionetti P, Pupi A, Veltroni M, et al. Evidence of subclinical intestinal inflammation by 99mtechnetium leukocyte scintigraphy in patients with HLA-B27 postiive juvenile onset active spondyloarthropathy. The Journal of Rheumatology. 2000;27:
  36. Demetter P, De Vos M, Van Huysse JA, et al. Colon mucosa of both spondyloarthritis and Crohn's disease patients is enriched with macrophages expressing the scavenger receptor CD163. Annals of the Rheumatic Diseases. 2005;64:321–324
  37. De Keyser F, Baeten D, Van den Bosch F, et al. Gut inflammation and spondyloarthropathies. Current Rheumatology Reports. 2002;4:525–532
  38. Keller C, Webb A, Davis J. Cytokines in the seronegative spondyloarthropathies and their modification by TNF blockade: a brief report and literature review. Annals of the Rheumatic Diseases. 2003;62:1128–1132
  39. Sonel B, Tutkak H, Duzgun N. Serum levels of IL-1 beta, TNF-alpha, IL-8, and acute phase proteins in seronegative spondyloarthropathies. Joint, Bone, Spine. 2002;69:463–467
  40. Gratacos J, Collado A, Filella X, et al. Serum cytokines (IL-6, TNF-alpha, IL-1 beta and IFN-gamma) in ankylosing spondylitis: a close correlation between serum IL-6 and disease activity and severity. British Journal of Rheumatology. 1994;33:927–931
  41. Claudepierre P, Rymer JC, Chevalier X. IL-10 plasma levels correlate with disease activity in spondyloarthropathy. The Journal of Rheumatology. 1997;24:1659–1661
  42. Bas S, Kvien TK, Buchs N, et al. Lower level of synovial fluid interferon-gamma in HLA-B27-positive than in HLA-B27-negative patients with Chlamydia trachomatis reactive arthritis. Rheumatology (Oxford, England). 2003;42:461–467
  43. Rudwaleit M, Siegert S, Yin Z, et al. Low T-cell production of TNFα and IFN γ in ankylosing spondylitis: its relation to HLA-B27 and influence of the TNF-308 gene polymorphism. Annals of the Rheumatic Diseases. 2001;60:36–42
  44. Zou J, Rudwaleit M, Brandt J, et al. Up regulation of the production of tumour necrosis factor alpha and interferon gamma by T-cells in ankylosing spondylitis during treatment with etanercept. Annals of the Rheumatic Diseases. 2003;62:561–564
  45. Zou J, Rudwaleit M, Brandt J, et al. Down-regulation of the nonspecific and antigen-specific T-cell cytokine response in ankylosing spondylitis during treatment with infliximab. Arthritis and Rheumatism. 2003;48:780–790
  46. Iwasaki A, Medzhitov R. Toll-like receptor control of the adaptive immune responses. Nature Immunology. 2004;5:987–995
  47. Akira S, Takeda K. Toll-like receptor signalling. Nature Reviews. Immunology. 2004;4:499–511
  48. Corr M. The tolls of arthritis. Arthritis and Rheumatism. 2005;52:2233–2236
  49. Gautier G, Humbert M, Deauvieau F, et al. A type I interferon autocrine-paracrine loop is involved in Toll-like receptor-induced interleukin-12p70 secretion by dendritic cells. The Journal of Experimental Medicine. 2005;201:1435–1446
  50. Yamamoto M, Sato S, Hemmi H, et al. Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway. Science. 2003;301:640–643
  51. Asea A, Rehli M, Kabingu E, et al. Novel signal transduction pathway utilized by extracellular HSP70: role of Toll-like receptor (TLR) 2 and TLR4. The Journal of Biological Chemistry. 2002;277:15028–15034
  52. Okamura Y, Watari M, Jerud ES, et al. The extra domain A of fibronectin activates Toll-like receptor 4. The Journal of Biological Chemistry. 2001;276:10229–10233
  53. Beg AA. Endogenous ligands of Toll-like receptors: implications for regulating inflammatory and immune responses. Trends in Immunology. 2002;23:509–512
  54. Radstake TR, Roelofs MF, Jenniskens YM, et al. Expression of Toll-like receptors 2 and 4 in rheumatoid synovial tissue and regulation by proinflammatory cytokines interleukin-12 and interleukin-18 via interferon-gamma. Arthritis and Rheumatism. 2004;50:3856–3865
  55. De Rycke L, Vandooren B, Kruithof E, et al. Tumor necrosis factor alpha blockade treatment down-modulates the increased systemic and local expression of Toll-like receptor 2 and Toll-like receptor 4 in spondylarthropathy. Arthritis and Rheumatism. 2005;52:2146–2158
  56. Cario E, Podolsky DK. Differential alteration in intestinal epithelial cell expression of Toll-like receptor 3 (TLR3) and TLR4 in inflammatory bowel disease. Infection and Immunity. 2000;68:7010–7017
  57. Benjamin RJ, Parham P. Guilt by association: HLA-B27 and ankylosing spondylitis. Immunology Today. 1990;11:137–142
  58. Edwards JCW, Bowness P, Archer JR. Jekyll and Hyde: the transformation of HLA-B27. Immunology Today. 2000;21:256–260
  59. Colbert RA. HLA-B27 misfolding: a solution to the spondyloarthropathy conundrum?. Molecular Medicine Today. 2000;6:224–230
  60. Penttinen MA, Ekman P, Granfors K. Non-antigen presenting effects of HLA-B27. Current Molecular Medicine. 2004;4:41–49
  61. Ringrose JH. HLA-B27 associated spondyloarthropathy, an autoimmune disease based on crossreactivity between bacteria and HLA-B27?. Annals of the Rheumatic Diseases. 1999;58:598–610
  62. Hermann E, Yu DTY, Meyer zum Buschenfelde K-H, Fleischer B. HLA-B27-restricted CD8 T-cells from synovial fluids of patients with reactive arthritis and ankylosing spondylitis. Lancet. 1993;342:646–650
  63. Ugrinovic S, Mertz A, Wu P, et al. A single nonamer from the yersinia 60-kDa heat shock protein is the target of HLA-B27-restricted CTL response in yersinia-induced reactive arthritis. Journal of Immunology. 1997;159:5715–5723
  64. Kuon W, Holzhutter H-G, Appel H, et al. Identification of HLA-B27-restricted peptides from Chlamydia trachomatis proteome with possible relevance to HLA-B27-associated disease. Journal of Immunology. 2001;167:4738–4746
  65. Duchmann R, Lambert C, May E, et al. CD4+ and CD8+ clonal T-cell expansions indicate a role of antigens in ankylosing spondylitis; a study in HLA-B27+ monozygotic twins. Clinical and Experimental Immunology. 2001;123:315–322
  66. Scofield RH, Kurien B, Gross T, et al. HLA-B27 binding of peptide from its own sequence and similar peptides from bacteria: implications for spondyloarthropathies. Lancet. 1995;345:1542–1544
  67. Frauendorf E, von Goessel H, May E, Marker-Hermann E. HLA-B27-restricted T-cells from patients with ankylosing spondylitis recognize peptides from B*2705 that are similar to bacteria-derived peptides. Clinical and Experimental Immunology. 2003;134:351–359
  68. Fiorillo MT, Maragno M, Butler R, et al. CD8+T-cell autoreactivity to an HLA-B27-restricted self-epitope correlates with ankylosing spondylitis. The Journal of Clinical Investigation. 2000;106:47–53
  69. Hülsmeyer M, Fiorillo MT, Bettosini F, et al. Dual, HLA-B27 subtype-dependent conformation of a self-peptide. The Journal of Experimental Medicine. 2004;199:271–281
  70. Leishman AJ, Naidenko OV, Attinger A, et al. T-cell responses modulated through interaction between CD8alphaalpha and the nonclassical MHC class I molecule, TL. Science. 2001;294:1936–1939
  71. Allen RL, O'Callaghan CA, McMichael AJ, Bowness P. HLA-B27 can form a novel β2-microglobulin-free heavy chain homodimer structure. Journal of Immunology. 1999;162:5045–5048
  72. Bird LA, Peh CA, Kollnberger S, et al. Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling. European Journal of Immunology. 2003;33:748–759
  73. Malik P, Klimovitsky P, Deng LW, et al. Uniquely conformed peptide-containing beta 2-microglobulin-free heavy chains of HLA-B2705 on the cell surface. Journal of Immunology. 2002;169:4379–4387
  74. Dangoria NS, DeLay ML, Kingsbury DJ, et al. HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum. The Journal of Biological Chemistry. 2002;277:23459–23468
  75. Kollnberger S, Bird LA, S M-Y, et al. Cell surface expression and immune receptor recogntion of HLA-B27 homodimers. Arthritis and Rheumatism. 2002;46:2972–2982
  76. Kollnberger S, Bird LA, Roddis M, et al. HLA-B27 heavy chain homodimers are expressed in HLA-B27 transgenic rodent models of spondyloarthritis and are ligands for paired Ig-like receptors. Journal of Immunology. 2004;173:1699–1710
  77. Chan AT, Kollnberger SD, Wedderburn LR, Bowness P. Expansion and enhanced survival of natural killer cells expressing the killer immunoglobulin-like receptor KIR3DL2 in spondylarthritis. Arthritis and Rheumatism. 2005;52:3586–3595
  78. Boyle LH, Goodall JC, Opat SS, Gaston JSH. The recognition of HLA-B27 by human CD4+T lymphocytes. Journal of Immunology. 2001;167:2619–2624
  79. Virtala M, Kirveskari J, Granfors K. HLA-B27 modulates the survival of Salmonella enteritidis in transfected L cells, possibly by impaired nitric oxide production. Infection and Immunity. 1997;65:2436–4242
  80. Laitio P, Virtala M, Salmi M, et al. HLA-B27 modulates intracellular survival of Salmonella enteritidis in human monocytic cells. European Journal of Immunology. 1997;27:1331–1338
  81. Penttinen MA, Heiskanen KM, Mohapatra R, et al. Enhanced intracellular replication of Salmonella enteritidis in HLA-B27-expressing human monocytic cells: dependency on glutamic acid at position 45 in the B pocket of HLA-B27. Arthritis and Rheumatism. 2004;50:2255–2263
  82. Saarinen M, Ekman P, Ikeda M, et al. Invasion of salmonella into human intestinal epithelial cells is modulated by HLA-B27. Rheumatology (Oxford, England). 2002;41:651–657
  83. Huppertz HI, Heesemann J. Invasion and persistence of salmonella in human fibroblasts positive or negative for endogenous HLA B27. Annals of the Rheumatic Diseases. 1997;56:671–676
  84. Young JL, Smith L, Matyszak MK, Gaston JSH. HLA-B27 expression does not modulate intracellular Chlamydia trachomatis infection of cell lines. Infection and Immunity. 2001;69:6670–6675
  85. Kuipers JG, Bialowons A, Dollman P, et al. The modulation of chlamydial replication by HLA-B27 depends on the cytoplasmic domain of HLA-B27. Clinical and Experimental Rheumatology. 2001;19:47–52
  86. Mear JP, Schreiber KL, Munz C, et al. Misfolding of HLA-B27 as a result of its B pocket suggests a novel mechanism for its role in susceptibility to spondyloarthropathies. Journal of Immunology. 1999;163:6665–6670
  87. Antoniou AN, Ford S, Taurog JD, et al. Formation of HLA-B27 homodimers and their relationship to assembly kinetics. The Journal of Biological Chemistry. 2004;279:8895–8902
  88. Tran TM, Satumtira N, Dorris ML, et al. HLA-B27 in transgenic rats forms disulfide-linked heavy chain oligomers and multimers that bind to the chaperone BiP. Journal of Immunology. 2004;172:5110–5119
  89. Colbert RA, Rowland-Jones SL, McMichael AJ, Frelinger JA. Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide. Proceedings of the National Academy of Sciences of the United States of America. 1993;90:6879–6883
  90. Colbert RA. The immunobiology of HLA-B27: variations on a theme. Current Molecular Medicine. 2004;4:21–30
  91. Whelan MA, Archer JR. Chemical reactivity of an HLA-B27 thiol group. European Journal of Immunology. 1993;23:3278–3285
  92. Schroder M, Kaufman RJ. The mammalian unfolded protein response. Annual Review of Biochemistry. 2005;74:739–789
  93. Harding HP, Calfon M, Urano F, et al. Transcriptional and translational control in the mammalian unfolded protein response. Annual Review of cell and Developmental Biology. 2002;18:575–599
  94. Turner MJ, Sowders DP, DeLay ML, et al. HLA-B27 misfolding in transgenic rats is associated with activation of the unfolded protein response. Journal of Immunology. 2005;175:2438–2448
  95. Deng J, Lu PD, Zhang Y, et al. Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Molecular and Cellular Biology. 2004;24:10161–10168
  96. Turner MJ, Sowders DP, DeLay ML, et al. HLA-B27 misfolding and induction by IFN-g activates the unfolded protein response which augments type I IFN production in macrophages from transgenic rats. Arthritis and Rheumatism. 2005;52:S691
  97. Smith JA, Turner MJ, Sowders DP, et al. The endoplasmic reticulum stress-induced unfolded protein response sensitizes macrophages to TLR-dependent IFN-b production. Arthritis and Rheumatism. 2005;52:S393
  98. Biron CA. Interferons alpha and beta as immune regulators—a new look. Immunity. 2001;14:661–664
  99. Theofilopoulos AN, Baccala R, Beutler B, Kono DH. Type I interferons (alpha/beta) in immunity and autoimmunity. Annual Review of Immunology. 2005;23:307–336
  100. Marrack P, Kappler J, Mitchell T. Type I interferons keep activated T-cells alive. The Journal of Experimental Medicine. 1999;189:521–530
  101. Le Bon A, Tough DF. Links between innate and adaptive immunity via type I interferon. Current Opinion in Immunology. 2002;14:432–436
  102. Takayanagi H, Kim S, Matsuo K, et al. RANKL maintains bone homeostasis through c-Fos-dependent induction of interferon-beta. Nature. 2002;416:744–749
  103. Deonarain R, Verma A, Porter AC, et al. Critical roles for IFN-beta in lymphoid development, myelopoiesis, and tumor development: links to tumor necrosis factor alpha. Proceedings of the National Academy of Sciences of the United States of America. 2003;100:13453–13458
  104. Tran TM, Dorris ML, Satumitra N, et al. Additional human beta-2m curbs HLA-B27 heavy chain misfolding and promotes arthritis and spondylitis but not colitis in male B27 transgenic rats. Arthritis and Rheumatism. 2005;52:S447
  105. Miyata T, Hori O, Zhang J, et al. The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyloidosis. The Journal of Clinical Investigation. 1996;98:1088–1094
  106. Schmidt AM, Yan SD, Yan SF, Stern DM. The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses. The Journal of Clinical Investigation. 2001;108:949–955
  107. Majors AK, Austin RC, de la Motte CA, et al. Endoplasmic reticulum stress induces hyaluronan deposition and leukocyte adhesion. The Journal of Biological Chemistry. 2003;278:47223–47231
  108. Ball EJ, Khan MA. HLA-B27 polymorphism. Joint, Bone, Spine. 2001;68:378–382
  109. D'Amato M, Fiorillo MT, Carcassi C, et al. Relevance of residue 116 of HLA-B27 in determining susceptibility to ankylosing spondylitis. European Journal of Immunology. 1995;25:3199–3201
  110. Feltkamp TE, Mardjuadi A, Huang F, Chou CT. Spondyloarthropathies in eastern Asia. Current Opinion in Rheumatology. 2001;13:285–290
  111. Olivieri I, Ciancio G, Padula A, et al. The HLA-B*2709 subtype confers susceptibility to spondyloarthropathy. Arthritis and Rheumatism. 2003;46:553–554
  112. Fiorillo MT, Meadows L, D'Amato M, et al. Susceptibility to ankylosing spondylitis correlates with the C-terminal residue of peptides presented by various HLA-B27 subtypes. European Journal of Immunology. 1997;27:368–373
  113. Sesma L, Montserrat V, Lamas J, et al. The peptide repertoires of HLA-B27 subtypes differentially associated to spondyloarthropathy (B*2704 and B*2706) differ by specific changes at three anchor positions. The Journal of Biological Chemistry. 2002;277:16744–16749
  114. Ramos M, Paradela A, Vazquez M, et al. Differential association of HLA-B*2705 and B*2709 to ankylosing spondylitis correlates with limited peptide subsets but not with altered cell surface stability. The Journal of Biological Chemistry. 2002;277:28749–28756
  115. Goodall JC, Ellis L, Hill Gaston JS. Spondylarthritis-associated and non-spondylarthritis-associated B27 subtypes differ in their dependence upon tapasin for surface expression and their incorporation into the peptide loading complex. Arthritis and Rheumatism. 2006;54:138–147
  116. Cauli A, Dessole G, Fiorillo MT, et al. Increased level of HLA-B27 expression in ankylosing spondylitis patients compared with healthy HLA-B27-positive subjects: a possible further susceptibility factor for the development of disease. Rheumatology (Oxford, England). 2002;41:1375–1379
  117. Cauli A, Dessole G, Cappai L, et al. The lack of association between HLA-B*2709 and ankylosing spondylitis is not due to a defective cellular expression of the B*2709 molecules. Arthritis and Rheumatism. 2005;52:S394
  118. Fiorillo MT, Cauli A, Carcassi C, et al. Two distinctive HLA haplotypes harbor the B27 alleles negatively or positively associated with ankylosing spondylitis in Sardinia: implications for pathogenesis. Arthritis and Rheumatism. 2003;48:1385–1389

PII: S1521-6942(06)00031-3

doi: 10.1016/j.berh.2006.03.001

Best Practice & Research Clinical Rheumatology
Volume 20, Issue 3 , Pages 571-591 , June 2006

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