Literature DB >> 8068508

Structure, function, and disease association of HLA-B27.

J A López de Castro1.   

Abstract

The specificity of antigen presentation by HLA-B27 and its modulation by subtype polymorphism can be understood from knowledge of the three-dimensional structure of this molecule and from biochemical analysis of bound peptides. These studies reveal the basis for the sharing of T cell determinants that might be critical to linkage of multiple subtypes to spondyloarthropathies. The mechanism of this association remains unknown, but involvement of T lymphocytes and HLA-B27 on antigen-presenting cells appears likely. Thus, a direct link between peptide presentation by HLA-B27 and its role in disease is emerging.

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Year:  1994        PMID: 8068508     DOI: 10.1097/00002281-199407000-00004

Source DB:  PubMed          Journal:  Curr Opin Rheumatol        ISSN: 1040-8711            Impact factor:   5.006


  4 in total

1.  HLA-B27 determination using serological methods. A comparison of enzyme immunoassay and a microlymphocytotoxic test with flow cytometry and a molecular biological assay.

Authors:  A Dunky; J Neumüller; C Hübner; G F Fischer; P M Bayer; E Wagner; D W Schwartz; W R Mayr
Journal:  Rheumatol Int       Date:  1996       Impact factor: 2.631

Review 2.  HLA-B27 and HLA-B73 polymorphism and its role on antigenicity, peptide presentation, and disease susceptibility.

Authors:  J A Lopez De Castro
Journal:  Clin Rheumatol       Date:  1996-01       Impact factor: 2.980

Review 3.  B27 polymorphism and peptide repertoire.

Authors:  P Parham
Journal:  Clin Rheumatol       Date:  1996-01       Impact factor: 2.980

4.  Spontaneous inflammatory arthritis in HLA-B27 transgenic mice lacking beta 2-microglobulin: a model of human spondyloarthropathies.

Authors:  S D Khare; H S Luthra; C S David
Journal:  J Exp Med       Date:  1995-10-01       Impact factor: 14.307

  4 in total

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