The Oxidative Folding and Misfolding of Human Leukocyte Antigen-B27

Antoniou, A.N., Guiliano, D.B., Lenart, I., Burn, G. and Powis, S.J. 2011. The Oxidative Folding and Misfolding of Human Leukocyte Antigen-B27. Antioxidants and Redox Signaling. 15 (2), pp. 669-684. https://doi.org/10.1089/ars.2010.3692

TitleThe Oxidative Folding and Misfolding of Human Leukocyte Antigen-B27
TypeJournal article
AuthorsAntoniou, A.N., Guiliano, D.B., Lenart, I., Burn, G. and Powis, S.J.
Abstract

The major histocompatibility complex class I molecule human leukocyte antigen (HLA)-B27 is strongly associated with a group of inflammatory arthritic disorders known as the spondyloarthropathies. Many autoimmune diseases exhibit associations with major histocompatibility complex molecules encoded within the class II locus with defined immune responses either mediated by T or B-lymphocytes. Despite the association being known for over 30 years, no defined immune response and target autoantigens have been characterized for the spondyloarthropathies. Thus, the mechanism and role of HLA-B27 in disease pathogenesis remains undetermined. One hypothesis that has recently received much attention has focused around the enhanced propensity for HLA-B27 to misfold and the increased tendency of the heavy chain to dimerize. The misfolding of HLA-B27 has been associated with its redox status and this is postulated to be involved in disease development. Here we discuss the impact of the redox status on HLA-B27 biosynthesis and function

JournalAntioxidants and Redox Signaling
Journal citation15 (2), pp. 669-684
ISSN1523-0864
1557-7716
Year2011
PublisherMary Ann Liebert
Digital Object Identifier (DOI)https://doi.org/10.1089/ars.2010.3692
Web address (URL)http://dx.doi.org/10.1089/ars.2010.3692
Publication dates
PublishedAug 2011

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