| Literature DB >> 24898250 |
Jie J Zhou1, Feng Wang1, Zhiwen Xu1, Wing-Sze Lo1, Ching-Fun Lau1, Kyle P Chiang2, Leslie A Nangle2, Melissa A Ashlock2, John D Mendlein2, Xiang-Lei Yang3, Mingjie Zhang4, Paul Schimmel5.
Abstract
Inflammatory and debilitating myositis and interstitial lung disease are commonly associated with autoantibodies (anti-Jo-1 antibodies) to cytoplasmic histidyl-tRNA synthetase (HisRS). Anti-Jo-1 antibodies from different disease-afflicted patients react mostly with spatially separated epitopes in the three-dimensional structure of human HisRS. We noted that two HisRS splice variants (SVs) include these spatially separated regions, but each SV lacks the HisRS catalytic domain. Despite the large deletions, the two SVs cross-react with a substantial population of anti-Jo-l antibodies from myositis patients. Moreover, expression of at least one of the SVs is up-regulated in dermatomyositis patients, and cell-based experiments show that both SVs and HisRS can be secreted. We suggest that, in patients with inflammatory myositis, anti-Jo-1 antibodies may have extracellular activity.Entities:
Keywords: Aminoacyl-tRNA Synthetase; Anti-Jo-1 Autoantibody; Autoimmune Disease; Dermatomyositis; Epitope Mapping; Immunology; Myositis; Secretion
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Year: 2014 PMID: 24898250 PMCID: PMC4094037 DOI: 10.1074/jbc.C114.571026
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157