HLA-B27 up-regulation causes accumulation of misfolded heavy chains and correlates with the magnitude of the unfolded protein response in transgenic rats: Implications for the pathogenesis of spondylarthritis-like disease.

@article{Turner2007HLAB27UC,
  title={HLA-B27 up-regulation causes accumulation of misfolded heavy chains and correlates with the magnitude of the unfolded protein response in transgenic rats: Implications for the pathogenesis of spondylarthritis-like disease.},
  author={Matthew J Turner and Monica L Delay and Shuzhen Bai and Erin I Klenk and Robert A. Colbert},
  journal={Arthritis and rheumatism},
  year={2007},
  volume={56 1},
  pages={215-23}
}
OBJECTIVE HLA-B27 is implicated in the pathogenesis of spondylarthritis (SpA), yet the molecular mechanisms are incompletely defined. HLA-B27 misfolding has been associated with endoplasmic reticulum stress and activation of the unfolded protein response (UPR) in macrophages from HLA-B27/human beta(2)-microglobulin-transgenic (B27-transgenic) rats. This study was performed to assess the mechanisms that drive activation of the HLA-B27-induced UPR and to determine whether splenocytes respond in a… CONTINUE READING

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