Functional significance of Asn-linked glycosylation of proteinase 3 for enzymatic activity, processing, targeting, and recognition by anti-neutrophil cytoplasmic antibodies.

@article{Specks2007FunctionalSO,
  title={Functional significance of Asn-linked glycosylation of proteinase 3 for enzymatic activity, processing, targeting, and recognition by anti-neutrophil cytoplasmic antibodies.},
  author={Ulrich Specks and David Fass and Javier Daniel Finkielman and Amber M Hummel and Margaret A Viss and Robert D. Litwiller and Cari J. McDonald},
  journal={Journal of biochemistry},
  year={2007},
  volume={141 1},
  pages={101-12}
}
Proteinase 3 (PR3) is a neutral serine protease stored in neutrophil granules. It has substantial sequence homology with elastase, cathepsin G and azurocidin. PR3 is the target antigen for autoantibodies (ANCA) in Wegener's granulomatosis, a necrotizing vasculitis syndrome. ANCA have been implicated in the pathogenesis of this disease. PR3 has two potential Asn-linked glycosylation sites. This study was designed to determine the occupancy of these glycosylation sites, and to evaluate their… CONTINUE READING