Characterization of proADAMTS5 processing by proprotein convertases.

@article{Longpr2009CharacterizationOP,
  title={Characterization of proADAMTS5 processing by proprotein convertases.},
  author={Jean-Michel Longpr{\'e} and Daniel R. McCulloch and B Koo and Jonathan P Alexander and Suneel S. Apte and Richard Leduc},
  journal={The international journal of biochemistry & cell biology},
  year={2009},
  volume={41 5},
  pages={1116-26}
}
ADAMTS5 (aggrecanase-2), a key metalloprotease mediating cartilage destruction in arthritis, is synthesized as a zymogen, proADAMTS5. We report a detailed characterization of the propeptide excision mechanism and demonstrate that it is a major regulatory step with unusual characteristics. Using furin-deficient cells and a furin inhibitor, we found that proADAMTS5 was processed by proprotein convertases, specifically furin and PC7, but not PC6B. Mutagenesis of three sites containing basic… CONTINUE READING

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