Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells.

@article{McNutt2007CatalyticAI,
  title={Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells.},
  author={Markey C. McNutt and Thomas A. Lagace and Jay D. Horton},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 29},
  pages={20799-803}
}
Proprotein convertase subtilisin/kexin type 9 (PCSK9), a member of the proteinase K subfamily of subtilases, promotes internalization and degradation of low density lipoprotein receptors (LDLRs) after binding the receptor on the surface of hepatocytes. PCSK9 has autocatalytic activity that releases the prodomain at the N terminus of the protein. The prodomain remains tightly associated with the catalytic domain as the complex transits the secretory pathway. It is not known whether enzymatic… CONTINUE READING
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