Evidence for furin-type activity-mediated C-terminal processing of profibrillin-1 and interference in the processing by certain mutations.

@article{Lnnqvist1998EvidenceFF,
  title={Evidence for furin-type activity-mediated C-terminal processing of profibrillin-1 and interference in the processing by certain mutations.},
  author={L. L{\"o}nnqvist and D. Reinhardt and L. Sakai and L. Peltonen},
  journal={Human molecular genetics},
  year={1998},
  volume={7 13},
  pages={
          2039-44
        }
}
Fibrillin-1 is a major component of the 10 nm microfibrils of the extracellular matrix (ECM). It is synthesized as an approximately 350 kDa precursor molecule, profibrillin-1, which is proteolytically processed into its biologically active approximately 320 kDa form. Furin, a calcium-dependent endoprotease of the subtilisin family, which is known to be the processing enzyme for a variety of proproteins, is believed to be responsible for the N-terminal proteolytic cleavage of profibrillin-1. In… Expand
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