Isolation of latent 31-kDa C-truncated stromelysin and 21-kDa stromelysin from rabbit synovial fibroblasts: an alternative activation pathway for stromelysin.

@article{Kolkenbrock1994IsolationOL,
  title={Isolation of latent 31-kDa C-truncated stromelysin and 21-kDa stromelysin from rabbit synovial fibroblasts: an alternative activation pathway for stromelysin.},
  author={H. Kolkenbrock and A. Hecker-Kia and D. Orgel and H. Huser and W. Schröder and N. Ulbrich},
  journal={Biological chemistry Hoppe-Seyler},
  year={1994},
  volume={375 4},
  pages={
          241-7
        }
}
The processing of culture medium of rabbit synovial fibroblasts led to the isolation of three stromelysin-1 (MMP-3) cleavage products: A 31-kDa protein, which represents a C-truncated latent stromelysin-1, an active stromelysin-1 of 21 kDa, that originates from the 31-kDa proform by activation. A third protein had a molecular mass of 25 kDa representing the C-terminal part of prostromelysin-1 and is missing in the C-truncated latent stromelysin-1. The activation process of human prostromelysin… Expand
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Substance P Induces the Secretion of Gelatinase A from Human Synovial Fibroblasts
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