[HTML][HTML] Cellular mechanisms for human procollagenase-3 (MMP-13) activation: evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate …
V Knäuper, H Will, C López-Otin, B Smith… - Journal of Biological …, 1996 - ASBMB
Gelatinase A and membrane-type metalloproteinase (MT1-MMP) were able to process
human procollagenase-3 (M r 60,000) to the fully active enzyme (Tyr 85 N terminus; M r
48,000). MT1-MMP activated procollagenase-3 via a M r 56,000 intermediate (Ile 36 N
terminus) to 48,000 which was the result of the cleavage of the Glu 84-Tyr 85 peptide bond.
We have established that the activation rate of procollagenase-3 by MT1-MMP was
enhanced in the presence of progelatinase A, thereby demonstrating a unique new …
human procollagenase-3 (M r 60,000) to the fully active enzyme (Tyr 85 N terminus; M r
48,000). MT1-MMP activated procollagenase-3 via a M r 56,000 intermediate (Ile 36 N
terminus) to 48,000 which was the result of the cleavage of the Glu 84-Tyr 85 peptide bond.
We have established that the activation rate of procollagenase-3 by MT1-MMP was
enhanced in the presence of progelatinase A, thereby demonstrating a unique new …