Activation of a recombinant membrane type 1‐matrix metalloproteinase (MT1‐MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)‐2
- 9 September 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 393 (1), 101-104
- https://doi.org/10.1016/0014-5793(96)00861-7
Abstract
Membrane type 1-matrix metalloproteinase (MT1-MMP) initiates the activation of the zymogen progelatinase A/72-kDa type IV collagenase by cleavage of the Asn66-Leu peptide bond. We previously pointed out that MT1-MMP possesses a unique amino acid sequence Arg-Arg-Lys-Arg111 which is a potential recognition sequence for furin-like proteases (Nature, 370 (1994) 61–65). Here, using a recombinant MT1-MMP expressed in Escherichia coli we demonstrated that furin specifically cleaves MT1-MMP between Arg111-Tyr in vitro, which resulted in a stimulation of progelatinase A-activation function. Tissue inhibitor of metalloproteinases (TIMP)-2 inhibited activation of progelatinase A by forming a stable complex with activated MT1-MMP.Keywords
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