Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2

作者：Sato H^*; Kinoshita T; Takino T; Nakayama K; Seiki M

来源：FEBS LETTERS, 1996, 393(1): 101-104.

DOI：10.1016/0014-5793(96)00861-7

• matrix metalloproteinase
• activation
• MT1-MMP

Membrane type 1-matrix metalloproteinase (MT1-MMP) initiates the activation of the zymogen progelatinase A/72-kDa type IV collagenase by cleavage of the Asn(66)-Leu peptide bond, We previously pointed out that MT1-MMP possesses a unique amino acid sequence Arg-Arg-Lys-Arg(111) 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 Arg(111)-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.