We have isolated and characterized the complete primary structure of a new member of the tissue inhibitor of metalloproteinase family (TIMP family) which we refer to as TIMP-2. TIMP-2 binds specifically to the latent form of the 72 kDa type IV collagenase. Inhibition of the activated enzyme occurs with 1:1 molar stoichiometry. TIMP-2 contains 12 cysteine residues, the positions of which are highly conserved when compared with the primary structure of TIMP-1. We have obtained a 1.0 kB cDNA clone which encodes for the pro-TIMP-2. This clone encodes for a 194 amino acid mature TIMP-2 molecule and a 26 amino acid signal peptide. Recent studies have focused on the production of recombinant TIMP-2 and transcriptional regulation of the TIMP-2 transcript levels.
