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A cDNA coding for a new zinc/metalloprotease was isolated from the cytoplasmic poly(A) RNA of human rheumatoid arthritis synovial fibroblasts. The full length cDNA contains a poly(A) tail at its 3′ end and encodes a polypeptide of 576 amino acid residues, possessing a short N-terminal sequence of Met-Ala-Lys, a long C-terminal metal-binding region of the ‘HEXXH-E’ type, and a hydrophobic sequence of 26 amino acid residues. The new zinc-dependent endopeptidase activity was named PNP (proline specific, new protease) and has an apparent molecular mass of 60,000 Da. The PNP was present in all the tissues examined and was increased in cytosolic fractions of fibroblast-like synoviocytes, derived from the rheumatoid arthritis joint. The specific activity of this enzyme, released from the cells by 1% Triton X-100 treatment, was 14 pmol/min/mg protein, which was approximately one tenth that of the normal fibroblast