MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors

We report the discovery, cloning, and characterization of a novel human mat rix metalloproteinase (MMP-28) cDNA gene. The deduced 520-amino-acid sequen ce of MMP-28 includes a signal peptide, a prodomain with an unusual cystein e-switch PRCGVTD motif followed by the furin cleavage RRKKR site, a catalyt ic domain, a hinge-region and a hemopexin-like domain. On the basis of thei r structural characteristics, MMP-28 belongs to the MMP-19 subfamily. The g enomic MMP-28 gene uniquely mapped to chromosome 17q11.2 includes eight exo ns and seven introns. The broad range of expression in carcinomas as well a s normal adult and fetal tissues suggests an important functional role for MMP-28. (C) 2001 Elsevier Science B.V. All rights reserved.