Journal
GENE
Volume 265, Issue 1-2, Pages 87-93Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0378-1119(01)00360-2
Keywords
extracellular matrix; chromosome 17; carcinoma; lung
Categories
Funding
- NCI NIH HHS [CA83017, CA77470] Funding Source: Medline
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We report the discovery, cloning, and characterization of a novel human matrix metalloproteinase (MMP-28) cDNA gene. The deduced 520-amino-acid sequence of MMP-28 includes a signal peptide, a prodomain with an unusual cysteine-switch PRCGVTD motif followed by the furin cleavage RRKKR site, a catalytic domain, a hinge-region and a hemopexin-like domain. On the basis of their structural characteristics, MMP-28 belongs to the MMP-19 subfamily. The genomic MMP-28 gene uniquely mapped to chromosome 17q11.2 includes eight exons and seven introns. The broad range of expression in carcinomas as well as normal adult and fetal tissues suggests an important functional role for MMP-28. (C) 2001 Elsevier Science B.V. All rights reserved.
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