Function of the Stroma-Derived Metalloproteinase, Stromelysin-3, in Invasive Breast Carcinomas.
Abstract
Stromelysin-3, a new member of the matrix metalloproteinase gene family, is specifically expressed in stromal cells surrounding invasive breast carcinoma cells, but its function has remained largely undefined. We now report that human stromelysin-3 is processed from an inactive zymogen to an active endoprotease following intracellular activation by the proprotem convertase, furin. Active stromelysin-3 is then secreted extracellularly where it is able to cleave and inactivate members of the serine proteinase inhibitor family. Given the fact that breast cancer cells have recently been shown to secrete powerful proteinase (e.g., leukocyte elastase, plasmin) whose activities are normally regulated by serine proteinase inhibitors, our data suggest that stromelysin-3 may regulate breast cancer cell function by controlling the local proteinase-antiproteinase balance.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 27, 1995
- Accession Number
- ADA299781
Entities
People
- Stephen J. Weiss
Organizations
- University of Michigan