Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement.

Although MMP-28 is involved in numerous important physiologic and pathologic conditions, the mechanisms of action of this secreted proteinase is not well understood. We now have demonstrated that furin serves as an intermolecular chaperone for MMP-28 secretion by interacting with the propeptide domain of MMP-28. Employing COS-1 cells transfected with MMP-28 cDNA, protein levels of MMP-28 were quite low in conditioned media as compared to cell lysates.