Intact, thioglycollate-stimulated murine macrophages cultured on an insoluble [3H]-elastin substratum progressively hydrolysed the elastin. Cell lysates had little activity. We compared the effect of various proteinase inhibitors on elastinolysis by either live cells or cell-free, elastase-rich conditioned medium. Only known inhibitors of macrophage elastase blocked the activity of elastase-rich cell-conditioned medium whereas inhibitors of cathepsin B also suppressed intact cell activity. Serum proteinase inhibitors blocked cell-derived soluble elastase activity but not intact cell elastolytic activity. We also observed that plasminogen added to the cell cultures markedly increased elastinolysis by live macrophages or cell-free elastase-rich medium. Purified plasmin alone had no measurable effect on native elastin. Additional experiments indicated that the plasmin enhancement was due to elastin-dependent activation of latent macrophage elastase. These results indicate that live macrophage elastinolysis is a co-operative process involving multiple proteinases, especially a cysteine proteinase(s) and elastase. Plasmin may be a physiological activator of latent macrophage elastase.
Research Article| September 15 1984
Co-operation between plasmin and elastase in elastin degradation by intact murine macrophages
Biochem J (1984) 222 (3): 721–728.
- Views Icon Views
- Share Icon Share
- Cite Icon Cite
H A Chapman, O L Stone; Co-operation between plasmin and elastase in elastin degradation by intact murine macrophages. Biochem J 15 September 1984; 222 (3): 721–728. doi: https://doi.org/10.1042/bj2220721
Download citation file: