Protease production by cultured microglia: Substrate gel analysis and immobilized matrix degradation
Version of Record online: 11 OCT 2004
Copyright © 1993 Wiley-Liss, Inc.
Journal of Neuroscience Research
Volume 35, Issue 3, pages 297–304, 15 June 1993
How to Cite
Colton, C. A., Keri, J. E., Chen, W.-T. and Monsky, W. L. (1993), Protease production by cultured microglia: Substrate gel analysis and immobilized matrix degradation. J. Neurosci. Res., 35: 297–304. doi: 10.1002/jnr.490350309
- Issue online: 11 OCT 2004
- Version of Record online: 11 OCT 2004
- Manuscript Accepted: 31 DEC 1992
- Manuscript Revised: 22 DEC 1992
- Manuscript Received: 3 SEP 1992
- extracellular matrix
The production of collagen-degrading proteases by cultured neonatal rat microglia was examined using an immobilized fibronectin-gelatin matrix coupled to a fluorescent marker and by substrate gel analysis. When microglia were plated onto the surface of the matrix and incubated under resting (nonstimulated) conditions, a small but visible amount of immobilized matrix was degraded. Treatment with lipopolysaccharide (LPS) or interleukin-1 (IL-1) significantly increased the number of microglia demonstrating substrate degradation. Substrate-SDS polyacrylamide gel electrophoresis of samples of supernatants from untreated cultured microglia indicated the presence of a 72 and a 92 kD metalloproteinase with characteristics corresponding to collagenases. Supernatants from untreated astrocyte cultures were shown to have primarily a 72 kD metalloproteinase. Proteinase activity increased on stimulation of the microglia with LPS and IL-1 in a dose-dependent fashion. These results indicate that cultured microglia release active proteases capable of degrading the extracellular matrix in a localized region. The production of proteases by activated microglia may have important physiological and pathophysiological consequences within the restricted extracellular matrix of the CNS. © 1993 Wiley-Liss, Inc.