Protease production by cultured microglia: substrate gel analysis and immobilized matrix degradation.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Colton, CA; Keri, JE; Chen, WT; Monsky, WL

Published Date

  • June 15, 1993

Published In

Volume / Issue

  • 35 / 3

Start / End Page

  • 297 - 304

PubMed ID

  • 8350390

International Standard Serial Number (ISSN)

  • 0360-4012

Digital Object Identifier (DOI)

  • 10.1002/jnr.490350309


  • eng

Conference Location

  • United States