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Protease production by cultured microglia: Substrate gel analysis and immobilized matrix degradation
Author(s) -
Colton C. A.,
Keri J. E.,
Chen W.T.,
Monsky W. L.
Publication year - 1993
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490350309
Subject(s) - protease , microglia , degradation (telecommunications) , substrate (aquarium) , chemistry , matrix (chemical analysis) , matrix metalloproteinase , biochemistry , chromatography , medicine , biology , enzyme , immunology , computer science , inflammation , ecology , telecommunications
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.

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