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Use of gel zymography to examine matrix metalloproteinase (gelatinase) expression in brain tissue or in primary glial cultures.

Authors
 Harald Frankowski  ;  Yu-Huan Gu  ;  Ji Hoe Heo  ;  Richard Milner  ;  Gregory J. del Zoppo 
Citation
 Methods in Molecular Biology (Clifton, N.J.), Vol.814 : 221-233, 2012 
Journal Title
 Methods in Molecular Biology (Clifton, N.J.) 
ISSN
 1064-3745 
Issue Date
2012
Abstract
Glia synthesize, package, and secrete several species of matrix proteases, including the gelatinases (pro-)MMP-2 and (pro-)MMP-9. In appropriate settings (e.g., experimental ischemia), these MMPs can be assayed from cerebral tissues or from astrocytes and microglia in culture by enzymatic substrate-dependent assays and by gelatin-based zymography. We describe the methodologies for the sensitive quantitative development of the inactive and active forms of both MMP-2 and MMP-9 from tissues and cells, by means of lysis of the collagen substrate in collagen-impregnated gel electropheresis by the zymogen and active gelatinases. These methodologies are a refinement of those used commonly, with instructions to increase sensitivity. Serious and often overlooked issues regarding sources of sample contamination and elements confounding the MMP band development and their interpretation are discussed.
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/91456
DOI
10.1007/978-1-61779-452-0_15
Appears in Collections:
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Neurology (신경과학교실)
Yonsei Authors
허지회(Heo, Ji Hoe)
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