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The Journal of Neuroscience, July 6, 2005, 25(27):6401-6408; doi:10.1523/JNEUROSCI.1563-05.2005
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Neurobiology of Disease
A Highly Specific Inhibitor of Matrix Metalloproteinase-9 Rescues Laminin from Proteolysis and Neurons from Apoptosis in Transient Focal Cerebral Ischemia
Zezong Gu,1 Jiankun Cui,1 Stephen Brown,3 Rafael Fridman,4 Shahriar Mobashery,3 Alex Y. Strongin,2 andStuart A. Lipton1 1Center for Neuroscience and Aging, 2Cell Adhesion and Extracellular Matrix Biology Program, The Burnham Institute, La Jolla, California 92037, 3Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, and 4Department of Pathology, Wayne State University, Detroit, Michigan 48201
Neuronal cell death occurs during many neurodegenerative disorders and stroke. The aberrant, excessive activity of matrix metalloproteinases (MMPs), especially MMP-9, contributes directly to neuron apoptosis and brain damage (Rosenberg et al., 1996; Asahi et al., 2001; Gu et al., 2002; Horstmann et al., 2003). We determined that MMP-9 degrades the extracellular matrix protein laminin and that this degradation induces neuronal apoptosis in a transient focal cerebral ischemia model in mice. We also determined that the highly specific thiirane gelatinase inhibitor SB-3CT blocks MMP-9 activity, including MMP-9-mediated laminin cleavage, thus rescuing neurons from apoptosis. We conclude that MMP-9 is a highly promising drug target and that SB-3CT derivatives have significant therapeutic potential in stroke patients.
Key words: matrix metalloproteinases; thiirane inhibitor; laminin; proteolysis; neurons; apoptosis
Received Dec 19, 2004; accepted May 16, 2005.
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