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The Journal of Neuroscience, December 3, 2003, 23(35):11127-11135
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Cellular/Molecular
Matrix Metalloproteinase-9 Facilitates Remyelination in Part by Processing the Inhibitory NG2 Proteoglycan
Peter H. Larsen,1 Jennifer E. Wells,1 William B. Stallcup,2 Ghislain Opdenakker,3 andV. Wee Yong1 1Neuroscience Research Group and the Departments of Oncology and Clinical Neurosciences, University of Calgary, Calgary, Alberta, Canada T2N 4N1, 2The Burnham Institute, La Jolla, California 92037, and 3Rega Institute for Medical Research, University of Leuven, Leuven, Belgium B-3000
Remyelination is a critical repair process that is initiated after a demyelinating insult. The failure to remyelinate contributes to neurological diseases such as multiple sclerosis. Here, we test the hypothesis that proteinase activity is required for the extensive remodeling of the extracellular matrix that occurs during remyelination. We show that mice lacking matrix metalloproteinase (MMP)-9 are impaired in myelin reformation after lysolecithin-induced demyelination. This deficiency may be explained at least in part by the failure to clear the accumulation of NG2, an inhibitory proteoglycan that retards the maturation and differentiation of oligodendrocytes that are needed for remyelination. These results emphasize for the first time that upregulation of MMP activity can be important for facilitating regeneration from some types of CNS injury.
Key words: myelin formation; metalloproteinase; extracellular matrix; oligodendrocyte; differentiation; proteoglycan
Received July 14, 2003; revised August 22, 2003; accepted September 16, 2003.
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