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Publication : Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan.

First Author  Larsen PH Year  2003
Journal  J Neurosci Volume  23
Issue  35 Pages  11127-35
PubMed ID  14657171 Mgi Jnum  J:87968
Mgi Id  MGI:3028753 Doi  10.1523/JNEUROSCI.23-35-11127.2003
Citation  Larsen PH, et al. (2003) Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan. J Neurosci 23(35):11127-35
abstractText  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.
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