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Background

Matrix metalloproteinase-28 (MMP-28) is a poorly understood member of the matrix metalloproteinase family. Metalloproteinases are important mediators in the development of the nervous system and can contribute to the maturation of the neural micro-environment.

Results

MMP-28 added to myelinating rat dorsal root ganglion (DRG) co-cultures reduces myelination and two antibodies targeted to MMP-28 (pAb180 and pAb183) are capable of binding MMP-28 and inhibiting its activity in a dose-dependent manner. Addition of 30 nM pAb180 or pAb183 to rat DRG cultures resulted in the 2.6 and 4.8 fold enhancement of myelination respectively while addition of MMP-28 to DRG co-cultures resulted in enhanced MAPK, ErbB2 and ErbB3 phosphorylation. MMP-28 protein expression was increased within demyelinated lesions of mouse experimental autoimmune encephalitis (EAE) and human multiple sclerosis lesions compared to surrounding normal tissue.

Conclusion

MMP-28 is upregulated in conditions of demyelination in vivo, induces signaling in vitro consistent with myelination inhibition and, neutralization of MMP-28 activity can enhance myelination in vitro. These results suggest inhibition of MMP-28 may be beneficial under conditions of dysmyelination."xsd:string
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http://purl.uniprot.org/citations/18778487http://purl.uniprot.org/core/author"Dotzlaf J.E."xsd:string
http://purl.uniprot.org/citations/18778487http://purl.uniprot.org/core/author"Smith R.C."xsd:string
http://purl.uniprot.org/citations/18778487http://purl.uniprot.org/core/author"Werner S.R."xsd:string
http://purl.uniprot.org/citations/18778487http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18778487http://purl.uniprot.org/core/name"BMC Neurosci"xsd:string
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http://purl.uniprot.org/citations/18778487http://purl.uniprot.org/core/title"MMP-28 as a regulator of myelination."xsd:string
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