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Cleavage of myelin associated glycoprotein by matrix metalloproteinases

Elizabeth Milward1, Kee Jun Kim, Arek Szklarczyk

  • 1School of Biomedical Sciences, The University of Newcastle and the Hunter Medical Research Institute, Callaghan, New South Wales 2308, Australia.

Journal of Neuroimmunology
|December 8, 2007
PubMed

Insights

Matrix metalloproteinases (MMPs) can cleave myelin associated glycoprotein (MAG), generating fragments that inhibit nerve growth. This suggests MMPs disrupt axon-glia communication and create growth-inhibiting molecules in demyelinating diseases.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Myelin associated glycoprotein (MAG) is crucial for axon-glia interactions.
  • Proteolytic cleavage of MAG generates derivative MAG (dMAG), which can inhibit axonal growth.
  • Matrix metalloproteinases (MMPs) are implicated in inflammatory and demyelinating diseases.

Purpose of the Study:

  • To investigate the ability of specific MMPs to cleave MAG.
  • To determine if MMP-cleaved MAG fragments inhibit neuronal outgrowth.

Main Methods:

  • Recombinant human MAG was incubated with MMP-2, MMP-7, MMP-9, and MMP-1.
  • MAG expressed on CHO cells was treated with MMP-7.
  • Neurite outgrowth assays were performed using dorsal root ganglion (DRG) neurons and MAG fragments.

Main Results:

  • MMP-2, MMP-7, and MMP-9 cleaved recombinant human MAG, while MMP-1 did not.
  • MMP-7 cleaved MAG at Leu 509 and Met 234.
  • MMP-7 cleaved cell-surface MAG, releasing inhibitory fragments into the medium.

Conclusions:

  • MMPs can cleave MAG, potentially disrupting axon-glia communication.
  • MMP-generated MAG fragments inhibit neurite outgrowth.
  • MMPs may play a role in neuroinflammation and demyelination by modifying MAG.

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