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The Journal of Neuroscience, March 1, 2006, 26(9):2458-2466; doi:10.1523/JNEUROSCI.4054-05.2006

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Cellular/Molecular
Glutamate Stimulates Oligodendrocyte Progenitor Migration Mediated via an _v Integrin/Myelin Proteolipid Protein Complex

Tatyana I. Gudz, Hitoshi Komuro, and Wendy B. Macklin

Department of Neurosciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195

Correspondence should be addressed to Dr. Wendy B. Macklin, Department of Neurosciences, NC30, Cleveland Clinic Foundation, Euclid Avenue, Cleveland, OH 44195. Email: mackliw{at}ccf.org

In the mammalian CNS, oligodendrocyte precursor cells (OPCs) express most neurotransmitter receptors, but their function remains unclear. The current studies suggest a physiological role for glutamate (AMPA and/or kainate) receptors in OPC migration. AMPA stimulated _v integrin-mediated OPC migration by increasing both the rate of cell movement and the frequency of Ca²⁺ transients. A protein complex containing the myelin proteolipid protein (PLP) and _v integrin modulated the AMPA-stimulated migration, and stimulation of OPC AMPA receptors resulted in increased association of the AMPA receptor subunits themselves with the _v integrin/PLP complex. Thus, after AMPA receptor stimulation, an _v integrin/PLP/neurotransmitter receptor protein complex forms that reduces binding to the extracellular matrix and enhances OPC migration. To assess the extent to which PLP was involved in the AMPA-stimulated migration, OPCs from the myelin-deficient (MD) rat, which has a PLP gene mutation, were analyzed. OPCs from the MD rat had a normal basal migration rate, but AMPA did not stimulate the migration of these cells, suggesting that the PLP/_v integrin complex was important for the AMPA-mediated induction. AMPA-induced modulation of OPC migration was abolished by pertussis toxin, although baseline migration was normal. Thus, G-protein-dependent signaling is crucial for AMPA-stimulated migration of OPCs but not for basal OPC migration. Other signaling pathways involved in this AMPA-stimulated OPC migration were also determined. These studies highlight novel signaling determinants of OPC migration and suggest that glutamate could play a pivotal role in regulating integrin-mediated OPC migration.

Key words: proteolipid protein; AMPA receptor; neurotransmitter receptor; Ca²⁺ transient; G_i-protein; GluR2; GluR4

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Received Sept. 23, 2005; revised Dec. 14, 2005; accepted Jan. 12, 2006.

Correspondence should be addressed to Dr. Wendy B. Macklin, Department of Neurosciences, NC30, Cleveland Clinic Foundation, Euclid Avenue, Cleveland, OH 44195. Email: mackliw{at}ccf.org

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