Differential RIP antigen (CNPase) expression in peripheral ensheathing glia.
The RIP monoclonal antibody is commonly used to identify oligodendrocytes. Recently, the RIP antigen was identified as 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase), a known non-compact myelin protein [Watanabe, M., Sakurai, Y., Ichinose, T., Aikawa, Y., Kotani, M., Itoh, K., 2006. Monoclonal antibody Rip specifically recognizes 2',3'-cyclic nucleotide 3'-phosphodiesterase in oligodendrocytes. J. Neurosci. Res. 84, 525-533]. In the present study we characterize normal and axotomy-induced changes in RIP immunoreactivity in peripheral glia. In myelinating Schwann cells, RIP demarcated paranodal regions of myelinated axons and clearly defined Schmidt-Lantermann incisures. Surprisingly, RIP immunoreactivity was not confined to myelinating glia. Robust RIP immunoreactivity was present in Remak bundles in mixed nerves and in sympathetic ganglia and grey rami. Following peripheral nerve injury, RIP immunoreactivity was redistributed diffusely throughout de-differentiating Schwann cell cytoplasm. In uninjured rats, low levels of RIP immunoreactivity were detectable in satellite cells surrounding dorsal root ganglion (DRG) neurons and in terminal Schwann cells at neuromuscular junctions. This pattern suggested a correlation between RIP immunoreactivity and the amount of axon-glial contact. We therefore injured the L5 spinal nerve to induce sympathetic sprouting and pericellular basket formation in the DRG, and asked whether relatively RIP-negative satellite glia, which normally contact only neuronal somata, would upregulate the RIP antigen upon contact with sprouting sympathetic axons. All perineuronal sympathetic sprouts infiltrated heavily RIP-immunoreactive satellite cell sheaths. RIP immunoreactivity was absent from placode-derived olfactory ensheathing glia, indicating that the relationship between axon-glial contact and RIP-immunoreactivity is restricted to peripheral ensheathing glia of the neural crest-derived Schwann cell lineage.
Toma
Jeremy S
JS
International Collaboration on Repair Discoveries, The University of British Columbia, Rm. 2465, 6270 University Boulevard, Vancouver, BC, Canada V6T 1Z4.
McPhail
Lowell T
LT
Ramer
Matt S
MS
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism; D019771:Axotomy / Q000379:methods; D005727:Ganglia, Spinal / Q000378:metabolism; D005786:Gene Expression Regulation / Q000502:physiology*; D007150:Immunohistochemistry / Q000379:methods; D008297:Male; D009457:Neuroglia / Q000201:enzymology*; D009830:Olfactory Bulb / Q000166:cytology; D009836:Oligodendroglia / Q000276:immunology*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012583:Schwann Cells / Q000201:enzymology; D012584:Sciatic Nerve / Q000166:cytology*; D020426:Sciatic Neuropathy / Q000378:metabolism / Q000473:pathology; D013997:Time Factors; D043222:Ubiquitin Thiolesterase / Q000378:metabolism
D000911:Antibodies, Monoclonal; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases; C489034:UCHL1 protein, rat; D043222:Ubiquitin Thiolesterase