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© The Rockefeller University Press, 0021-9525/1998//1095 $5.00
The Journal of Cell Biology, Volume 142, Number 4, , 1998 1095-1104


Articles

Functional Gap Junctions in the Schwann Cell Myelin Sheath



Rita J. Balice-Gordon*, Linda J. Bone{ddagger}, and Steven S. Scherer{ddagger}

* Department of Neuroscience and {ddagger} Department of Neurology, The University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6074

The Schwann cell myelin sheath is a multilamellar structure with distinct structural domains in which different proteins are localized. Intracellular dye injection and video microscopy were used to show that functional gap junctions are present within the myelin sheath that allow small molecules to diffuse between the adaxonal and perinuclear Schwann cell cytoplasm. Gap junctions are localized to periodic interruptions in the compact myelin called Schmidt–Lanterman incisures and to paranodes; these regions contain at least one gap junction protein, connexin32 (Cx32). The radial diffusion of low molecular weight dyes across the myelin sheath was not interrupted in myelinating Schwann cells from cx32-null mice, indicating that other connexins participate in forming gap junctions in these cells. Owing to the unique geometry of myelinating Schwann cells, a gap junction-mediated radial pathway may be essential for rapid diffusion between the adaxonal and perinuclear cytoplasm, since this radial pathway is approximately one million times faster than the circumferential pathway.

Key Words: myelin • gap junctions • glia • connexin • neuropathy • Schwann cell



Abbreviations used in this paper: AGA, 18-{alpha}-glycerrhetinic acid; CMTX, X-linked Charcot-Marie-Tooth disease; Cx32, connexin32; MAG, myelin-associated glycoprotein; PNS, peripheral nervous system; SIT, silicon-intensified target.

Address all correspondence to R.J. Balice-Gordon, Department of Neuroscience, University of Pennsylvania School of Medicine, 215 Stemmler Hall, Philadelphia, PA 19104-6074. Tel.: (215) 898-1037. Fax: (215) 573-9050. E-mail: rbaliceg{at}mail.med.upenn.edu

A portion of these results has appeared in abstract form (Bone, L.J., S.S. Scherer, and R.J. Balice-Gordon. 1996. The role of the gap junction protein connexin32 in myelinating Schwann cells. Soc. Neurosa Abstracts. 22:1981).



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