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Volume 17, Number 20, Issue of October 15, 1997 pp. 7754-7762
Copyright ©1997 Society for Neuroscience

Neurons Promote the Translocation of Peripheral Myelin Protein 22 into Myelin

Received March 9, 1997; revised June 24, 1997; accepted Aug. 7, 1997.

Sangeeta Pareek¹, Lucia Notterpek², G. Jackson Snipes¹, Roland Naef³, Wayne Sossin¹, Jacynthe Laliberté¹, Sandra Iacampo¹, Ueli Suter³, Eric M. Shooter², and Richard A. Murphy¹

¹ Montreal Neurological Institute and the Faculty of Medicine, McGill University, Montreal, Quebec H3A 2B4, Canada, ² Department of Neurobiology, Stanford University School of Medicine, Stanford, California 94305, and ³ Institute of Cell Biology, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland

Schwann cells express low levels of myelin proteins in the absence of neurons. When Schwann cells and neurons are cultured together the production of myelin proteins is elevated, and myelin is formed. For peripheral myelin protein 22 (PMP22), the exact amount of protein produced is critical, because peripheral neuropathies result from its underexpression or overexpression. In this study we examined the effect of neurons on Schwann cell PMP22 production in culture and in peripheral nerve using metabolic labeling and pulse-chase studies as well as immunocytochemistry. Most of the newly synthesized PMP22 in Schwann cells is rapidly degraded in the endoplasmic reticulum. Only a small proportion of the total PMP22 acquires complex glycosylation and accumulates in the Golgi compartment. This material is translocated to the Schwann cell membrane in detectable amounts only when axonal contact and myelination occur. Myelination does not, however, alter the rapid turnover of PMP22 in Schwann cells. PMP22 may therefore be a unique myelin protein in that axonal contact promotes its insertion into the Schwann cell membrane and myelin without altering its rapid turnover rate within the cell.

Key words: Schwann cells; PMP22; glycosylation; turnover; Golgi; axonal contact

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