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Vol. 9, Issue 3, 599-609, March 1998
Department of Physiological Chemistry, Faculty of Medical Sciences,
University of Groningen, the Netherlands
Myelin sheets originate from distinct areas at the oligodendrocyte
(OLG) plasma membrane and, as opposed to the latter, myelin membranes
are relatively enriched in glycosphingolipids and cholesterol. The OLG
plasma membrane can therefore be considered to consist of different
membrane domains, as in polarized cells; the myelin sheet is
reminiscent of an apical membrane domain and the OLG plasma membrane
resembles the basolateral membrane. To reveal the potentially polarized
membrane nature of OLG, the trafficking and sorting of two typical
markers for apical and basolateral membranes, the viral proteins
influenza virus-hemagglutinin (HA) and vesicular stomatitis virus-G
protein (VSVG), respectively, were examined. We demonstrate that in
OLG, HA and VSVG are differently sorted, which presumably occurs upon
their trafficking through the Golgi. HA can be recovered in a Triton
X-100-insoluble fraction, indicating an apical raft type of
trafficking, whereas VSVG was only present in a Triton X-100-soluble
fraction, consistent with its basolateral sorting. Hence, both an
apical and a basolateral sorting mechanism appear to operate in OLG.
Surprisingly, however, VSVG was found within the myelin sheets
surrounding the cells, whereas HA was excluded from this domain.
Therefore, despite its raft-like transport, HA does not reach a
membrane that shows features typical of an apical membrane. This
finding indicates either the uniqueness of the myelin membrane or the
requirement of additional regulatory factors, absent in OLG, for apical
delivery. These remarkable results emphasize that polarity and
regulation of membrane transport in cultured OLG display features that
are quite different from those in polarized cells.
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