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Vol. 10, Issue 10, 3187-3196, October 1999
¶
*Department of Neurology, University of Tübingen, D-77076
Tübingen, Germany; §Department of Medical Chemistry
and Biochemistry, University of Milan, 20133 Milan, Italy;
¶Max Planck Institute for Molecular Cell Biology and
Genetics, Dresden, Germany; and Exogenous application of gangliosides to cells affects many
cellular functions. We asked whether these effects could be attributed to the influence of gangliosides on the properties of
sphingolipid-cholesterol microdomains on the plasma membrane, also
termed rafts. The latter are envisaged as lateral assemblies of
sphingolipids (including gangliosides), cholesterol, and a specific set
of proteins. Rafts have been implicated in processes such as membrane
trafficking, signal transduction, and cell adhesion. Recently, using a
chemical cross-linking approach with Madin-Darby canine kidney (MDCK)
cells permanently expressing a GPI-anchored form of growth
hormone decay accelerating factor (GH-DAF) as a model system, we could
show that GPI-anchored proteins are clustered in rafts in living cells. Moreover, this clustering was dependent on the level of cholesterol in
the cell. Here we show that incubation of MDCK cells with gangliosides abolished subsequent chemical cross-linking of GH-DAF. Furthermore, insertion of gangliosides into the plasma membrane of MDCK GH-DAF cells
renders GH-DAF soluble when subjected to extraction with Triton X-114
at 4°C. Our data suggest that exogenous application of gangliosides
displaces GPI-anchored proteins from sphingolipid-cholesterol microdomains in living cells.
Department of Cell
Biology, Max-Delbrück Centre for Molecular Medicine, D-13092
Berlin-Buch, Germany
These authors contributed equally to this work.
Corresponding author. E-mail address:
kurzchal{at}orion.rz.mdc-berlin.de.
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