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Inhibition of complex glycosylation increases the formation of PrPsc

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78892

Winklhofer,  K. F.
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78089

Heller,  U.
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78558

Reintjes,  A.
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78784

Tatzelt,  J.
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Winklhofer, K. F., Heller, U., Reintjes, A., & Tatzelt, J. (2003). Inhibition of complex glycosylation increases the formation of PrPsc. Traffic, 4(5), 313-322.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6C05-5
Zusammenfassung
N-linked glycans with complex structure have a major role in the biological activity of a wide variety of cell surface and secreted glycoproteins. Here, we show that geldanamycin, an inhibitor of Hsp90, interferes with the formation of complex glycosylated mammalian prion protein (PrPC ). Similarly to inhibitors of alpha-mannosidases, geldanamycin stabilized a high mannose PrPC glycoform and prevented the subsequent processing into complex structures. Moreover, a PrP/Grp94 complex could be isolated from geldanamycin-treated cells, suggesting that Grp94 might play a role in the processing of PrPC in the endoplasmic reticulum. Inhibition of complex glycosylation did not interfere with the glycosylphosphatidylinositol (GPI) anchor attachment and cellular trafficking of high mannose PrPC to the outer leaflet of the plasma membrane. In scrapie-infected neuroblastoma cells, however, high mannose PrPC glycoforms were preferred substrates for the formation of PrP-scrapie (PrPSc ). Our study reveals that complex glycosylation is dispensable for the cellular trafficking of PrPC , but modulates the formation of PrPSc .