NDLI: Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains

Content Provider	PubMed Central
Author	Vey, Martin Pilkuhn, Susanne Wille, Holger Nixon, Randal Dearmond, Stephen j. Smart, Eric j. Anderson, Richard g. w. Albert, Taraboulos Prusiner, Stanley b.
Copyright Year	1996
Abstract	Results of transgenetic studies argue that the scrapie isoform of the prion protein (PrPSc) interacts with the substrate cellular PrP (PrPC) during conversion into nascent PrPSc. While PrPSc appears to accumulate primarily in lysosomes, caveolae-like domains (CLDs) have been suggested to be the site where PrPC is converted into PrPSc. We report herein that CLDs isolated from scrapie-infected neuroblastoma (ScN2a) cells contain PrPC and PrPSc. After lysis of ScN2a cells in ice-cold Triton X-100, both PrP isoforms and an N-terminally truncated form of PrPC (PrPC-II) were found concentrated in detergent-insoluble complexes resembling CLDs that were isolated by flotation in sucrose gradients. Similar results were obtained when CLDs were purified from plasma membranes by sonication and gradient centrifugation; with this procedure no detergents are used, which minimizes artifacts that might arise from redistribution of proteins among subcellular fractions. The caveolar markers ganglioside GM1 and H-ras were found concentrated in the CLD fractions. When plasma membrane proteins were labeled with the impermeant reagent sulfo-N-hydroxysuccinimide-biotin, both PrPC and PrPSc were found biotinylated in CLD fractions. Similar results on the colocalization of PrPC and PrPSc were obtained when CLDs were isolated from Syrian hamster brains. Our findings demonstrate that both PrPC and PrPSc are present in CLDs and, thus, support the hypothesis that the PrPSc formation occurs within this subcellular compartment.
Starting Page	14945
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	25
Volume Number	93
Language	English
Publisher	The National Academy of Sciences of the USA
Publisher Date	1996-12-10
Access Restriction	Open
Rights Holder	The National Academy of Sciences of the USA
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains.

Separation and properties of cellular and scrapie prion proteins.

COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform

Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice.

Separation and properties of cellular and scrapie prion proteins.

Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice.

Three scrapie prion isolates exhibit different accumulation patterns of the prion protein scrapie isoform.

Purified prion proteins and scrapie infectivity copartition into liposomes.

Recombinant scrapie-like prion protein of 106 amino acids is soluble

Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains

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Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains.

Separation and properties of cellular and scrapie prion proteins.

COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform

Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice.

Separation and properties of cellular and scrapie prion proteins.

Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice.

Three scrapie prion isolates exhibit different accumulation patterns of the prion protein scrapie isoform.

Purified prion proteins and scrapie infectivity copartition into liposomes.

Recombinant scrapie-like prion protein of 106 amino acids is soluble

Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains