Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains
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- Martin Vey
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
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- Susanne Pilkuhn
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
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- Holger Wille
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
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- Randal Nixon
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
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- Stephen J. DeArmond
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
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- Eric J. Smart
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
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- Richard G. W. Anderson
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
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- Albert Taraboulos
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
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- Stanley B. Prusiner
- Departments of Neurology, Pathology, and Biochemistry and Biophysics, University of California, San Francisco, CA 94143; Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75235; and The Hebrew University—Hadassah Medical School, 91120 Jerusalem, Israel
抄録
<jats:p> Results of transgenetic studies argue that the scrapie isoform of the prion protein (PrP <jats:sup>Sc</jats:sup> ) interacts with the substrate cellular PrP (PrP <jats:sup>C</jats:sup> ) during conversion into nascent PrP <jats:sup>Sc</jats:sup> . While PrP <jats:sup>Sc</jats:sup> appears to accumulate primarily in lysosomes, caveolae-like domains (CLDs) have been suggested to be the site where PrP <jats:sup>C</jats:sup> is converted into PrP <jats:sup>Sc</jats:sup> . We report herein that CLDs isolated from scrapie-infected neuroblastoma (ScN2a) cells contain PrP <jats:sup>C</jats:sup> and PrP <jats:sup>Sc</jats:sup> . After lysis of ScN2a cells in ice-cold Triton X-100, both PrP isoforms and an N-terminally truncated form of PrP <jats:sup>C</jats:sup> (PrP <jats:sup>C</jats:sup> -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- <jats:italic>N</jats:italic> -hydroxysuccinimide-biotin, both PrP <jats:sup>C</jats:sup> and PrP <jats:sup>Sc</jats:sup> were found biotinylated in CLD fractions. Similar results on the colocalization of PrP <jats:sup>C</jats:sup> and PrP <jats:sup>Sc</jats:sup> were obtained when CLDs were isolated from Syrian hamster brains. Our findings demonstrate that both PrP <jats:sup>C</jats:sup> and PrP <jats:sup>Sc</jats:sup> are present in CLDs and, thus, support the hypothesis that the PrP <jats:sup>Sc</jats:sup> formation occurs within this subcellular compartment. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 93 (25), 14945-14949, 1996-12-10
Proceedings of the National Academy of Sciences
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詳細情報 詳細情報について
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- CRID
- 1363388844711549568
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- NII論文ID
- 80009405597
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- ISSN
- 10916490
- 00278424
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