The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains
Open accessAbstract
Results of transgenetic studies argue that the scrapie isoform of the prion protein (PrP Sc ) interacts with the substrate cellular PrP (PrP C ) during conversion into nascent PrP Sc . While PrP Sc appears to accumulate primarily in lysosomes, caveolae-like domains (CLDs) have been suggested to be the site where PrP C is converted into PrP Sc . We report herein that CLDs isolated from scrapie-infected neuroblastoma (ScN2a) cells contain PrP C and PrP Sc . After lysis of ScN2a cells in ice-cold Triton X-100, both PrP isoforms and an N-terminally truncated form of PrP C (PrP C -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 PrP C and PrP Sc were found biotinylated in CLD fractions. Similar results on the colocalization of PrP C and PrP Sc were obtained when CLDs were isolated from Syrian hamster brains. Our findings demonstrate that both PrP C and PrP Sc are present in CLDs and, thus, support the hypothesis that the PrP Sc formation occurs within this subcellular compartment.
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Citations
Cites
Hooper, N. M., Hryszko, J., & Turner, A. J. (1990) · Biochemical Journal · doi:10.1042/bj2670509 · Cited by 91
Cited by
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Self-citationRole of Caveolae and Caveolins in Health and Disease
Cohen, A. W., Hnasko, R., Schubert, W., & Lisanti, M. P. (2004) · Physiological Reviews · doi:10.1152/physrev.00046.2003 · Cited by 893
Physiology of the prion protein
Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617
Moore, R. C., Lee, I. Y., Silverman, G. L., Harrison, P. M., Strome, R., Heinrich, C., Karunaratne, A., Pasternak, S. H., Chishti, M. A., Liang, Y., et al. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3108 · Cited by 530
Self-citationMolecular Features of the Copper Binding Sites in the Octarepeat Domain of the Prion Protein
Burns, C. S., Aronoff-Spencer, E., Dunham, C. M., Lario, P., Avdievich, N. I., Antholine, W. E., Olmstead, M. M., Vrielink, A., Gerfen, G. J., Peisach, J., et al. (2002) · Biochemistry · doi:10.1021/bi011922x · Cited by 417
Metadata
- Authors
- Vey, M., Pilkuhn, S., Wille, H., Nixon, R., DeArmond, S. J., Smart, E. J., Anderson, R. G. W., Taraboulos, A., & Prusiner, S. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-12-10
- Volume
- 93
- Issue
- 25
- Pages
- 14945-14949
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2081852339
- Cited by
- 525
- References
- 1
- FWCI
- 7.17
- Type
- journal article
- Language
- en
- Open access
- green
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- Vey, M., Pilkuhn, S., Wille, H., Nixon, R., DeArmond, S. J., Smart, E. J., Anderson, R. G. W., Taraboulos, A., & Prusiner, S. B. (1996). Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.25.14945
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