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Cited by 132Prion Diseases and Protein MisfoldingAlzheimer's disease research and treatmentsAmyloidosis: Diagnosis, Treatment, Outcomes

Rapid anterograde axonal transport of the cellular prion glycoprotein in the peripheral and central nervous systems

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Borchelt, D.R., Koliatsos, V.E., Guarnieri, M., Pardo, C.A., Sisodia, S.S., Price, D.L.·1994·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)36683-8
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Abstract

In prion diseases, the cellular prion protein (PrPc), abundant in neurons, is converted posttranslationally into an amyloid-forming scrapie prion protein (PrPSc), which accumulates in white matter tracts and nerve terminals.The trafficking of PrPC in neurons was investigated in vivo by injecting [3SSlmethionine into the L4 and L5 dorsal root ganglia and the entorhinal cortices of adult rats and by tracing the movement of radiolabeled PrPc.In both paradigms, labeled 33-35-kDa PrPc was transported, within 4 h, to distal mons and nerve terminals cofractionating with proteins in the fast component.Future studies using these methods may allow us to determine whether PrPc is converted into Prpsc during axonal transport and whether PrPSc is transported in animals with prion diseases.The accumulation of PrP&' is a common feature of the prion disorders, including scrapie in sheep and Creutzfeldt-Jakob disease, familial Creutzfeldt-Jakob disease, Gerstmann-Straussler-Scheinker disease, familial fatal insomnia, and kuru in humans (1-6).Most ofthe prion disorders are transmissible (7-ll), including the familial prion disorders, which are caused by mutations in the human PrP gene (5,6).The principal component of the transmissible agent is PrPSc (6, 12).The PrPSc molecule is derived from a cellular prion protein(PrP'), which is encoded by a single copy gene (13, 14).The chief distinguishing feature of PrP& is that it resists protease digestion, yielding a fragment that aggregates into amyloid rods in the presence of detergents (13,151.Recent evidence indicates that PrPsc and PrPc are conformational isomers (16-18).In the case of familial prion disorders, it is hypothesized that mutations in human PrP alter the conformation of the protein, creating molecules that fold into PrP-like entities (19, 20).The normal function of PrPC, a glycolipid-anchored glycoprotein, is unknown (21-23).Cellular PrP mRNA is expressed in 05146 and NS 20471 and by the American Health Assistance Founda-* This work was supported

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  1. Gasset, M., Baldwin, M. A., Fletterick, F. J., and Prusiner, S. B. (1993) Proc. and Prusiner, S. B. (1991) J. Virol. 65, 1340-1351
  2. Pan, K.-M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A,, Groth, D., Mehl- Nutl. Acad. Sci. U. S. A. SO, 1-5 horn, I., Huang, Z., Fletterick, R. J., Cohen, F. E., and Prusiner, S. B. (1993) Proc. Natl. Acad. Sei. U. S. A. 90,10962-10966
  3. Goldfarb, L. G., Brown, P., Haltia, M., Ghiso, J., Frangione, B., and Gajdusek, D. C. (1993) Proc. Natl. Acad. Sci. U. S. A. SO, 4451-4454
  4. Taraboulos, A., Jendroska, K., Serban, D., Yang, S.-L., and DeArmond, S. J. (1992) Proc. Nutl. Acad. Sei. U. S. A. 89, 7620-7624
  5. Taraboulos, A., Raeber, A., Borchelt, D. R., Serban, D., and Prusiner, S. B. D., and Prusiner, S. B. (1990) Proc. Nutl. Acad. Sei. U. S. A. 87,8262-8266
  6. Beyreuther, K., Fischer, P., Masters, C. L., and Price, D. L. (199O)Proc. Natl. Glycobiology 3, 319-329 Neurosci. 13, 3136-3142

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Authors
Borchelt, D. R., Koliatsos, V. E., Guarnieri, M., Pardo, C. A., Sisodia, S. S., & Price, D. L.
Affiliations
Johns Hopkins University (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1994-05
Volume
269
Issue
20
Pages
14711-14714
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(17)36683-8
OpenAlex
W1565265443
Cited by
132
References
62
Citations by year
2026: 1 · 2025: 2 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 4 · 2018: 1 · 2017: 3 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 6
FWCI
1.14
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institute on Aging (P50AG005146, AG 05146)
  • National Institute of Neurological Disorders and Stroke (NS10580, NS-20471)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
Keywords
cellular prion protein, axonal transport, anterograde transport, prion disease, PrPSc, dorsal root ganglia, entorhinal cortex, peripheral nervous system, central nervous system, protein trafficking
MeSH terms
Animals, Axonal Transport, Brain, Cell Line, Electrophoresis, Polyacrylamide Gel, Ganglia, Spinal, Cricetinae, Mesocricetus, Methionine, Nerve Endings, Nerve Tissue Proteins, Neurons, Organ Specificity, Prions, Rabbits, Sciatic Nerve, Sulfur Radioisotopes, Rats, Sprague-Dawley, PrPSc Proteins, Rats

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