A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity.
- 1 September 1991
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 88 (17), 7664-7668
- https://doi.org/10.1073/pnas.88.17.7664
Abstract
The mammalian prion protein (PrPC) is a cellular protein of unknown function, an altered isoform of which (PrPSc) is a component of the infectious particle (prion) thought to be responsible for spongiform encephalopathies in humans and animals. We report here the isolation of a cDNA that encodes a chicken protein that is homologous to PrPC. This chicken prion-like protein (ch-PrLP) is identical to the mouse PrP at 33% of its amino acid positions, including an uninterrupted stretch of 24 identical residues, and it displays the same structural domains. In addition, ch-PrLP, like its mammalian counterpart, is attached to the cell surface by a glycosyl-phosphatidylinositol anchor. We find that ch-PrLP is the major protein in preparations of an acetylcholine receptor-inducing activity that has been purified greater than 10(6)-fold from brain on the basis of its ability to stimulate synthesis of nicotinic receptors by cultured myotubes. The ch-PrLP gene is expressed in the spinal cord and brain as early as embryonic day 6; and in the spinal cord, the protein appears to be concentrated in motor neurons. Our results therefore raise the possibility that prion proteins serve normally to regulate the chemoreceptor number at the neuromuscular junction and perhaps in the central nervous system as well.Keywords
This publication has 26 references indexed in Scilit:
- Unraveling prion diseases through molecular geneticsTrends in Neurosciences, 1989
- SCRAPIE PRIONSAnnual Review of Microbiology, 1989
- At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cellsJournal of Molecular Biology, 1987
- Computer-assisted predictions of signal peptidase processing sitesBiochemical and Biophysical Research Communications, 1987
- Trans-activation of human immunodeficiency virus occurs via a bimodal mechanismCell, 1986
- Scrapie and cellular PrP isoforms are encoded by the same chromosomal geneCell, 1986
- Signal sequencesJournal of Molecular Biology, 1985
- A Method for Isolation of Intact, Translationally Active Ribonucleic AcidDNA, 1983
- Novel Proteinaceous Infectious Particles Cause ScrapieScience, 1982
- A general method applicable to the search for similarities in the amino acid sequence of two proteinsJournal of Molecular Biology, 1970