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Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein.

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Affiliations

  • 1. Department of Neurology, University of California, San Francisco 94143.
      Authors
    • Stahl N 1
    (1 author)

Biochemistry, 01 Sep 1990, 29(38):8879-8884
https://doi.org/10.1021/bi00490a001 PMID: 1980209 

Abstract 

Analysis of carboxy-terminal peptides derived from endoproteinase Lys-C digests of the scrapie isoform of the hamster prion protein revealed that the majority of the molecules are glycoinositol phospholipid linked through ethanolamine attached at serin-231. However, approximately 15% of PrPSc had a carboxy-terminal peptide that ends at glycine-228. It is intriguing that this glycine is part of the PrP sequence Gly-Arg-Arg, which is an established target sequence for the proteolysis and release of bioactive peptides from larger precursors. The mechanism of formation, as well as the role of the truncated carboxy terminus in the dissemination and neuropathology of scrapie, remains to be determined.

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Read article at publisher's site: https://doi.org/10.1021/bi00490a001

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NCRR NIH HHS (1)

NIA NIH HHS (1)

NINDS NIH HHS (1)