A soluble form of prion protein in human cerebrospinal fluid: Implications for prion-related encephalopathies

Fabrizio Tagliavini, Frances Prelli, Monica Porro, Mario Salmona, Orso Bugiani, Blas Frangione

Research output: Contribution to journalArticlepeer-review

Abstract

The cellular prion protein (PrPC) is a 33-35 kDa sialoglycoprotein anchored to the external surface of neural and non-neural cells by a glycosyl phosphatidylinositol moiety. In addition, a secretory form of PrPC has been found in cell-free translation systems and in cell cultures. On this basis, we investigated human cerebrospinal fluid for the presence of soluble PrP and identified a protein whose molecular weight, antigenic determinants, N-terminal amino acid sequence and sensitivity to protease digestion corresponded to those of PrPC. In prion-related encephalopathies of humans and animals, the secretory form of PrPC might be converted into the abnormal isoform PrPSc and play a role in the dissemination of the disease process and amyloid formation.

Original languageEnglish
Pages (from-to)1398-1404
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume184
Issue number3
DOIs
Publication statusPublished - May 15 1992

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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