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

doi:10.1016/S0006-291X(05)80038-5

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 journal › Article › peer-review

Abstract

The cellular prion protein (PrP^C) 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 PrP^C 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 PrP^C. In prion-related encephalopathies of humans and animals, the secretory form of PrP^C might be converted into the abnormal isoform PrP^Sc and play a role in the dissemination of the disease process and amyloid formation.

Original language	English
Pages (from-to)	1398-1404
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	184
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(05)80038-5
Publication status	Published - May 15 1992

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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

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.",

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T1 - A soluble form of prion protein in human cerebrospinal fluid

T2 - Implications for prion-related encephalopathies

AU - Tagliavini, Fabrizio

AU - Prelli, Frances

AU - Porro, Monica

AU - Salmona, Mario

AU - Bugiani, Orso

AU - Frangione, Blas

PY - 1992/5/15

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

Abstract

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