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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@article{Tagliavini1992ASF, title={A soluble form of prion protein in human cerebrospinal fluid: implications for prion-related encephalopathies.}, author={Fabrizio Tagliavini and Frances Prelli and Massimo Porro and Mario Salmona and Orso Bugiani and Blas Frangione}, journal={Biochemical and biophysical research communications}, year={1992}, volume={184 3}, pages={1398-404} }