A Soluble Form of Prion Protein in Human Cerebrospinal Fluid: Implications for Prion-Related Encephalopathies

Biochem Biophys Res Commun. 1992 May 15;184(3):1398-404. doi: 10.1016/s0006-291x(05)80038-5.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adolescent
  • Adult
  • Amino Acid Sequence
  • Antibodies
  • Biomarkers / cerebrospinal fluid
  • Brain Diseases / cerebrospinal fluid
  • Brain Diseases / diagnosis*
  • Child, Preschool
  • Epitopes / analysis
  • Humans
  • Membrane Glycoproteins / cerebrospinal fluid
  • Molecular Sequence Data
  • Molecular Weight
  • Peptides / chemical synthesis
  • Peptides / immunology
  • PrPSc Proteins
  • Prions / cerebrospinal fluid*
  • Prions / isolation & purification
  • Solubility

Substances

  • Antibodies
  • Biomarkers
  • Epitopes
  • Membrane Glycoproteins
  • Peptides
  • PrPSc Proteins
  • Prions