NR ALIP
AU Tagliavini,F.; Prelli,F.; Porro,M.; Salmona,M.; Bugiani,O.; Frangione,B.
TI A soluble form of prion protein in human cerebrospinal fluid: implications for prion-related encephalopathies.
QU Biochemical and Biophysical Research Communications 1992 May 15; 184(3): 1398-404
PT journal article
AB 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.
MH Adolescent; Adult; Amino Acid Sequence; Antibodies; Biological Markers/cerebrospinal fluid; Brain Diseases/cerebrospinal fluid/*diagnosis; Child, Preschool; Epitopes/analysis; Human; Membrane Glycoproteins/cerebrospinal fluid; Molecular Sequence Data; Molecular Weight; Peptides/chemical synthesis/immunology; PrPsc Proteins; Prions/*cerebrospinal fluid/isolation & purification; Solubility; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
AD Istituto Neurologico Carlo Besta, Milano, Italy.
SP englisch
PO USA