Abstract
Prion diseases are neurodegenerative disorders characterized by the accumulation of abnormal isoforms of prion protein (PrP(Sc)) in the central nervous system. PrP(Sc) isoforms differ from their normal homologue (PrP(C)), in that they possess increased β-sheet conformation, are partially protease resistant and may be associated with amyloid deposition. Amyloid proteins are thought to derive from soluble precursors or fragments thereof, present in biological fluids, which in the disease state undergo conformational change lending to aggregation and deposition in target tissues. We report here that platelets carry PrP mRNA and release PrP(C), a sialoglycoprotein bound to the cell surface by a glycosylphosphatidylinositol (GPI) anchor. Soluble PrP(C) and a N-terminal truncated PrP(C) isoform starting at position 90 are secreted by resting and agonist-stimulated platelets and are detectable after partial deglycosylation of releasates. N-terminal sequence analysis of the soluble 27-30 kDa isoform, GQGGGTHSQ(W)NKP, revealed homology to scrapie PrP27-30, the protease resistant core derived from PrP(Sc). These findings indicate that in addition to PrP(C), platelets process a soluble PrP27-30 isoform. Whether this isoform can be converted into scrapie PrP27-30 remains to be determined.
| Original language | English |
|---|---|
| Pages (from-to) | 572-577 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 223 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Jun 25 1996 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
PRP27-30 is a normal soluble prion protein fragment released by human platelets. / Perini, Francesco; Vidal, Ruben; Ghetti, Bernardino; Tagliavini, Fabrizio; Frangione, Blas; Prelli, Frances.
In: Biochemical and Biophysical Research Communications, Vol. 223, No. 3, 25.06.1996, p. 572-577.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - PRP27-30 is a normal soluble prion protein fragment released by human platelets
AU - Perini, Francesco
AU - Vidal, Ruben
AU - Ghetti, Bernardino
AU - Tagliavini, Fabrizio
AU - Frangione, Blas
AU - Prelli, Frances
PY - 1996/6/25
Y1 - 1996/6/25
N2 - Prion diseases are neurodegenerative disorders characterized by the accumulation of abnormal isoforms of prion protein (PrP(Sc)) in the central nervous system. PrP(Sc) isoforms differ from their normal homologue (PrP(C)), in that they possess increased β-sheet conformation, are partially protease resistant and may be associated with amyloid deposition. Amyloid proteins are thought to derive from soluble precursors or fragments thereof, present in biological fluids, which in the disease state undergo conformational change lending to aggregation and deposition in target tissues. We report here that platelets carry PrP mRNA and release PrP(C), a sialoglycoprotein bound to the cell surface by a glycosylphosphatidylinositol (GPI) anchor. Soluble PrP(C) and a N-terminal truncated PrP(C) isoform starting at position 90 are secreted by resting and agonist-stimulated platelets and are detectable after partial deglycosylation of releasates. N-terminal sequence analysis of the soluble 27-30 kDa isoform, GQGGGTHSQ(W)NKP, revealed homology to scrapie PrP27-30, the protease resistant core derived from PrP(Sc). These findings indicate that in addition to PrP(C), platelets process a soluble PrP27-30 isoform. Whether this isoform can be converted into scrapie PrP27-30 remains to be determined.
AB - Prion diseases are neurodegenerative disorders characterized by the accumulation of abnormal isoforms of prion protein (PrP(Sc)) in the central nervous system. PrP(Sc) isoforms differ from their normal homologue (PrP(C)), in that they possess increased β-sheet conformation, are partially protease resistant and may be associated with amyloid deposition. Amyloid proteins are thought to derive from soluble precursors or fragments thereof, present in biological fluids, which in the disease state undergo conformational change lending to aggregation and deposition in target tissues. We report here that platelets carry PrP mRNA and release PrP(C), a sialoglycoprotein bound to the cell surface by a glycosylphosphatidylinositol (GPI) anchor. Soluble PrP(C) and a N-terminal truncated PrP(C) isoform starting at position 90 are secreted by resting and agonist-stimulated platelets and are detectable after partial deglycosylation of releasates. N-terminal sequence analysis of the soluble 27-30 kDa isoform, GQGGGTHSQ(W)NKP, revealed homology to scrapie PrP27-30, the protease resistant core derived from PrP(Sc). These findings indicate that in addition to PrP(C), platelets process a soluble PrP27-30 isoform. Whether this isoform can be converted into scrapie PrP27-30 remains to be determined.
UR - http://www.scopus.com/inward/record.url?scp=0030601023&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030601023&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1996.0936
DO - 10.1006/bbrc.1996.0936
M3 - Article
VL - 223
SP - 572
EP - 577
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -