On the same cell type GPI-anchored normal cellular prion and DAF protein exhibit different biological properties.
Biochem Biophys Res Commun
; 303(2): 446-51, 2003 Apr 04.
Article
in En
| MEDLINE
| ID: mdl-12659837
ABSTRACT
Normal cellular prion protein (PrP(C)) and decay-accelerating factor (DAF) are glycoproteins linked to the cell surface by glycosylphosphatidylinositol (GPI) anchors. Both PrP(C) and DAF reside in detergent insoluble complex that can be isolated from human peripheral blood mononuclear cells. However, these two GPI-anchored proteins possess different cell biological properties. The GPI anchor of DAF is markedly more sensitive to cleavage by phosphatidylinositol-specific phospholipase C (PI-PLC) than that of PrP(C). Conversely, PrP(C) has a shorter cell surface half-life than DAF, possibly due to the fact that PrP(C) but not DAF is shed from the cell surface. This is the first demonstration that on the surface of the same cell type two GPI-anchored proteins differ in their cell biological properties.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Type C Phospholipases
/
Prions
/
Glycosylphosphatidylinositols
/
CD55 Antigens
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2003
Document type:
Article
Affiliation country:
China