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Expression of cellular prion protein on platelets from patients with gray platelet or Hermansky-Pudlak syndrome and the protein's association with alpha-granules
Holada K, Glierova H, Simak J, Vostal JG.
Language English Country Italy
Grant support
NI7416
MZ0
CEP Register
Digital library NLK
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NLK
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- MeSH
- Creutzfeldt-Jakob Syndrome blood transmission MeSH
- Cytoplasmic Granules chemistry ultrastructure MeSH
- Hermanski-Pudlak Syndrome blood MeSH
- Blood Transfusion MeSH
- Humans MeSH
- Transfusion Reaction MeSH
- Prions blood MeSH
- PrPC Proteins blood MeSH
- Blood Platelets chemistry MeSH
- Check Tag
- Humans MeSH
The cellular prion protein (PrPc) is a membrane glycoprotein expressed on many human cells including platelets. We investigated the cellular localization of platelet PrPc. In resting platelets most PrPc was localized inside the cells. The correlation of PrPc and P-selectin surface up-regulation after platelet activation suggested its association with alpha-granules. This was confirmed by normal expression of PrPc on Hermansky-Pudlak syndrome platelets, which lack dense granules, and failure of gray platelet syndrome platelets, which lack alpha-granules, to up-regulate PrPc. Our results warrant further studies on the role of platelet PrPc in the transmission of prion diseases by blood transfusion.
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- $a Expression of cellular prion protein on platelets from patients with gray platelet or Hermansky-Pudlak syndrome and the protein's association with alpha-granules / $c Holada K, Glierova H, Simak J, Vostal JG.
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- $a Institute of Immunology and Microbiology, 1st Faculty of Medicine Charles University Prague, Studnickova 7, 128 20 Prague 2, Czech Republic. karel.holada@LF1.cuni.cz
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- $a The cellular prion protein (PrPc) is a membrane glycoprotein expressed on many human cells including platelets. We investigated the cellular localization of platelet PrPc. In resting platelets most PrPc was localized inside the cells. The correlation of PrPc and P-selectin surface up-regulation after platelet activation suggested its association with alpha-granules. This was confirmed by normal expression of PrPc on Hermansky-Pudlak syndrome platelets, which lack dense granules, and failure of gray platelet syndrome platelets, which lack alpha-granules, to up-regulate PrPc. Our results warrant further studies on the role of platelet PrPc in the transmission of prion diseases by blood transfusion.
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