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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.
Jazyk angličtina Země Itálie
Grantová podpora
NI7416
MZ0
CEP - Centrální evidence projektů
Digitální knihovna NLK
Plný text - Část
Zdroj
NLK
Directory of Open Access Journals
od 1994
Free Medical Journals
od 1994
Freely Accessible Science Journals
od 1994
Open Access Digital Library
od 1994-01-01
ROAD: Directory of Open Access Scholarly Resources
od 1996
- MeSH
- Creutzfeldtova-Jakobova nemoc krev přenos MeSH
- cytoplazmatická granula chemie ultrastruktura MeSH
- Heřmanského-Pudlákův syndrom krev MeSH
- krevní transfuze MeSH
- lidé MeSH
- potransfuzní reakce MeSH
- priony krev MeSH
- PrPC proteiny krev MeSH
- trombocyty chemie MeSH
- Check Tag
- lidé 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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