Normal prion protein trafficking in cultured human erythroblasts
| Autor: | Rebecca E. Griffiths, D J Anstee, Kate J. Heesom |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Erythroblasts
Prions Endosome animal diseases Immunology Endosomes Platelet Membrane Glycoproteins CD59 Biology Endocytosis Biochemistry Tetraspanin 28 Cell membrane Membrane Microdomains Tetraspanin Antigens CD mental disorders medicine Humans Cells Cultured Tetraspanin 30 Cell Membrane Cell Biology Hematology Microvesicles nervous system diseases Cell biology Transport protein Protein Transport medicine.anatomical_structure CD81 |
| Zdroj: | Blood. 110:4518-4525 |
| ISSN: | 1528-0020 0006-4971 |
| Popis: | Normal prion protein (PrPc), an essential substrate for development of prion disease, is widely distributed in hematopoietic cells. Recent evidence that variant Creutzfeldt-Jakob disease can be transmitted by transfusion of red cell preparations has highlighted the need for a greater understanding of the biology of PrPc in blood and blood-forming tissues. Here, we show that in contrast to another glycosylphosphoinositol-anchored protein CD59, PrPc at the cell surface of cultured human erythroblasts is rapidly internalized through the endosomal pathway, where it colocalizes with the tetraspanin CD63. In the plasma membrane, PrPc colocalizes with the tetraspanin CD81. Cross-linking with anti-PrPc or anti-CD81 causes clustering of PrPc and CD81, suggesting they can share the same microdomain. These data are consistent with a role for tetraspanin-enriched microdomains in trafficking of PrPc. These results, when taken together with recent evidence that exosomes released from cells as a result of endosomal-mediated recycling to the plasma membrane contain prion infectivity, provide a pathway for the propagation of prion diseases. |
| Databáze: | OpenAIRE |
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