In vitro incorporation of GPI-anchored proteins into human erythrocytes and their fate in the membrane
| Autor: | Gianluca Civenni, St, Test, Brodbeck U, Bütikofer P |
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| Rok vydání: | 1998 |
| Předmět: |
Isoflurophate
Membrane Glycoproteins Glycosylphosphatidylinositols Octoxynol Phosphatidylinositol Diacylglycerol-Lyase Immunology Erythrocyte Membrane Membrane Proteins Cell Biology Hematology Tritium Biochemistry carbohydrates (lipids) Solubility Type C Phospholipases Acetylcholinesterase Phospholipase D Humans lipids (amino acids peptides and proteins) Calcium Ethanolamine Variant Surface Glycoproteins Trypanosoma |
| Zdroj: | Europe PubMed Central |
| ISSN: | 0006-4971 |
| Popis: | In many different cells, glycosylphosphatidylinositol (GPI)-anchored molecules are clustered in membrane microdomains that resist extraction by detergents at 4°C. In this report, we identified the presence of such domains in human erythrocytes and examined the ability of exogenously-added GPI-anchored molecules to colocalize with the endogenous GPI-anchored proteins in these detergent-insoluble complexes. We found that the addition to human erythrocytes of three purified GPI-anchored proteins having different GPI lipid moieties resulted in their efficient and correct incorporation into the membrane. The extent of membrane insertion was dependent on the intactness of the GPI lipid moiety. However, unlike the endogenous GPI-anchored proteins, the in vitro incorporated GPI molecules were not resistant to membrane extraction by Triton X-100 at 4°C. In addition, in contrast to the endogenous GPI-anchored proteins, they were not preferentially released from erythrocytes during vesiculation induced by calcium loading of the cells. These results suggest that in vitro incorporated GPI-linked molecules are excluded from pre-existing GPI-enriched membrane areas in human erythrocytes and that these microdomains may represent the sites of membrane vesicle formation. |
| Databáze: | OpenAIRE |
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