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• W93254315 startingPage "1784" @default.
• W93254315 abstract "Abstract 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." @default.
• W93254315 created "2016-06-24" @default.
• W93254315 creator A5050868687 @default.
• W93254315 creator A5053106363 @default.
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• W93254315 date "1998-03-01" @default.
• W93254315 modified "2023-09-28" @default.
• W93254315 title "In Vitro Incorporation of GPI-Anchored Proteins Into Human Erythrocytes and Their Fate in the Membrane" @default.
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• W93254315 doi "https://doi.org/10.1182/blood.v91.5.1784" @default.
• W93254315 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9473247" @default.
• W93254315 hasPublicationYear "1998" @default.
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