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      Glycosyl Phosphatidylinositol Anchor

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          Recently, we and others demonstrated the unique potential for glycosyl phosphatidylinositol (GPI) anchored proteins to transfer from one cell membrane to another in a process we termed ‘painting’. The GPI-anchored proteins were shown to transfer intact and functional. The full significance of this phenomenon has yet to be fully realized, but implications exist in many areas including disease transmission (prions), cell protection (endothelial cells), and senescence (erythrocytes). It is of interest to note that cells exhibiting limited or no biosynthetic capacity (spermatozoa and erythrocytes) have been implicated thus far in cell-cell transfer of GPI-linked molecules. This observation demonstrates the potential for GPI-linked proteins to be ‘painted’ onto cells which otherwise may be incapable of expressing exogenous proteins. We show in this paper that GPI-linked CD59 and decay-accelerating factor will transfer intact from erythrocytes to endothelial cells in transgenic mice. We also demonstrate that the transfer process occurs under physiological conditions using several experimental models including organ and bone marrow transplantation. We detail the procedure to effect transfer of GPI-linked proteins from one cell type to another in either an in vivo or in vitro system.

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          Intercellular transfer of a glycosylphosphatidylinositol (GPI)-linked protein: release and uptake of CD4-GPI from recombinant adeno-associated virus-transduced HeLa cells.

          A diverse group of GPI-anchored protein structures are ubiquitously expressed on the external cell membranes of eukaryotes. Whereas the physiological role for these structures is usually defined by their protein component, the precise biological significance of the glycolipid anchors remains vague. In the course of producing a HeLa cell line (JM88) that contained a recombinant adeno-associated virus genome expressing a GPI-anchored CD4-GPI fusion protein on the surface of the cells, we noted the transfer of CD4-GPI to native HeLa cells. Transfer occurred after direct cell contact or exposure to JM88 cell supernatants. The magnitude of contact-mediated CD4-GPI transfer correlated with temperature. Supernatant CD4-GPI also attached to human red blood cells and could be cleaved with phosphatidylinositol-specific phospholipase C. The attached CD4-GPI remained biologically active after transfer and permitted the formation of syncytium when coated HeLa cells were incubated with glycoprotein 160 expressing H9 cells. JM88 cells provide a model for the production, release, and reattachment of CD4-GPI and may furnish insight into a physiologic role of naturally occurring GPI-anchored proteins. This approach may also allow the production of other recombinant GPI-anchored proteins for laboratory and clinical investigation.

            Author and article information

            Nephron Exp Nephrol
            Cardiorenal Medicine
            S. Karger AG
            April 1998
            20 March 1998
            : 6
            : 2
            : 148-151
            Nextran, Princeton, N.J., USA
            20516 Exp Nephrol 1998;6:148–151
            © 1998 S. Karger AG, Basel

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            Tables: 2, References: 28, Pages: 4
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            Technical Seminar: Tissue Targeting


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