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

Efficient Lymphoreticular Prion Propagation Requires PrPcin Stromal and Hematopoietic Cells

“…It is possible that under these circumstances prions undergo very slow splenic replication and reach an equilibrium with elimination of infectivity. PrP c is a glycophosphatidylinositol-anchored protein (46), and since these proteins can easily transfer from one cell to another (3,27), it is conceivable that "painting" of the Alternatively, the original inoculum may be chronically stored: other antigens, such as human immunodeficiency virus type 1 virions (44,45) and human serum albumin (47), are known to be retained on the plasma membrane of FDCs for months or even years (23,34,48). The immunological or cellular mechanism of such retention may be independent of PrP c : molecules acting as partners of antigen presentation like complement factors (25) or Fc␥ receptors (11) are likely to be involved.…”

Intercellular Trogocytosis Plays an Important Role in Modulation of Immune Responses

“…The glycosyl-phosphatidylinositol (GPI)-anchored proteins are transferred across the homotypic interactions between HeLa cells (38), and the transmembrane protein bride is internalized from one cell by contact with another during the eye development in Drosophila melanogaster (39). Thus, these studies conducted in various systems together present strong evidence that the cell surface proteins are commonly transferred between cells both in vitro and in vivo (9).…”

Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrPC

“…The presence of PrP C in myelin of NSE-PrP mice, therefore, suggests that axolemmal PrP undergoes high-affinity interactions with myelin membrane proteins, as shown for other proteins of the myelin-axolemmal complex (Menon et al, 2003). Alternatively, neuronally synthesized PrP C may be transferred onto myelin sheaths by cell painting, which was shown to be highly efficient in the case of GPI-linked proteins (Anderson et al, 1996).…”

“…If so, oligodendrocytes may provide PrP C to the axon-myelin interface, which would abrogate any cell-autonomous axonal ⌬PrP toxicity in trans. Intercellular transfer of glycosylphosphatidylinositol (GPI)-anchored protein (a phenomenon called "cell painting") was described for CD4 (Anderson et al, 1996) and for PrP C in vitro (Liu et al, 2002). Alternatively, PrP C may act as a ligand and trigger signaling through receptors expressed by neighboring cells.…”