Miller J L, Giattina M, Mackie E J, Dwyer N K
Laboratory of Chemical Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
J Lab Clin Med. 1998 Mar;131(3):215-21. doi: 10.1016/s0022-2143(98)90092-0.
Glycosylphosphatidylinositol-anchored proteins (GPI-proteins) expressed on the outer leaflet of cell membranes are involved in diverse physiologic as well as pathologic processes in humans. Previously, we demonstrated the intercellular transfer of overexpressed CD4-GPI in vitro from transduced HeLa cells to their parental cell line. In this report we present further information on the transfer process and the nature of the transferred GPI-proteins. In mixed-cell populations, the transfer of CD4-GPI was detectable within minutes at levels proportional to the ratio of donor and recipient cells. The amount of CD4-GPI detected with flow cytometry on the surface of the recipient cells varied according to cell type. Microscopy of mixed cell populations revealed discrete CD4-GPI containing aggregates on the target cells, whereas colocalized transfer of cytoplasm was not detected. Separation of cocultivated cells by semipermeable membranes largely prevented CD4-GPI transfer, but aggregates containing CD4-GPI were demonstrated by electron microscopy in supernatants passed through filters of 0.4-mm pore size.