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Many proteins are associated with the outer layer of the cell membrane through a posttranslationally added glycosyl phosphatidylinositol (GPI) anchor. The functional significance of this type of protein linkage is unclear, although it results in increased lateral mobility, sorting to the apical surface of the cell, reinsertion into cell membranes, and possibly cell signaling. Here evidence is presented that GPI-linked proteins can undergo intermembrane transfer in vivo. GPI-linked proteins expressed on the surface of transgenic mouse red blood cells were transferred in a functional form to endothelial cells in vivo. This feature of GPI linkage may be potentially useful for the delivery of therapeutic proteins to vascular endothelium.

Type

Journal article

Journal

Science

Publication Date

07/07/1995

Volume

269

Pages

89 - 92

Keywords

Animals, Antigens, CD, Base Sequence, Bone Marrow Transplantation, CD55 Antigens, CD59 Antigens, Cell Membrane, Cells, Cultured, Complement Inactivator Proteins, Endothelium, Vascular, Erythrocytes, Globins, Glycosylphosphatidylinositols, Humans, Membrane Glycoproteins, Mice, Mice, Transgenic, Molecular Sequence Data, Myocardium