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Science 7 July 1995:
Vol. 269. no. 5220, pp. 89 - 92
DOI: 10.1126/science.7541557
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Articles

Science, Vol 269, Issue 5220, 89-92
Copyright © 1995 by American Association for the Advancement of Science

articles

In vivo transfer of GPI-linked complement restriction factors from erythrocytes to the endothelium

DL Kooyman, GW Byrne, S McClellan, D Nielsen, M Tone, H Waldmann, TM Coffman, KR McCurry, JL Platt, and JS Logan

Sir William Dunn School of Pathology, Oxford, UK.

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.


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