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Enrichment of two glycosyl-phosphatidylinositol-anchored proteins,
acetylcholinesterase and decay accelerating factor, in vesicles released
from human red blood cells
P Butikofer, FA Kuypers, CM Xu, DT Chiu and B Lubin
Children's Hospital Oakland Research Institute, CA.
Several proteins are attached to the cell membrane by a glycosyl-
phosphatidylinositol (GPI) anchor. In this report, we show that during
vesiculation of human RBCs in vitro, two of these proteins,
acetylcholinesterase and decay accelerating factor, redistribute on the
cell surface and become enriched in the released vesicles. As a result, the
remnant cells are depleted of these proteins. We suggest that alterations
in the architecture of the RBC membrane that precede vesiculation lead to
selective polarization of GPI-anchored proteins within the domain of the
membrane destined to become a vesicle. Since vesiculation occurs in many
cell types, and if the loss of GPI-anchored proteins accompanies this
process, it may have important biologic significance.
Volume 74,
Issue 5,
pp. 1481-1485,
10/01/1989
Copyright © 1989 by The American Society of Hematology
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