Enrichment of two glycosyl-phosphatidylinositol-anchored proteins, acetylcholinesterase and decay accelerating factor, in vesicles released from human red blood cells

Abstract

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.

Complement‐induced procoagulant alteration of red blood cell membranes with microvesicle formation in paroxysmal nocturnal haemoglobinuria (PNH): implication for thrombogenesis in PNH

“…A23187-induced microvesiculation of RBC. Calciuminduced vesiculation of RBC was performed exactly as described by Bu È tikofer et al (1989). Brie¯y, washed RBC (16% haematocrit) were equilibrated in 10 mM Tris-HCl, pH 7´4, 144 mM NaCl, 2 g/l glucose, and 1 mM CaCl 2 (378C, 3 min).…”

Transfer of the glycosylphosphatidylinositol‐anchored 5′‐nucleotidase CD73 from adiposomes into rat adipocytes stimulates lipid synthesis

“…Subsequently, the predominant site of release of both microvesicles and GPI-proteins was identified as DIGs (Del Conde et al, 2005). Compatible with this view was the observed loss of the DIGs-associated GPIproteins, CD55 and CD59, from human erythrocytes upon their storage (Long et al, 1993) and the spontaneous release of the GPI-proteins, acetylcholinesterase and decay accelerating factor, from human erythrocytes into microvesicles (Bütikofer et al, 1989).…”

The phospholipid composition and cholesterol content of platelet-derived microparticles: a comparison with platelet membrane fractions

“…MPs are thought to be formed by budding of the surface membrane, in a process that also involves proteolysis of components of the membrane skeleton [16,17]. Certain platelet proteins are selectively shed into released vesicles [4][5][6]18], and the same phenomenon has been described for other cell types as well [19][20][21][22][23]. Whether membrane lipids are also selectively sorted into MPs is unknown.…”