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Blood, 1 April 2002, Vol. 99, No. 7, pp. 2569-2577
RED CELLS
Ca++-dependent vesicle release from erythrocytes
involves stomatin-specific lipid rafts, synexin (annexin VII),
and sorcin
Ulrich Salzer,
Peter Hinterdorfer,
Ursula Hunger,
Cordula Borken, and
Rainer Prohaska
From the Institute of Medical Biochemistry, University
of Vienna, Vienna Biocenter, Vienna, Austria, and the Institute for
Biophysics, Johannes Kepler University, Linz, Austria.
Cytosolic Ca++ induces the shedding of microvesicles
and nanovesicles from erythrocytes. Atomic force microscopy was used to determine the sizes of these vesicles and to resolve the patchy, fine
structure of the microvesicle membrane. The vesicles are highly
enriched in glycosyl phosphatidylinositol-linked proteins, free of cytoskeletal components, and depleted of the major
transmembrane proteins. Both types of vesicles contain 2 as-yet-unrecognized red cell proteins, synexin and sorcin, which
translocate from the cytosol to the membrane upon
Ca++ binding. In nanovesicles, synexin and sorcin are
the most abundant proteins after hemoglobin. In contrast, the
microvesicles are highly enriched in stomatin. The membranes of both
microvesicles and nanovesicles contain lipid rafts. Stomatin is the
major protein of the microvesicular lipid rafts, whereas synexin and
sorcin represent the major proteins of the nanovesicular rafts in the presence of Ca++. Interestingly, the raft proteins
flotillin-1 and flotillin-2 are not found in the vesicles but remain in
the red cell membrane. These data indicate the presence of different
types of lipid rafts in the erythrocyte membrane with distinct fates
after Ca++ entry. Synexin, which is known to be vital to
the process of membrane fusion, is suggested to be a key component in
the process of vesicle release from erythrocytes.
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