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Blood, 15 February 2001, Vol. 97, No. 4, pp. 1141-1143
BRIEF REPORT
Stomatin, flotillin-1, and flotillin-2 are major integral
proteins of erythrocyte lipid rafts
Ulrich Salzer and
Rainer Prohaska
From the Institute of Medical Biochemistry, University
of Vienna, Vienna Biocenter, Vienna, Austria.
Lipid rafts are sphingolipid- and cholesterol-rich
membrane microdomains that are insoluble in nonionic detergents, have a low buoyant density, and preferentially contain lipid-modified proteins, like glycosyl phosphatidylinositol (GPI)-anchored proteins. The lipid rafts were isolated from human erythrocytes and major protein
components were identified. Apart from the GPI-anchored proteins, the
most abundant integral proteins were found to be the distantly related
membrane proteins stomatin (band 7.2b), flotillin-1, and flotillin-2.
Flotillins, already described as lipid raft components in neurons and
caveolae-associated proteins in A498 kidney cells, have not been
recognized as red cell components yet. In addition, it was shown that
the major cytoskeletal proteins, spectrin, actin, band 4.1, and band
4.2, are partly associated with the lipid rafts. Stomatin and the
flotillins are present as independently organized high-order oligomers,
suggesting that these complexes act as separate scaffolding components
at the cytoplasmic face of erythrocyte lipid rafts.

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