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Isolation of cDNA coding for an ubiquitous membrane protein deficient in
high Na+, low K+ stomatocytic erythrocytes
GW Stewart, BE Hepworth-Jones, JN Keen, BC Dash, AC Argent and CM Casimir
Department of Medicine, University College and Middlesex Medical School,
Rayne Institute, London, UK.
Human red blood cells (RBCs) that are deficient in an integral membrane-
associated protein ("stomatin") of apparent molecular mass 31 Kd show a
catastrophic increase in passive membrane permeability to the univalent
cations Na+ and K+ and are stomatocytic in shape. We have purified this
protein from normal RBC membranes and isolated a cDNA clone coding for it.
The deduced protein sequence is unrelated to that of any known ion-
transport-related protein. Selective solubilization studies using
detergents show that while the protein is strongly associated with the
phospholipid bilayer, it also binds to the cytoskeleton. The predicted
polypeptide has a single trans-membranous hydrophobic segment near the
N-terminus, which would locate it in the membrane; the large C-terminal
domain is hydrophilic and cytoplasmic in orientation and is presumed to be
responsible for the attachment to the cytoskeleton. By inference, the
protein has the function of closing a latent ion channel. The messenger RNA
encoding this protein is ubiquitously distributed in different human cell
types and tissues and is thus presumably a widely distributed regulator of
transmembrane cation fluxes. As a membrane- bound inhibitor protein of Na+
and K+ transport, it is unique among the known components of
membrane-transport proteins.
Volume 79,
Issue 6,
pp. 1593-1601,
03/15/1992
Copyright © 1992 by The American Society of Hematology
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