Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes
Stewart, G. W. and Hepworth-Jones, B. E. and Keen, J. N. and Dash, B. C. and Argent, A. C. and Casimir, Colin M. (1992) Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes. Blood, 79 (6). pp. 1593-1601. ISSN 0006-4971
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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.
|Research Areas:||Middlesex University Schools and Centres > School of Science and Technology > Natural Sciences|
Middlesex University Schools and Centres > School of Science and Technology > Natural Sciences > Molecular Biology group
|Citations on ISI Web of Science:||88|
|Deposited On:||02 Dec 2009 10:22|
|Last Modified:||10 Dec 2014 16:29|
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