Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes.
Blood
; 79(6): 1593-601, 1992 Mar 15.
Article
en En
| MEDLINE
| ID: mdl-1547348
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Potasio
/
Sodio
/
ADN
/
Proteínas Sanguíneas
/
Membrana Eritrocítica
/
Eritrocitos Anormales
/
Proteínas de la Membrana
Límite:
Humans
Idioma:
En
Revista:
Blood
Año:
1992
Tipo del documento:
Article
Pais de publicación:
Estados Unidos