Mechanism of anion exchange across the red cell membrane by band 3: interactions between stilbenedisulfonate and NAP-taurine binding sites

Biochemistry ◽  
1981 ◽  
Vol 20 (20) ◽  
pp. 5695-5701 ◽  
Author(s):  
Ian G. Macara ◽  
Lewis C. Cantley
Keyword(s):  
Cell Membrane ◽  
Anion Exchange ◽  
Binding Sites ◽  
Band 3 ◽  
Red Cell ◽  
Red Cell Membrane

scholarly journals Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites

1992 ◽  
Vol 282 (1) ◽  
pp. 75-80 ◽  
Author(s):  
E Kahana ◽  
J C Pinder ◽  
K S Smith ◽  
W B Gratzer
Keyword(s):  
Cell Membrane ◽  
Fluorescence Quenching ◽  
Binding Sites ◽  
Cytoskeletal Proteins ◽  
Lipid Phase ◽  
Side Chains ◽  
Red Cell ◽  
Segmental Mobility ◽  
Red Cell Membrane ◽  
Hydrophobic Binding

The intrinsic fluorescence of spectrin is strongly quenched by low concentrations of 2-bromostearate. This results from binding at a series of hydrophobic sites. Analysis of dynamic fluorescence quenching by acrylamide, iodide and caesium ions, separately and in conjunction with 2-bromostearate, leads to the conclusion that most of the tryptophan side-chains are exposed to solvent. The sites at which the fatty-acid-quenched tryptophans are located apparently interact with the lipid bilayer in the cell, as judged by quenching by bromostearate dissolved in the lipid phase. A minor proportion of the side-chains in native spectrin give rise to sharp proton magnetic resonance signals, indicative of segmental mobility; these chain elements contain some tryptophan residues, as revealed by weak downfield signals from the heterocyclic ring protons. These signals are not appreciably perturbed by stearic acid or by phosphatidylserine liposomes, suggesting that the hydrophobic binding sites are not in mobile chain elements. By contrast with a series of globular proteins which, with the exception of serum albumins, show little or no quenching by 2-bromostearate, the peripheral red cell membrane skeletal proteins ankyrin (and its spectrin-binding domain), protein 4.1 and (to a lesser extent) actin show evidence of a high affinity for the hydrophobic ligand and may, like spectrin, interact directly with the bilayer in situ.

scholarly journals Plasmodium falciparum histidine-rich protein 1 associates with the band 3 binding domain of ankyrin in the infected red cell membrane

2000 ◽  
Vol 1502 (3) ◽  
pp. 461-470 ◽  
Author(s):  
Cathleen Magowan ◽  
Wataru Nunomura ◽  
Karena L. Waller ◽  
Jackson Yeung ◽  
Joy Liang ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Cell Membrane ◽  
Band 3 ◽  
Binding Domain ◽  
Red Cell ◽  
Red Cell Membrane

ELECTRICAL RESISTANCE OF THE RED CELL MEMBRANE AND THE RELATION BETWEEN NET ANION TRANSPORT AND THE ANION EXCHANGE MECHANISM

1980 ◽  
Vol 341 (1 Anion and Pro) ◽  
pp. 357-360 ◽  
Author(s):  
J. F. Hoffman ◽  
J. H. Kaplan ◽  
T. J. Callahan ◽  
J. C. Freedman
Keyword(s):  
Cell Membrane ◽  
Anion Exchange ◽  
Electrical Resistance ◽  
Anion Transport ◽  
Exchange Mechanism ◽  
Red Cell ◽  
Red Cell Membrane

Relation between red cell membrane (Na+ + K+)-ATPase and band 3 protein

1981 ◽  
Vol 649 (3) ◽  
pp. 557-571 ◽  
Author(s):  
Eric T. Fossel ◽  
A.K. Solomon
Keyword(s):  
Cell Membrane ◽  
Band 3 ◽  
Red Cell ◽  
Band 3 Protein ◽  
Red Cell Membrane

Proteolysis of band 3 is enhanced by anti-Rho(D) binding to the red cell membrane

1984 ◽  
Vol 124 (2) ◽  
pp. 437-442 ◽  
Author(s):  
Edward J. Victoria ◽  
Jeanine E. Kleeman ◽  
S.P. Masouredis
Keyword(s):  
Cell Membrane ◽  
Band 3 ◽  
Red Cell ◽  
Red Cell Membrane

Red cell membrane protein distribution during malarial invasion

1989 ◽  
Vol 92 (4) ◽  
pp. 691-699
Author(s):  
A.R. Dluzewski ◽  
P.R. Fryer ◽  
S. Griffiths ◽  
R.J. Wilson ◽  
W.B. Gratzer
Keyword(s):  
Cell Membrane ◽  
Host Cell ◽  
Transmembrane Protein ◽  
Parasitophorous Vacuole ◽  
Lamellar Body ◽  
Band 3 ◽  
Red Cell ◽  
Protein Distribution ◽  
Red Cell Membrane ◽  
Thin Sections

Immuno-gold labelling electron microscopy of thin sections was used to determine the distribution of red cell membrane and membrane skeleton proteins in the vicinity of internalized malaria parasites. When examined immediately after invasion (young ring-stage parasites), the parasitophorous vacuole membranes of both Plasmodium falciparum and P. knowlesi were found to be characterized by the essentially complete absence of spectrin, ankyrin and the most abundant transmembrane protein, band 3. P. knowlesi merozoites were trapped in the attached but not internalized state by pretreatment with cytochalasin B. In this merozoite-red cell complex antibody labelling showed that band 3 had been eliminated from the region of the host cell membrane in contact with the parasite. Internal vesicles, originating apparently from the site of attachment, were often observed in the red cell. Opposite the attached parasite a cavity was also sometimes seen in the host cell, presumably representing an incipient internal vesicle. The membrane was intact, as judged by the absence of protein (haemoglobin) in the cavity, and, like the membranes surrounding the internal vesicles, was devoid of membrane proteins. A large multilamellar body was sometimes seen in the merozoite close to its point of attachment. The lamellar spacing was about 50 nm. The electron microscope images suggest a diffusion of electron-dense material from the lamellar body into the cavity in the host cell.

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