Molecular mapping of human band 3 anion transport regions using synthetic peptides

1991 ◽  
Vol 5 (1) ◽  
pp. 109-115 ◽  
Author(s):  
Marguerite M. B. Kay
Keyword(s):  
Synthetic Peptides ◽  
Molecular Mapping ◽  
Band 3 ◽  
Anion Transport

Antibodies to synthetic peptides based on band 3 motifs react specifically with Plasmodium falciparum (humanmalaria)-infected erythrocytes and block cytoadherence

Parasitology ◽  
1994 ◽  
Vol 108 (4) ◽  
pp. 389-396 ◽  
Author(s):  
I. Crandall ◽  
I. W. Sherman
Keyword(s):  
Amino Acids ◽  
Plasmodium Falciparum ◽  
Synthetic Peptides ◽  
Protein Band ◽  
Significant Degree ◽  
Band 3 ◽  
Anion Transport ◽  
Amelanotic Melanoma ◽  
Murine Mabs ◽  
Antibodies To Synthetic Peptides

SUMMARYRabbit polyclonal and mouse monoclonal antibodies (Mabs) prepared against synthetic peptides patterned on exofacialloops 3 (amino acids 546–555) and 7 (821–834) of the human anion transport protein band 3 inhibited the cytoadherence of Plasmodium falciparum-infected erythrocytes to C32 amelanotic melanoma cells. Mabs directed against exofacial loop4 (amino acids 628–642) did not inhibit adherence to a significant degree. The murine Mabs recognized only P. falciparum- infected erythrocytes suggesting that the epitopes of loops 3, 4 and 7 are normally cryptic in uninfected erythrocytes.

Alterations of band 3 transport protein by cellular aging and disease: erythrocyte band 3 and glucose transporter share a functional relationship

1990 ◽  
Vol 68 (12) ◽  
pp. 1419-1427 ◽  
Author(s):  
Gieljan J. C. G. M. Bosman ◽  
Marguerite M. B. Kay
Keyword(s):  
Glucose Transport ◽  
Structural Changes ◽  
Glucose Transporter ◽  
Functional Relationship ◽  
Band 3 ◽  
Anion Transport ◽  
Cellular Aging ◽  
Abnormal Band ◽  
Membrane Spanning

Structural changes in human erythrocyte band 3 that affect anion transport are correlated with changes in glucose transport in situ. Breakdown of band 3, observed during normal erythrocyte aging in situ and in some diseases involving erythrocytes, is associated with an increase in Km and a decrease in Vmax of sulfate self-exchange, and with an increase in Km and Vmax of glucose efflux. Erythrocytes containing a high molecular weight form of band 3 exhibit an increase in Vmax of sulfate exchange and a decrease in Vmax of glucose efflux. Identical transport characteristics are observed in abnormal band-3-containing erythrocytes from individuals with familial amyotrophic chorea with acanthocytosis. A third band 3 alteration, fast-aging band 3, exhibits decreased Vmax of sulfate exchange and an increase in Km and decrease in Vmax of glucose efflux. Changes in band 3 structure that are the result of unstable hemoglobin or a deficiency in glucose-6-phosphate dehydrogenase and that do not affect anion transport have no effect on glucose transport characteristics. These data indicate the existence of a functional relationship between the membrane-spanning, anion-transport domain of band 3 and glucose transport in human erythrocytes. Antibodies to synthetic peptides reveal structural changes in membranes from the three inborn band 3 alterations and in band 3 itself in membranes from fast-aging band 3. Thus, immunological data suggests a structural relationship between anion and glucose transporters.Key words: red cell, anion transport, membrane proteins, aging, choreoacanthocytosis, anemia.

Erythrocyte Band 3 Protein Phosphorylation Modulates Anion Transport in Nephrolithiasic Patients

1994 ◽  
pp. 137-138
Author(s):  
B. Baggio ◽  
L. Bordin ◽  
G. Gambaro ◽  
M. Vincenti ◽  
M. Nassuato ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Band 3 ◽  
Anion Transport ◽  
Band 3 Protein

The red cell band 3 protein: its role in anion transport

1982 ◽  
Vol 299 (1097) ◽  
pp. 497-507 ◽  
Keyword(s):  
Binding Sites ◽  
Band 3 ◽  
Anion Transport ◽  
Anion Binding ◽  
Hydrophobic Residues ◽  
Ping Pong ◽  
Hydrophilic Residues ◽  
Aqueous Core ◽  
Positively Charged

Studies of anion transport across the red blood cell membrane fall generally into two categories: (1) those concerned with the operational characterization of the transport system, largely by kinetic analysis and inhibitor studies; and (2) those concerned with the structure of band 3, a transmembrane peptide identified as the transport protein. The kinetics are consistent with a ping-pong model in which positively charged anion-binding sites can alternate between exposure to the inside and outside compartments but can only shift one position to the other when occupied by an anion. The structural studies on band 3 indicate that only 60 % of the peptide is essential for transport. That particular portion is in the form of a dimer consisting of an assembly of membrane-crossing strands (each monomer appears to cross at least five times). The assembly presents its hydrophobic residues toward the interior of the bilayer, but its hydrophilic residues provide an aqueous core. The transport involves a small conformational change in which an anion-binding site (involving positively charged residues) can alternate between positions that are topologically in and topologically out.

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