An Mbol RFLP in the human erythrocyte surface protein band 3-like 1 gene (EPB3L1) on chromosome 7q35–7q36

1993 ◽  
Vol 2 (3) ◽  
pp. 337-337
Author(s):  
Michael K. Showe ◽  
Donna Williams ◽  
Louise C. Showe
Keyword(s):  
Human Erythrocyte ◽  
Surface Protein ◽  
Protein Band ◽  
Band 3 ◽  
Erythrocyte Surface

scholarly journals Relationship of the human erythrocyte Wrb antigen to an interaction between glycophorin A and band 3

Blood ◽  
1990 ◽  
Vol 76 (4) ◽  
pp. 842-848 ◽  
Author(s):  
MJ Telen ◽  
JA Chasis
Keyword(s):  
Human Erythrocyte ◽  
Integral Membrane Protein ◽  
Protein Band ◽  
Band 3 ◽  
Glycophorin A ◽  
Lipid Moiety ◽  
Erythrocyte Antigen ◽  
Relationship Of ◽  
Murine Monoclonal Antibodies

Abstract The Wrb antigen is a high-frequency human erythrocyte antigen invariably absent from En (a-) erythrocytes, which lack glycophorin A. However, glycophorin A from En (a+) Wr (a+b-) red cells has an amino acid sequence identical to that of glycophorin A from Wr (b+) erythrocytes. Evidence has suggested that the Wrb antigen may require the interaction of glycophorin A with either a lipid moiety or with another erythrocyte-integral membrane protein, band 3. We have investigated the role of band 3 in Wrb expression using murine monoclonal antibodies (MoAbs) with Wrb specificity. These antibodies reacted by radioimmunoassay (RIA) only with cells expressing both glycophorin A and band 3. In immunoprecipitation studies, Wrb antibodies immunoprecipitated both band 3 and glycophorin A, while antibodies specific for band 3 or glycophorin precipitated only the protein with which they were reactive. These data strongly suggest that band 3 is the other membrane component necessary for expression of Wrb and that band 3 and glycophorin A are closely associated in the erythrocyte membrane.

scholarly journals Relationship of the human erythrocyte Wrb antigen to an interaction between glycophorin A and band 3

Blood ◽  
1990 ◽  
Vol 76 (4) ◽  
pp. 842-848 ◽  
Author(s):  
MJ Telen ◽  
JA Chasis
Keyword(s):  
Human Erythrocyte ◽  
Integral Membrane Protein ◽  
Protein Band ◽  
Band 3 ◽  
Glycophorin A ◽  
Lipid Moiety ◽  
Erythrocyte Antigen ◽  
Relationship Of ◽  
Murine Monoclonal Antibodies

The Wrb antigen is a high-frequency human erythrocyte antigen invariably absent from En (a-) erythrocytes, which lack glycophorin A. However, glycophorin A from En (a+) Wr (a+b-) red cells has an amino acid sequence identical to that of glycophorin A from Wr (b+) erythrocytes. Evidence has suggested that the Wrb antigen may require the interaction of glycophorin A with either a lipid moiety or with another erythrocyte-integral membrane protein, band 3. We have investigated the role of band 3 in Wrb expression using murine monoclonal antibodies (MoAbs) with Wrb specificity. These antibodies reacted by radioimmunoassay (RIA) only with cells expressing both glycophorin A and band 3. In immunoprecipitation studies, Wrb antibodies immunoprecipitated both band 3 and glycophorin A, while antibodies specific for band 3 or glycophorin precipitated only the protein with which they were reactive. These data strongly suggest that band 3 is the other membrane component necessary for expression of Wrb and that band 3 and glycophorin A are closely associated in the erythrocyte membrane.

scholarly journals Interaction ofPlasmodium vivaxTryptophan-rich Antigen PvTRAg38 with Band 3 on Human Erythrocyte Surface Facilitates Parasite Growth

2015 ◽  
Vol 290 (33) ◽  
pp. 20257-20272 ◽  
Author(s):  
Mohd. Shoeb Alam ◽  
Vandana Choudhary ◽  
Mohammad Zeeshan ◽  
Rupesh K. Tyagi ◽  
Sumit Rathore ◽  
...  
Keyword(s):  
Human Erythrocyte ◽  
Band 3 ◽  
Parasite Growth ◽  
Erythrocyte Surface

The nature of human erythrocyte receptors for Neisseria gonorrhoeae

1982 ◽  
Vol 28 (2) ◽  
pp. 219-222 ◽  
Author(s):  
G. M. Wiseman ◽  
P. McNicol
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Human Erythrocyte ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Glycophorin A ◽  
Receptor Sites ◽  
Human Erythrocyte Membranes ◽  
Sepharose 4B

Normal and trypsinized human erythrocyte membranes were used as a model in the study of host cell receptors for Neisseria gonorrhoeae. Receptor sites were identified by adherence inhibition assays of fractions of membranes eluted from polyacrylamide gel electrophoresis columns. Results indicated that inhibition of gonococcus T1 and T4 adherence was associated with erythrocyte protein bands 3 and 4 and glycophorin A, the major sialoglycoprotein. Further investigation revealed that band 3 preparations isolated by affinity chromatography on concanavalin A – Sepharose 4B columns continued to inhibit T1 adherence to erythrocytes but did not inhibit adherence of T4 organisms. It is suggested that protein band 3 is the receptor on erythrocytes for T1 gonococci and that glycophorin A may be the receptor for T4 cells.

Consequences of the presence of elongated variant of the major transmembrane protein (Band 3 protein) in the human erythrocyte

1991 ◽  
Vol 198 (3) ◽  
pp. 255-260 ◽  
Author(s):  
Wanda Retelewska ◽  
Maria Gaczyńska ◽  
Grzegorz Bartosz ◽  
Luba Judkiewicz
Keyword(s):  
Human Erythrocyte ◽  
Transmembrane Protein ◽  
Protein Band ◽  
Band 3 ◽  
Band 3 Protein
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