The Low-Incidence Blood Group Antigen, Wda, Is Associated with Substitution Val(557-> Met in Human Erythrocyte Band 3 (AE1)

Vox Sanguinis ◽  
1996 ◽  
Vol 71 (2) ◽  
pp. 118-120
Author(s):  
Lesley J. Bruce ◽  
Teresa Zelinski ◽  
Kay Ridgwell ◽  
Michael J. A. Tanner
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Blood Group Antigen ◽  
Low Incidence

The Low-Incidence Blood Group Antigen, Wda, Is Associated with the Substitution Val557→ Met in Human Erythrocyte Band 3 (AE1)

Vox Sanguinis ◽  
1996 ◽  
Vol 71 (2) ◽  
pp. 118-120 ◽  
Author(s):  
Lesley J. Bruce ◽  
Teresa Zelinski ◽  
Kay Ridgwell ◽  
Michael J. A. Tanner
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Blood Group Antigen ◽  
Low Incidence

scholarly journals Structural relationships between human erythrocyte sialoglycoproteins β and γ and abnormal sialoglycoproteins found in certain rare human erythrocyte variants lacking the Gerbich blood-group antigen(s)

1987 ◽  
Vol 244 (1) ◽  
pp. 123-128 ◽  
Author(s):  
M E Reid ◽  
D J Anstee ◽  
M J A Tanner ◽  
K Ridgwell ◽  
G T Nurse
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Blood Group Antigen ◽  
Human Erythrocyte Membrane ◽  
Diffuse Band ◽  
Structural Relationships ◽  
Normal Erythrocyte

The human erythrocyte membrane sialoglycoproteins beta and gamma are important for the maintenance of the discoid shape of the normal erythrocyte. In this paper we show that the human erythrocyte sialoglycoproteins beta and gamma (hereafter called beta and gamma) are structurally related. Rabbit antisera produced against purified beta and beta 1 and rendered specific to the cytoplasmic portion of these proteins also react with the cytoplasmic portion of gamma. Some human anti-Gerbich (Ge) sera react with the extracellular portion of both beta and gamma. This reactivity is shown to be directed towards a common epitope on beta and gamma. However, most anti-Ge sera do not react with beta, but react with an extracellular epitope only present on gamma. All individuals who lack the Ge antigens lack beta and gamma. In some cases abnormal sialoglycoproteins are present in the erythrocytes, and these are shown to be structurally related to beta and gamma. Rabbit antisera raised against the purified abnormal sialoglycoprotein from a Ge-negative erythrocyte type reacted with the cytoplasmic portion of both beta and gamma. Unlike normal beta and gamma, the abnormal sialoglycoproteins found in Ge-negative erythrocytes migrate as a diffuse band on SDS/polyacrylamide-gel electrophoresis. Studies using endoglycosidases suggest that the diffuse nature of these bands results from carbohydrate heterogeneity and that the abnormal sialoglycoproteins contain N-glycosidically linked oligosaccharides with repeating lactosamine units. Such polylactosamine chains are not present on normal beta or gamma.

A Thr552 ->Ile substitution in erythroid band 3 gives rise to the Warrior blood group antigen

Transfusion ◽  
1997 ◽  
Vol 37 (4) ◽  
pp. 398-405 ◽  
Author(s):  
P Jarolim ◽  
JL Murray ◽  
HL Rubin ◽  
G Coghlan ◽  
T Zelinski
Keyword(s):  
Blood Group ◽  
Band 3 ◽  
Blood Group Antigen

Characterization of Seven Low Incidence Blood Group Antigens Carried by Erythrocyte Band 3 Protein

Blood ◽  
1998 ◽  
Vol 92 (12) ◽  
pp. 4836-4843
Author(s):  
P. Jarolim ◽  
H.L. Rubin ◽  
D. Zakova ◽  
J. Storry ◽  
M.E. Reid
Keyword(s):  
Blood Group ◽  
Molecular Basis ◽  
Structural Model ◽  
Major Effect ◽  
Band 3 ◽  
Normal Band ◽  
Blood Group System ◽  
Blood Group Antigens ◽  
Dna Encoding ◽  
Low Incidence

Recent studies have demonstrated that band 3 carries antigens of the Diego blood group system and have elucidated the molecular basis of several previously unassigned low incidence and high incidence antigens. Because the available serological data suggested that band 3 may carry additional low incidence blood group antigens, we screened band 3 genomic DNA encoding the membrane domain of band 3 for single-strand conformational polymorphisms. We found that the putative first ectoplasmic loop of band 3 carries blood group antigen ELO, 432 Arg→Trp; the third putative loop harbors antigens Vga (Van Vugt), 555 Tyr→His, BOW 561 Pro→Ser, Wu (Wulfsberg), 565 Gly→Ala, and Bpa (Bishop), 569 Asn→Lys; and the putative fourth ectoplasmic loop carries antigens Hga (Hughes), 656 Arg→Cys, and Moa (Moen), 656 Arg→His. We studied erythrocytes from carriers of five of these blood group antigens. We found similar levels of reticulocyte mRNA corresponding to the two band 3 gene alleles, normal content and glycosylation of band 3 in the red blood cell membrane, and normal band 3-mediated sulfate influx into red blood cells, suggesting that the mutations do not have major effect on band 3 structure and function. In addition to elucidating the molecular basis of seven low incidence blood group antigens, these results help to create a more accurate structural model of band 3.

Characterization of Seven Low Incidence Blood Group Antigens Carried by Erythrocyte Band 3 Protein

Blood ◽  
1998 ◽  
Vol 92 (12) ◽  
pp. 4836-4843 ◽  
Author(s):  
P. Jarolim ◽  
H.L. Rubin ◽  
D. Zakova ◽  
J. Storry ◽  
M.E. Reid
Keyword(s):  
Blood Group ◽  
Molecular Basis ◽  
Structural Model ◽  
Major Effect ◽  
Band 3 ◽  
Normal Band ◽  
Blood Group System ◽  
Blood Group Antigens ◽  
Dna Encoding ◽  
Low Incidence

Abstract Recent studies have demonstrated that band 3 carries antigens of the Diego blood group system and have elucidated the molecular basis of several previously unassigned low incidence and high incidence antigens. Because the available serological data suggested that band 3 may carry additional low incidence blood group antigens, we screened band 3 genomic DNA encoding the membrane domain of band 3 for single-strand conformational polymorphisms. We found that the putative first ectoplasmic loop of band 3 carries blood group antigen ELO, 432 Arg→Trp; the third putative loop harbors antigens Vga (Van Vugt), 555 Tyr→His, BOW 561 Pro→Ser, Wu (Wulfsberg), 565 Gly→Ala, and Bpa (Bishop), 569 Asn→Lys; and the putative fourth ectoplasmic loop carries antigens Hga (Hughes), 656 Arg→Cys, and Moa (Moen), 656 Arg→His. We studied erythrocytes from carriers of five of these blood group antigens. We found similar levels of reticulocyte mRNA corresponding to the two band 3 gene alleles, normal content and glycosylation of band 3 in the red blood cell membrane, and normal band 3-mediated sulfate influx into red blood cells, suggesting that the mutations do not have major effect on band 3 structure and function. In addition to elucidating the molecular basis of seven low incidence blood group antigens, these results help to create a more accurate structural model of band 3.

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