A red cell band 3 variant with altered stilbene disulphonate binding is associated with the Diego (Dia) blood group antigen

Spring, Frances A.; Bruce, Lesley J.; Anstee, David J.; Tanner, M. J. A.

doi:10.1042/bj2880713

Cited by 59 publications

(28 citation statements)

References 13 publications

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“…The Diego blood (Dia) group antigen was the first to be ascribed to an amino acid change in the extracellular portion of AE1 (Spring, Bruce, Anstee, & Tanner, 1992). As such, these epitopes define regions of AE1 that face the cell exterior, thereby providing valuable topological information ( Fig.…”

Section: Ae1-associated Blood Group Antigensmentioning

confidence: 99%

Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters

Cordat

Reithmeier

2014

Current Topics in Membranes

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Section: Ae1-associated Blood Group Antigensmentioning

confidence: 99%

Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters

Cordat

Reithmeier

2014

Current Topics in Membranes

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“…Membranes were prepared from untreated or chymotrypsin-treated red cells (26). The membrane proteins were separated by SDS-PAGE using the method of Laemmli (27).…”

Section: Anion Transport Studiesmentioning

confidence: 99%

Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.

Bruce¹,

Cope²,

Jones³

et al. 1997

J. Clin. Invest.

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323

287

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All affected patients in four families with autosomal dominant familial renal tubular acidosis (dRTA) were heterozygous for mutations in their red cell HCO 3 Ϫ /Cl Ϫ exchanger, band 3 ( AE1, SLC4A1 ) genes, and these mutations were not found in any of the nine normal family members studied. The mutation Arg 589 → His was present in two families, while Arg 589 → Cys and Ser 613 → Phe changes were found in the other families. Linkage studies confirmed the co-segregation of the disease with a genetic marker close to AE1 . The affected individuals with the Arg 589 mutations had reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. The red cells of individuals with the Ser 613 → Phe mutation had markedly increased red cell sulfate transport but almost normal red cell iodide transport. The erythroid and kidney isoforms of the mutant band 3 proteins were expressed in Xenopus oocytes and all showed significant chloride transport activity. We conclude that dominantly inherited dRTA is associated with mutations in band 3; but both the disease and its autosomal dominant inheritance are not related simply to the anion transport activity of the mutant proteins. ( J. Clin. Invest. 1997.

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“…Recently, we have shown that the AE-1 variant known as Memphis variant I1 is associated with the expression of the Diego (Dia) blood group antigen (16). Further studies have revealed that the Occurrence of the Dia antigen is dependent upon the AE-1 mutation Pro854 -+ Leu (17).…”

Section: Location Of the Dia Antigen To Ae-1mentioning

confidence: 97%

Functional Factors in the Red Cell Membrane: Interactions Between the Membrane and its Underlying Skeleton

Anstee¹,

Hemming²,

Tanner³

1995

Immunological Investigations

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Recent studies involving two abnormal red cell phenotypes (South-east Asian ovalocytosis and Leach phenotype) provide novel information concerning the nature and significance of interactions of both the anion transport protein AE-1 (syn. band 3) and Glycophorins C and D with the underlying skeleton. The location of Wra and Dia blood group antigens to mutations on AE-1 at residues 658 and 854 respectively, together with the availability of monoclonal antibodies recognising epitopes dependent upon the integrity of the third extracellular loop of AE-1, have allowed us to study the organisation of the membrane domain of the mutant AE-1 found in South-east Asian ovalocytes (AE-1 SAO). The results suggest that the organisation of the whole membrane domain of AE-1 SAO is abnormal and that the organisation of other integral membrane proteins like those involved in expression of Rh blood group antigens may also be affected. Increased homo- and hetero-associations involving AE-1 SAO and other integral proteins may in turn result in reduced membrane flexibility. Purified protein 4.1 binds with 50-fold higher affinity to protein 4.1 depleted normal red cell membranes than to protein 4.1 depleted red cell membranes of Leach phenotype which lack Glycophorin C (GPC) and Glycophorin D (GPD). Experiments using purified protein 4.1 and p55 together with synthetic peptides corresponding to different regions of the cytoplasmic domain of Glycophorins C and D (GPC/D) demonstrate that protein 4.1 interacts directly with GPC through residues 82-98. They also show that p55 binds to GPC through residues 112-128. Since p55 also binds directly to protein 4.1 it is clear that protein 4.1 can bind to GPC through two different sites either directly through residues 82-98 or indirectly through p55. These results show that GPC and GPD provide major attachment sites for the red cell skeleton via protein 4.1 and that p55 is part of this complex.

show abstract

A red cell band 3 variant with altered stilbene disulphonate binding is associated with the Diego (Dia) blood group antigen

Cited by 59 publications

References 13 publications

Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters

Structure, Function, and Trafficking of SLC4 and SLC26 Anion Transporters

Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.

Functional Factors in the Red Cell Membrane: Interactions Between the Membrane and its Underlying Skeleton

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