Substitution Glu480Lys in erythroid band 3 corresponds to the Fr<sup>a</sup> blood group antigen and supports existence of the second ectoplasmic loop of band 3

Jarolím, Petr; Kalabova, Dana; Reid, Marion E.

doi:10.1111/j.1537-2995.2004.03291.x

Cited by 6 publications

(5 citation statements)

References 37 publications

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“…These estimates agree with existing topological data on EC1 [23][24][25], and are consistent with the region surrounding Tyr 486 being extracellular [29,30]. As well, our new model ( Figure 5) puts Glu 480 in EC2, rather than within TM3 [21], and accounts for its association with the Fr a blood group antigen [29,30]. The polar sequences Gly 455 -Ala-Pro-Gln linking TMs 2 and 3, and Glu 508 -Gly-Ser are placed on the cytosolic side of the membrane in our new model.…”

Section: Discussionsupporting

confidence: 91%

“…N-Glycosylation sites created in an extended EC1 can be glycosylated [20,21,28], confirming the extracellular disposition of the EC1. The presence of the low-incidence Froese blood group antigen Fr a , resulting from the G480K mutation in the loop connecting TMs 3 and 4, confirms the existence of EC2 [29,30]. No internal markers have defined the cytosolic loop linking TMs 2 and 3, although these long hydrophobic segments are connected by a short polar sequence (Gly 455 -Ala-Pro-Gln).…”

Section: Introductionmentioning

confidence: 91%

See 1 more Smart Citation

Topology of transmembrane segments 1–4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis

Cheung

Reithmeier

2005

Biochemical Journal

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Human AE1 (anion exchanger 1), or Band 3, is an abundant membrane glycoprotein found in the plasma membrane of erythrocytes. The physiological role of the protein is to carry out chloride/bicarbonate exchange across the plasma membrane, a process that increases the carbon-dioxide-carrying capacity of blood. To study the topology of TMs (transmembrane segments) 1-4, a series of scanning N-glycosylation mutants were created spanning the region from EC (extracellular loop) 1 to EC2 in full-length AE1. These constructs were expressed in HEK-293 (human embryonic kidney) cells, and their N-glycosylation efficiencies were determined. Unexpectedly, positions within putative TMs 2 and 3 could be efficiently glycosylated. In contrast, the same positions were very poorly glycosylated when present in mutant AE1 with the SAO (Southeast Asian ovalocytosis) deletion (DeltaA400-A408) in TM1. These results suggest that the TM2-3 region of AE1 may become transiently exposed to the endoplasmic reticulum lumen during biosynthesis, and that there is a competition between proper folding of the region into the membrane and N-glycosylation at introduced sites. The SAO deletion disrupts the proper integration of TMs 1-2, probably leaving the region exposed to the cytosol. As a result, engineered N-glycosylation acceptor sites in TM2-3 could not be utilized by the oligosaccharyltransferase in this mutant form of AE1. The properties of TM2-3 suggest that these segments form a re-entrant loop in human AE1.

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Section: Discussionsupporting

confidence: 91%

Section: Introductionmentioning

confidence: 91%

Topology of transmembrane segments 1–4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis

Cheung

Reithmeier

2005

Biochemical Journal

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“…1a. However, E480L has been argued to be an antigen on the extracellular side (Jarolim et al 2004). An N-glycosylation site (35 amino acids of loop 7-8 including the native glyco-sylation site) inserted at residue 484 of the N642D mutant is N-glycosylated in a cell-free system (Popov et al 1997).…”

Section: N-terminal Half Of the Ae1 Membrane Domain (Tm1 To Tm7)mentioning

confidence: 99%

Topology models of anion exchanger 1 that incorporate the anti-parallel V-shaped motifs found in the EM structureThis paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health and Disease, and has undergone the Journal’s usual peer review process.

Hirai

Yamaguchi

Ikeda

2011

Biochem. Cell Biol.

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We recently published the three-dimensional structure of the membrane domain of human erythrocyte anion exchanger 1 (AE1) at 7.5 Å resolution, solved by electron crystallography. The structure exhibited distinctive anti-parallel V-shaped motifs, which protrude from the membrane bilayer on both sides. Similar motifs exist in the previously reported structure of a bacterial chloride channel (ClC)-type protein. Here, we propose two topology models of AE1 that reflect the anti-parallel V-shaped structural motifs. One is assumed to have structural similarity with the ClC protein and the other is only assumed to have internal repeats, as is often the case with transporters. Both models are consistent with most topological results reported thus far for AE1, each having advantages and disadvantages.

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“…With this approach and by combining 2-DE and MALDI-TOF MS, several membrane proteins as well as filamentous proteins were identified on 2-D gels. With the exception of band 3, which carries Diego antigens [53], no other red blood cell antigens relevant to transfusion medicine were directly or indirectly identified in this study. Tyan et al [54], by profiling erythrocyte proteins after proteolytic digestion and identification using 2-D ESI-MS/MS, identified 272 proteins.…”

Section: Erythrocytesmentioning

confidence: 66%

Proteomics and transfusion medicine: Future perspectives

et al. 2006

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Limited number of important discoveries have greatly contributed to the progresses achieved in the blood transfusion; ABO histo-blood groups, citrate as anticoagulant, fractionation of plasma proteins, plastic bags and apheresis machines. Three major types of blood products are transfused to patients: red cell concentrates, platelet concentrates and fresh frozen plasma. Several parameters of these products change during storage process and they have been well studied over the years. However, several aspects have completely been ignored; in particular those related to peptide and protein changes. This review presents what has been done using proteomic tools and the potentials of proteomics for transfusion medicine.

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Substitution Glu480Lys in erythroid band 3 corresponds to the Fr^a blood group antigen and supports existence of the second ectoplasmic loop of band 3

Cited by 6 publications

References 37 publications

Topology of transmembrane segments 1–4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis

Topology of transmembrane segments 1–4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis

Proteomics and transfusion medicine: Future perspectives

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Substitution Glu480Lys in erythroid band 3 corresponds to the Fra blood group antigen and supports existence of the second ectoplasmic loop of band 3

Cited by 6 publications

References 37 publications

Topology of transmembrane segments 1–4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis

Topology of transmembrane segments 1–4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis

Proteomics and transfusion medicine: Future perspectives

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Substitution Glu480Lys in erythroid band 3 corresponds to the Fr^a blood group antigen and supports existence of the second ectoplasmic loop of band 3