Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane

Passow, Hermann

doi:10.1007/3540153330_2

Cited by 157 publications

(145 citation statements)

References 300 publications

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“…5). The best matches from data base searches were between these putative membrane domains and the membrane-spanning domains of a number of eucaryotic and viral proteins, most notably with one of the membrane domains of the band 3 anion-exchange protein (32). We infer from these results that ORF1 encodes an integral membrane protein, but the similarities were not strong enough to allow any inferences as to function.…”

Section: Resultsmentioning

confidence: 91%

Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence

et al. 1993

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Section: Resultsmentioning

confidence: 91%

Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence

et al. 1993

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“…PCR products corresponding to ␣-and ␤-globin, the globin mRNA expressed by erythroid precursors in adult mammals, were found in isolated glomeruli ( Figure 1B). To confirm purity of glomeruli and lack of contaminating erythroid cells obtained by the sieving, we also performed RT-PCR of an abundant-in-erythrocyte gene, AE1, 5,6 and showed that glomeruli did not express AE1. The absence of the PCR products generated by primers specific for the AE1 gene transcript strongly suggested that globin gene expression in rat glomeruli was not the result of erythroid cell contamination.…”

Section: Hb Is Expressed In Glomeruli Of the Normal Rat Kidneymentioning

confidence: 99%

Hemoglobin Is Expressed by Mesangial Cells and Reduces Oxidant Stress

Nishi¹,

Inagi²,

Kato³

et al. 2008

Journal of the American Society of Nephrology

130

125

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Hemoglobin (Hb) serves as the main oxygen transporter in erythrocytes, but it is also expressed in nonhematopoietic organs, where it serves an unknown function. In this study, microarray and proteomic analyses demonstrated Hb expression in the kidney. Rat kidneys were perfused extensively with saline, and glomeruli were isolated by several techniques (sieving, manual dissection, and laser capturemicrodissection). Reverse transcriptase-PCR revealed glomerular ␣-and ␤-globin expression, and immunoblotting demonstrated expression of the protein. In situ hybridization studies showed expression of the globin subunits in the mesangium, and immunostaining confirmed this localization of Hb. Furthermore, globin mRNA expression was detected in primary cultures of rat mesangial cells but not in cultured glomerular endothelial or epithelial cells. For investigation of Hb function in mesangial cells, the SV40-MES13 murine mesangial cell line was transfected with a vector expressing ␣-and ␤-globins; this overexpression reduced production of hydrogen peroxide-induced intracellular radical oxygen species and enhanced cell viability against oxidative stress. In summary, Hb is expressed by rat mesangial cells, and its potential functions may include antioxidative defense.

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“…Human erythrocyte AE isoform 1 (AE1) is the bestcharacterized member [1,2]. Although the kinetics of anion exchange have been studied extensively for AE1 [3,4], relating these kinetic data to a mechanistic model for protein function requires structural information describing the anion-translocation channel.…”

Section: Introductionmentioning

confidence: 99%

“…TwoAbbreviations used : AE, anion exchanger ; AE1, AE isoform 1 ; AE1C − , cysteineless form of AE1 ; BCECF-AM, 2h,7h-bis-(2-carboxyethyl)-(5 and 6)-carboxyfluorescein acetoxymethyl ester ; biotin maleimide, 3-(N-maleimidylpropionyl)biocytin ; BMH, bismaleimidohexane ; C 12 E 8 , octaethylene glycol monodecyl ether ; CuP, Cu(II)-(1,10-phenanthroline) 3 ; DTT, dithiothreitol ; EC, extracellular loop ; IC, intracellular loop ; o-PDM, N,Nh-ophenylenedimaleimide ; p-PDM, N,Nh-p-phenylenedimaleimide ; TM, transmembrane segment. 1 Present address: Department of Clinical Laboratory Sciences, John Radcliffe Hospital, University of Oxford, Oxford OX3 9DU, U.K. 2 To whom correspondence should be addressed (e-mail joe.casey!ualberta.ca).…”

Section: Introductionmentioning

confidence: 99%

Cysteine-directed cross-linking localizes regions of the human erythrocyte anion-exchange protein (AE1) relative to the dimeric interface

Taylor

Zhu

Casey

2001

Biochemical Journal

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The human erythrocyte anion-exchanger isoform 1 (AE1) is a dimeric membrane protein that exchanges chloride for bicarbonate across the erythrocyte plasma membrane. Crystallographic studies suggest that the transmembrane anion channel lies at the interface between the two monomers, whereas kinetic analysis provides evidence that each monomer contains an anion channel. We have studied the structure-function relationship of residues at the dimeric interface of AE1 by cysteine-directed cross-linking. Single cysteine mutations were introduced in 16 positions of putative loop regions throughout AE1. The ability of these residues to be chemically cross-linked to their partner within the dimeric protein complex was assessed by mobility of the protein on immunoblots. Introduced cysteine residues in extracellular loops (ECs) 1-4 and intracellular loop 1 formed

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Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane

Cited by 157 publications

References 300 publications

Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence

Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence

Hemoglobin Is Expressed by Mesangial Cells and Reduces Oxidant Stress

Cysteine-directed cross-linking localizes regions of the human erythrocyte anion-exchange protein (AE1) relative to the dimeric interface

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