ArticleThe Biochemical journal1989
Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus of the protein to the cytoplasmic side of the red cell membrane and distribution of the protein in some human tissues.
Article in The Biochemical journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 82 citations in OpenAlex.
- Increased Anion Exchanger-1 (Band 3) on the Red Blood Cell Membrane Accelerates Scavenging of Nitric Oxide Metabolites and Predisposes Hypertension Risks.Function (Oxford, England) · 2025Article
- Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1.American journal of physiology. Cell physiology · 2021Review
- Article
- Structure and Function of SLC4 Family [Formula: see text] Transporters.Frontiers in physiology · 2015Article
- Anion exchanger 1 interacts with nephrin in podocytes.Journal of the American Society of Nephrology : JASN · 2010Article
- Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2).Haematologica · 2010Article
- Topology of transmembrane segments 1-4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis.The Biochemical journal · 2005Article
- Band 3 mutations, renal tubular acidosis and South-East Asian ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band 3 transport in red cells.The Biochemical journal · 2000Article
- Structural model for the organization of the transmembrane spans of the human red-cell anion exchanger (band 3; AE1).The Biochemical journal · 1999Article
- Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined by scanning and insertional N-glycosylation mutagenesis.The Biochemical journal · 1999Article
- Lysine-691 of the anion exchanger from human erythrocytes is located on its cytoplasmic surface.The Biochemical journal · 1998Article
- Complementation studies with co-expressed fragments of human red cell band 3 (AE1): the assembly of the anion-transport domain in xenopus oocytes and a cell-free translation system.The Biochemical journal · 1998Article
- Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.The Journal of clinical investigation · 1997Article
- Infection of C3HeB/FeJ mice with the docile strain of lymphocytic choriomeningitis virus induces autoantibodies specific for erythrocyte Band 3.Immunology · 1997Article
- Functional cell surface expression of the anion transport domain of human red cell band 3 (AE1) in the yeast Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Monoclonal antibodies that react with human band 3 residues 542-555 recognize different conformations of this protein in uninfected and Plasmodium falciparum infected erythrocytes.Molecular and cellular biochemistry · 1995Article
- Isolation and characterization of CD47 glycoprotein: a multispanning membrane protein which is the same as integrin-associated protein (IAP) and the ovarian tumour marker OA3.The Biochemical journal · 1994Article
- Article
- Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868-->Leu in the membrane domain of band 3.The Biochemical journal · 1993Article
- Functional activation of plasma membrane anion exchangers occurs in a pre-Golgi compartment.The Journal of cell biology · 1993Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
(1) We have prepared murine monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein (band 3). (2) All of these antibodies react with regions of the protein located at the cytoplasmic surface of the red cell. (3) One of the antibodies reacts with an epitope present on a cytoplasmic loop of the protein located between the C-terminus and a point 168 amino acids from the C-terminus. The other antibodies recognize different epitopes on the C-terminal tail of the protein and the sequences likely to be involved in these epitopes are defined. (4) Our results show that the C-terminus of the red-cell anion transport protein is located on the cytoplasmic side of the red-cell membrane. (5) None of the antibodies inhibited sulphate exchange transport when introduced into resealed red-cell membranes; however, the bivalent form of one of the antibodies reduced the inhibitory potency of 4-acetamido-4'-isothiocyanatostilbene disulphonate on sulphate exchange transport in resealed erythrocyte membranes. (6) Immunostaining of human kidney sections with the antibodies showed strong staining of the basolateral membrane of some but not all of the epithelial cells of distal tubules and the initial connecting segment of collecting tubules. With human liver, only the haematopoeitic cells of fetal liver reacted with all the antibodies.
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