ArticleBiophysical journal1995
Loss of rotational mobility of band 3 proteins in human erythrocyte membranes induced by antibodies to glycophorin A.
Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- Interaction of the human erythrocyte Band 3 anion exchanger 1 (AE1, SLC4A1) with lipids and glycophorin A: Molecular organization of the Wright (Wr) blood group antigen.PLoS computational biology · 2018Article
- Full-Length Anion Exchanger 1 Structure and Interactions with Ankyrin-1 Determined by Zero Length Crosslinking of Erythrocyte Membranes.Structure (London, England : 1993) · 2017Article
- Diffusion of glycophorin A in human erythrocytes.Biochimica et biophysica acta · 2016Article
- Photophysical studies of bioconjugated ruthenium metal-ligand complexes incorporated in phospholipid membrane bilayers.Inorganic chemistry · 2013Article
- Article
- Flexibility of the cytoplasmic domain of the anion exchange protein, band 3, in human erythrocytes.Biophysical journal · 2001Article
- Red-cell glycophorin A-band 3 interactions associated with the movement of band 3 to the cell surface.The Biochemical journal · 2000Article
- Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer.Biophysical journal · 1998Article
- The orientation of eosin-5-maleimide on human erythrocyte band 3 measured by fluorescence polarization microscopy.Biophysical journal · 1996Article
- A tethered adhesive particle model of two-dimensional elasticity and its application to the erythrocyte membrane.Biophysical journal · 1996Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The effect of antibodies to glycophorin A on the rotational diffusion of band 3 in human erythrocyte membranes was investigated by transient dichrosim. Three antibodies that recognize different epitopes on the exofacial domain of glycophorin A all strongly reduce the rotational mobility of band 3. The effect is at most only weakly dependent on the distance of the epitope from the membrane surface. The degree of immobilization obtained with two of the antibodies, BRIC14 and R18, is very similar to that produced by antibodies to band 3 itself. Similar results were obtained with membranes stripped of skeletal proteins. Fab fragments and an antibody to glycophorin C had no effect on band 3 rotational mobility. These results rule out a mechanism whereby band 3 rotational immobilization results from enhanced interactions with the membrane skeleton that are mediated by a conformational change in glycophorin A. Rather, they strongly indicate that the antibodies to glycophorin A cross-link existing band 3-glycophorin A complexes that have lifetimes that are long compared with the millisecond time scale of the transient dichroism measurements.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.