ArticleBlood cells, molecules & diseases2015
Fluorescence assay of the interaction between hemoglobin and the cytoplasmic domain of erythrocyte membrane band 3.
Article in Blood cells, molecules & diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- X-Linked EGFP Reporter as a Tool to Examine X-Chromosome Inactivation in Mouse Embryos and Embryonic Fibroblasts.Biomolecules · 2026Article
- Mechanical Stimulation of Red Blood Cells Aging: Focusing on the Microfluidics Application.Micromachines · 2025Review
- Hemoglobin Binding to the Red Blood Cell (RBC) Membrane Is Associated with Decreased Cell Deformability.International journal of molecular sciences · 2024Article
- The Impact of CaCells · 2023Article
- Carbonyl Stress in Red Blood Cells and Hemoglobin.Antioxidants (Basel, Switzerland) · 2021Review
- Oxygen tension-mediated erythrocyte membrane interactions regulate cerebral capillary hyperemia.Science advances · 2019Article
- Myosin IIA interacts with the spectrin-actin membrane skeleton to control red blood cell membrane curvature and deformability.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Effects of Hypoxia on Erythrocyte Membrane Properties-Implications for Intravascular Hemolysis and Purinergic Control of Blood Flow.Frontiers in physiology · 2017Review
- Cation Homeostasis in Red Cells From Patients With Sickle Cell Disease Heterologous for HbS and HbC (HbSC Genotype).EBioMedicine · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Oxygen tension has emerged as a potent regulator of multiple erythrocyte properties, including glucose metabolism, cell volume, ATP release, and cytoskeletal organization. Because hemoglobin (Hb)(1) binds to the cytoplasmic domain of band 3 (cdb3) in an oxygen dependent manner, with deoxyHb exhibiting significantly greater affinity for cdb3 than oxyHb, the deoxyHb-cdb3 interaction has been hypothesized to constitute the molecular switch for all O2-controlled erythrocyte processes. In this study, we describe a rapid and accurate method for quantitating the interaction of deoxyHb binding to cdb3. For this purpose, enhanced green fluorescent protein (eGFP) is fused to the COOH-terminus of cdb3, and the binding of Hb to the NH2-terminus of cdb3-eGFP is quantitated by Hb-mediated quenching of cdb3-eGFP fluorescence. As expected, the intensity of cdb3-eGFP fluorescence decreases only slightly following addition of oxyHb. However, upon deoxygenation of the same Hb-cdb3 solution, the fluorescence decreases dramatically (i.e. confirming that deoxyHb exhibits much greater affinity for cdb3 than oxyHb). Using this fluorescence quenching method, we not only confirm previously established characteristics of the Hb-cdb3 interaction, but also establish an assay that can be exploited to screen for inhibitors of the sickle Hb-cdb3 interaction that accelerates sickle Hb polymerization.
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