ArticleThe Biochemical journal2002
Ca2+ promotes erythrocyte band 3 tyrosine phosphorylation via dissociation of phosphotyrosine phosphatase from band 3.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 55 citations in OpenAlex.
- Proteomic Analysis of the Role of the Adenylyl Cyclase-cAMP Pathway in Red Blood Cell Mechanical Responses.Cells · 2022Article
- Identification of tyrosine kinase inhibitors that halt Plasmodium falciparum parasitemia.PloS one · 2020Article
- Reticulocyte and red blood cell deformation triggers specific phosphorylation events.Blood advances · 2019Article
- Squeezing for Life - Properties of Red Blood Cell Deformability.Frontiers in physiology · 2018Review
- The Effect of Sepsis on the Erythrocyte.International journal of molecular sciences · 2017Review
- Human Erythrocyte Acetylcholinesterase in Health and Disease.Molecules (Basel, Switzerland) · 2017Review
- Short-Term Effects of Chlorpromazine on Oxidative Stress in Erythrocyte Functionality: Activation of Metabolism and Membrane Perturbation.Oxidative medicine and cellular longevity · 2016Article
- Band 3 Erythrocyte Membrane Protein Acts as Redox Stress Sensor Leading to Its Phosphorylation by p (72) Syk.Oxidative medicine and cellular longevity · 2016Article
- Oxidative stress in β-thalassaemia and sickle cell disease.Redox biology · 2015Review
- Particle Simulation of Oxidation Induced Band 3 Clustering in Human Erythrocytes.PLoS computational biology · 2015Article
- C4d deposits on the surface of RBCs in trauma patients and interferes with their function.Critical care medicine · 2014Article
- Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging.Frontiers in physiology · 2014Review
- Mechanisms tagging senescent red blood cells for clearance in healthy humans.Frontiers in physiology · 2013Review
- Hemoglobin redox reactions and red blood cell aging.Antioxidants & redox signaling · 2013Review
- Calcium in red blood cells-a perilous balance.International journal of molecular sciences · 2013Review
- Palytoxin induces functional changes of anion transport in red blood cells: metabolic impact.The Journal of membrane biology · 2011Article
- Aging and death signalling in mature red cells: from basic science to transfusion practice.Blood transfusion = Trasfusione del sangue · 2010Review
- Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation.The Journal of biological chemistry · 2008Article
- PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells.Proteomics · 2008Article
- Augmented erythrocyte band-3 phosphorylation in septic mice.Biochimica et biophysica acta · 2007Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The anion-exchange band 3 protein is the main erythrocyte protein that is phosphorylated by protein tyrosine kinase (PTK). We have previously identified a band 3-associated phosphotyrosine phosphatase (PTP) that is normally highly active and prevents the accumulation of band 3 phosphotyrosine. Band 3 tyrosine phosphorylation can be induced by inhibition of PTP (vanadate, thiol oxidation), activation of PTK (hypertonic NaCl) or intracellular increased Ca(2+) (mechanism unknown). We now show that there is inhibition of dephosphorylation of band 3 in Ca(2+)/ionophore-treated erythrocytes and in membranes isolated from the treated cells. These membranes exhibit phosphatase activity upon the addition of exogenous substrate. Dephosphorylation of the endogenous substrate (band 3) can be activated in these membranes by the addition of Mg(2+). Thus the inability of PTP to dephosphorylate the band 3 phosphotyrosine is not due to inhibition of the enzyme itself. Ca(2+) rise in the erythrocyte causes dissociation of PTP from band 3, thus leaving the kinase unopposed. This is shown by a significant diminution in band 3/PTP co-precipitation. Addition of Mg(2+) to these membranes leads to reassociation of band 3 with PTP. The Ca(2+)-induced inhibition of band 3 dephosphorylation may be due to Ca(2+)-dependent alterations in membrane components and structure, affecting the interaction of band 3 with PTP. The Ca(2+)-induced tyrosine phosphorylation, involving an apparent PTP inhibition via dissociation from the substrate, may play a role in signal transduction pathways and in certain pathological disorders associated with increased cell Ca(2+).
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