myo-Inositol trispyrophosphate: a novel allosteric effector of hemoglobin with high permeation selectivity across the red blood cell plasma membrane
| العنوان: | myo-Inositol trispyrophosphate: a novel allosteric effector of hemoglobin with high permeation selectivity across the red blood cell plasma membrane |
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| المؤلفون: | Ruth Greferath, Jean-Marie Lehn, Claude Nicolau, Carolina D. Duarte |
| المساهمون: | Institut de Science et d'ingénierie supramoléculaires (ISIS), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Chaire Chimie des Interactions Moléculaires, Collège de France (CdF (institution)) |
| المصدر: | ChemBioChem ChemBioChem, Wiley-VCH Verlag, 2010, pp.2543-2548. ⟨10.1002/cbic.201000499⟩ |
| سنة النشر: | 2010 |
| مصطلحات موضوعية: | Cell Membrane Permeability, Erythrocytes, Taurine, Inositol Phosphates, Allosteric regulation, 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, Hemoglobins, Allosteric Regulation, Anion Exchange Protein 1, Erythrocyte, medicine, [CHIM]Chemical Sciences, Humans, Molecular Biology, Band 3, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Ion Transport, biology, Chemistry, 030302 biochemistry & molecular biology, Organic Chemistry, Transport protein, Dissociation constant, Red blood cell, medicine.anatomical_structure, DIDS, biology.protein, Molecular Medicine, Hemoglobin, Intracellular |
| الوصف: | myo-Inositol trispyrophosphate (ITPP), a novel membrane-permeant allosteric effector of hemoglobin (Hb), enhances the regulated oxygen release capacity of red blood cells, thus counteracting the effects of hypoxia in diseases such as cancer and cardiovascular ailments. ITPP-induced shifting of the oxygen-hemoglobin equilibrium curve in red blood cells (RBCs) was inhibited by DIDS and NAP-taurine, indicating that band 3 protein, an anion transporter mainly localized on the RBC membrane, allows ITPP entry into RBCs. The maximum intracellular concentration of ITPP, determined by ion chromatography, was 5.5×10(-3) M, whereas a drop in concentration to the limit of detection was observed in NAP-taurine-treated RBCs. The dissociation constant of ITPP binding to RBC ghosts was found to be 1.72×10(-5) M. All data obtained indicate that ITPP uptake is mediated by band 3 protein and is thus highly tissue-selective towards RBCs, a feature of major importance for its potential therapeutic use. |
| تدمد: | 1439-7633 1439-4227 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2eaf12fd74999cf0a518ac32f06d04d https://pubmed.ncbi.nlm.nih.gov/21086482 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....c2eaf12fd74999cf0a518ac32f06d04d |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14397633 14394227 |
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