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Hemoglobin Variants as Targets for Stabilizing Drugs.
Molecules
January 2025
Faculty of Science, Pavol Jozef Šafárik University in Košice, Park Angelinum 19, 040 01 Košice, Slovakia.
Hemoglobin is an oxygen-transport protein in red blood cells that interacts with multiple ligands, e.g., oxygen, carbon dioxide, carbon monoxide, and nitric oxide.
View Article and Find Full Text PDFModulation of the Oxygenation State and Intracellular pH of Erythrocytes by Inositol-Trispyrophosphate Investigated by P NMR Study of 2,3-DPG.
J Cell Mol Med
January 2025
Centre for Molecular Biophysics, UPR CNRS 4301, Orleans, France.
The hypoxic microenvironment is crucial for tumour cell growth and invasiveness. Tumour tissue results from adaptation to reduced oxygen availability. Hypoxia first activates pro-angiogenic signals for alleviation.
View Article and Find Full Text PDFAssessing the kinetics of oxygen-unloading from red cells using FlowScore, a flow-cytometric proxy of the functional quality of blood.
EBioMedicine
January 2025
Department of Physiology, Anatomy & Genetics, University of Oxford, Oxford, UK. Electronic address:
Background: Metrics evaluating the functional quality of red blood cells (RBCs) must consider their role in oxygen delivery. Whereas oxygen-carrying capacity is routinely reported using haemoglobin assays, the rate of oxygen exchange is not measured, yet also important for tissue oxygenation. Since oxygen-unloading depends on the diffusion pathlength inside RBCs, cell geometry offers a plausible surrogate.
View Article and Find Full Text PDFFT-4202, a selective pyruvate kinase R activator for sickle cell disease.
Exp Hematol
January 2025
Forma Therapeutics, Inc., Watertown, MA.
Anemia in patients with sickle cell disease (SCD) increases 2,3-diphosphoglycerate (2,3-DPG), decreasing hemoglobin-oxygen (HbO) affinity to improve oxygen offloading and promote hemoglobin polymerization (sickling) of red blood cells (RBCs). We report the discovery of FT-4202, an investigational, selective pyruvate kinase type-R (PKR) activator with a multimodal mechanism of action and potential to increase ATP and decrease 2,3-DPG, resulting in increased HbO affinity, decreased Hb polymerization, and improved RBC health. FT-4202 was identified via structure-enabled lead optimization medicinal chemistry using X-ray crystallography, molecular modeling, and thermal shift assays.
View Article and Find Full Text PDFBeyond hemoglobin: Critical role of 2,3-bisphosphoglycerate mutase in kidney function and injury.
Acta Physiol (Oxf)
January 2025
Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institut für Translationale Physiologie (CCM), Berlin, Germany.
Article Synopsis
- The study explores the role of 2,3-bisphosphoglycerate mutase (BPGM) in the kidney, highlighting its upregulation during acute kidney injury in both mice and humans.
- Using a specialized mouse model, researchers found that BPGM is mainly located in the distal nephron and its knockout led to rapid kidney injury and structural damage after just four days.
- The absence of BPGM disrupts crucial metabolic processes, elevating oxidative stress and inflammation while linking stress responses between different parts of the nephron, underscoring its importance in kidney function.
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