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Prehemolytic impact of phenothiazine drugs on the attachment of spectrin network in red blood cells.
Folia Med (Plovdiv)
October 2023
Trakia University, Stara Zagora, Bulgaria.
Chlorpromazine, thioridazine, and trifluoperazine are phenothiazine drugs that cause colloid-osmotic hemolysis of human erythrocytes by unknown mechanism. To clarify this mechanism, the impact of these drugs on the βsp (1.4 MHz) and γ1sp (9 MHz) dielectric relaxations was investigated.
View Article and Find Full Text PDFMembrane skeleton hyperstability due to a novel alternatively spliced 4.1R can account for ellipsoidal camelid red cells with decreased deformability.
J Biol Chem
February 2023
Laboratory of Molecular Medicine, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan. Electronic address:
The red blood cells (RBCs) of vertebrates have evolved into two basic shapes, with nucleated nonmammalian RBCs having a biconvex ellipsoidal shape and anuclear mammalian RBCs having a biconcave disk shape. In contrast, camelid RBCs are flat ellipsoids with reduced membrane deformability, suggesting altered membrane skeletal organization. However, the mechanisms responsible for their elliptocytic shape and reduced deformability have not been determined.
View Article and Find Full Text PDFArchitecture of the human erythrocyte ankyrin-1 complex.
Nat Struct Mol Biol
July 2022
Department of Anesthesiology, Columbia University Irving Medical Center, New York, NY, USA.
The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.
View Article and Find Full Text PDFMultimodal imaging reveals membrane skeleton reorganisation during reticulocyte maturation and differences in dimple and rim regions of mature erythrocytes.
J Struct Biol X
December 2021
Division of Infectious Diseases and Immune Defence, The Walter & Eliza Hall Institute, Melbourne, Australia.
Article Synopsis
- - The study investigates the properties of red blood cells (RBCs), focusing on how they can change shape as they move through blood vessels, which is supported by a protein network made of spectrin and actin.
- - Microscopy techniques revealed that as RBCs mature from reticulocytes, they lose up to 30% of their surface area while increasing the density of their spectrin-actin network by around 20%.
- - Differences in the structure of the mature RBC membrane were noted, with the rim area having 1.5% more junctional complexes and a 2% greater density of band 4.1 compared to the dimple region.
Inhibition of Band 3 tyrosine phosphorylation: a new mechanism for treatment of sickle cell disease.
Br J Haematol
August 2020
Department of Chemistry, Purdue University, West Lafayette, IN, USA.
Many hypotheses have been proposed to explain how a glutamate to valine substitution in sickle haemoglobin (HbS) can cause sickle cell disease (SCD). We propose and document a new mechanism in which elevated tyrosine phosphorylation of Band 3 initiates sequelae that cause vaso-occlusion and the symptoms of SCD. In this mechanism, denaturation of HbS and release of heme generate intracellular oxidants which cause inhibition of erythrocyte tyrosine phosphatases, thus permitting constitutive tyrosine phosphorylation of Band 3.
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