Alteration Young’s moduli by protein 4.1 phosphorylation play a potential role in the deformability development of vertebrate erythrocytes

The mechanical properties of stored red blood cells measured by a convenient microfluidic approach combining with mathematic model

“…43 Disrupting the network via protein 4.1R phosphorylation to alter its spectrin-actin binding affinity results in a significant increase in the Young's modulus. 41 During the first days of storage, the oxidation of cytoskeletal proteins 4.2 and 4.1, spectrin, and band 3 is observed. These are followed by breakdown of actin, GAPDH, band 4.9, and ankyrin, as well as the cross-linking of spectrin.…”

“…The mechanical properties of RBCs depend on their cytoskeletal protein networks. 41 The RBC cytoskeleton network is predominantly composed of spectrin tetramers, actin, and protein 4.1R, along with adaptor proteins, 36 which be attached to membrane by Band 3 via ankyrin. 42 The cytoskeleton network plays a crucial role in maintaining the normal morphology of the RBC, which allows RBCs to deform and pass through narrow capillaries.…”