Segmental flexibility of spectrin reflects erythrocyte membrane deformability.

The frequency-dependent contribution of spectrin, the main cytoskeletal protein of red blood cell (RBC) membrane, to the complex admittance and capacitance of suspended RBCs have revealed two dielectric relaxations, βsp (1.4 MHz) and γ1sp (7 MHz). The strength of these relaxations was related to the ability of RBC membrane to deform. In this study the two relaxations were inhibited by N-ethylmaleimide (up to 5 mM), known to impair the RBC deformability, and the degree of inhibition, i.e., the number of accessible SH-groups on spectrin, depended on the deformation of RBC membrane. Dithiothreitol (up to 5 mM), which does not affect RBC deformability, did not affect the above dielectric relaxations in line with the absence of S-S groups on spectrin. Phenylhydrazine (up to 3 mM) and hydrogen hydroperoxide (up to 450 μM) are known to denature the haemoglobin of RBCs producing nanoparticles (globins) that bind to spectrin turning the RBC membrane rigid. At the same concentrations they were shown to inhibit progressively the two relaxations on spectrin. The results are in line with the involvement of some globin-sized segments of spectrin in the dielectric activity of spectrin and in the ability of RBC plasma membrane to deform.