Evolution of the Vertebrate Erythrocytes Membrane Skeleton Protein Affinity is Caused by Protein Kinase C

Abstract: To study the relationship between the vertebrate erythrocytes membrane skeleton protein affinity and deformability of RBCs. Atomic force microscope (AFM) was applied to detect the viscoelasticity and fluorescence intensity was observed by indirect immunofluorescence labeling of these vertebrate erythrocytes (human， chicken， frog， fish) that were treated with Phorbol-12-myrisrate-13-acetate (PMA)， a PKC activator， for 0 minutes， 2 hours， respectively. Bioinformatics softwares were used to compare the RBCs protein 4.1 and α-spectrin sequence. The measured Young’s modulus of erythrocytes (human， chicken， frog， fish) increased significantly after PMA treatment 2 hours and were (0.388±0.035) kPa， (0.219±0.022) kPa， (0.191±0.036) kPa and (0.141±0.007) kPa respectively. Fluorescence intensity increased significantly after PMA treatment 2 hours because chicken， frog， fish erythrocytes protein 4.1 have the phosphorylation serine sites corresponding to the number 312 of human erythrocytes protein 4.1 and PKC phosphorylate chicken， frog， fish erythrocytes. Young’s modulus increased is consistent with biological evolution because of PKC. This trend provides a basis interpretation for the acquiring deformability of RBCs from biological evolution and molecular mechanism.

CSTR: 32200.14.cjcb.2013.04.0010