DNase-I-dependent dissociation of erythrocyte cytoskeletons.

Abstract

The human erythrocyte contains a complex of peripheral membrane proteins which forms an extensive network or cytoskeleton on the cytoplasmic membrane surface. When erythrocyte cytoskeletons were treated with DNase I, the cytoskeletons dissociated and erythrocyte actin was solubilized. The dissociation of the cytoskeletons by DNase I paralleled the disruption of actin filaments in vitro by DNase I and was blocked by the addition of actin to the DNase I. Large protein complexes remained after DNase I disrupts the cytoskeletons, but these complexes were no longer visible in the light microscope nor sedimentable and were selectively depleted with respect to actin. DNase I apparently binds to and solubilization actin, which serves as a structural link between protein complexes in the erythrocyte cytoskeleton.