Distribution of actin, myosin, and spectrin during enucleation in erythroid cells of hamster embryo.

Yolk-sac derived erythroblasts undergo semi-synchronous maturation and some of them enucleate in the peripheral blood of embryos. We have studied the assembly and distribution of actin, myosin, and spectrin during the enucleation of Syrian hamster embryonic erythroblasts. At day 11 of the gestation, that is just before the start of the enucleation, formation of a cytoskeletal structure consisted chiefly of particulate associations of F(filamentous)-actin was detected by the staining with rhodamine-labeled phalloidin. Stress-fiber-like structures were not observed in each differentiation stage after day 10. Distribution of myosin, actin, and spectrin was studied immunocytochemically to know the role of them in the enucleation of erythroid cells that starts at late day 11 or early day 12 in the gestation. The enucleation is preceded by the approach and the subsequent attachment of nucleus to the plasma membrane. At that time, actin and myosin are present in the cytoplasmic and cortical region of the cells. From the time when the extrusion of nucleus has started, condensation of actin and myosin was observed at the cell cortex area surrounding the extruding nucleus, and a contractile ring-like structure was infrequently observed. Spectrin was observed in the cortical region of the cells, and the change of the localization of spectrin was not observed throughout the terminal differentiation process (days 10-12) of the embryonic erythroid cells. The results show the possible involvement of a myosin-actin contractile system that appears around the extruding nucleus within the mechanism of erythroid enucleation.