Dissociation of cells from sea urchin embryos alters the synthesis of actins and other proteins.
The effects of altered cellular microenvironments on patterns of protein synthesis at various periods during sea urchin development were quantitated by comparing the relative incorporation of [35S]methionine into selected polypeptides of intact embryos and cells dissociated from them. The effects of increasing times of reassociation were also determined. Quantitative, but not qualitative, differences in incorporation were noted. Actins, as well as heterogeneous acidic polypeptides with an Mr of about 80 kDa, showed increased incorporation in dissociated cells labeled at the time control embryos were recently hatched blastulae. Labeling of another acidic group of polypeptides with an Mr of about 100 kDa was decreased. Possible mechanisms regulating these shifts in incorporation were investigated by the use of inhibitors. The dissociation-triggered changes were insensitive to actinomycin D, cordycepin, dibutyryl cAMP, 3-isobutyl-1-methylxanthine, and trifluoperazine; however, the latter two stimulated incorporation into some polypeptides in intact blastulae. Age-dependent shifts in incorporation were also detected in both intact embryos and dissociated/reassociating cells.