Estradiol-stimulated nuclear ribonucleoprotein transport in the rat uterus: a molecular basis.

Abstract

The present investigation probes the intranuclear molecular changes that serve to link the nuclear binding of estradiol with the hormone-stimulated ribonucleoprotein (RNP) transport in the rat uterus. Within 2 min of in vitro exposure of isolated uterine nuclei to 10 nM 17 beta-estradiol a Mg2+-dependent nuclear ATPase becomes activated and reaches its peak activity. This is immediately followed by a phase of ATP resynthesis. This newly synthesized ATP serves as the substrate for the nuclear protein kinases. Cyclic AMP inhibits this ATP resynthesis and, as a consequence, prevents the estradiol-stimulated nuclear protein kinase activity and the exit of the RNP-estradiol complex from the nuclei. cGMP is stimulatory to the estradiol-mediated nuclear ribonucleoprotein transport.