Estradiol-stimulated nuclear ribonucleoprotein transport in the rat uterus: a molecular basis.
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.
Thampan
R V
RV
School of Life Sciences, University of Hyderabad, India.
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D002467:Cell Nucleus / Q000378:metabolism; D004958:Estradiol / Q000494:pharmacology*; D005260:Female; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D012261:Ribonucleoproteins / Q000378:metabolism*; D014599:Uterus / Q000166:cytology* / Q000187:drug effects
D012261:Ribonucleoproteins; D004958:Estradiol; D000255:Adenosine Triphosphate; D011494:Protein Kinases