Insulin binding sites on the nuclear envelope: potential relationship to mRNA metabolism.
Insulin regulates the growth and metabolism of most tissues. The hormonal potency of insulin results, to a large extent, from its ability to regulate target cells at a variety of subcellular sites. For many years, the effects of insulin on membrane transport, enzyme activity, and protein synthesis have been studied extensively. Less attention, however, was given to how insulin regulates nuclear functions. Recently the presence of specific binding sites for insulin on nuclei and nuclear envelopes have been documented and characterized. These binding sites have biochemical characteristics that are different from insulin binding sites on the plasma membrane. Moreover, direct in vitro effects of insulin on messenger RNA (mRNA) metabolism have recently been reported. These effects include the stimulation of mRNA efflux from intact nuclei, and stimulation of nucleoside triphosphatase activity (NTPase), the enzyme that regulates mRNA efflux. Thus, significant insight is now being gained concerning the action of insulin on the cell nucleus.
D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D004261:DNA Replication / Q000187:drug effects; D003921:Diabetes Mellitus, Experimental / Q000378:metabolism; D007328:Insulin / Q000031:analogs & derivatives / Q000378:metabolism*; D007700:Kinetics; D009685:Nuclear Envelope / Q000378:metabolism*; D043583:Nucleoside-Triphosphatase; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D011384:Proinsulin / Q000378:metabolism; D012313:RNA / Q000096:biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*
D007328:Insulin; D012333:RNA, Messenger; C024339:insulin, desoctapeptide-; D012313:RNA; D011384:Proinsulin; D010744:Phosphoric Monoester Hydrolases; D043583:Nucleoside-Triphosphatase