Protein kinase translocation as an early event in the hormonal control of uterine contraction.
beta-Adrenergic stimulation with isoproterenol inhibits contractility, increases cyclic adenosine monophosphate (AMP) concentration, decreases the concentration of unsaturated cyclic AMP receptor sites, and increases cyclic AMP-independent kinase in the uterus of ovariectomized rats. The total soluble kinase activity is reduced. The protein kinase activity lost from the cytosol was translocated to the microsomal fraction mostly in a cyclic AMP-independent form, suggesting a particulate substrate for the activated enzyme.
D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D002369:Castration; D002458:Cell Fractionation; D000242:Cyclic AMP / Q000378:metabolism* / Q000494:pharmacology; D003600:Cytosol / Q000378:metabolism; D003864:Depression, Chemical; D004789:Enzyme Activation; D005260:Female; D066298:In Vitro Techniques; D007545:Isoproterenol / Q000494:pharmacology*; D008861:Microsomes / Q000378:metabolism; D009119:Muscle Contraction / Q000187:drug effects*; D010761:Phosphorus Radioisotopes; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D013268:Stimulation, Chemical; D014599:Uterus / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*
D010761:Phosphorus Radioisotopes; D000242:Cyclic AMP; D011494:Protein Kinases; D007545:Isoproterenol