Cation-dependent prolactin activation of guanylate cyclase.
Prolactin enhanced guanylate cyclase [E.C.4.6.1.2] two- to threefold in ovary, testis, mammary gland, liver and kidney. Dose response relationships revealed that maximal activation of this enzyme was at a concentration of one nanomolar and that increasing prolactin's concentration to the millimolar range caused no further increase in activity. There was an absolute cation requirement for prolactin's enhancement of guanylate cyclase. Calcium or manganese allowed prolactin to increase guanylate cyclase activity. Greater enhancement of this enzyme's activity by prolactin was observed when manganese was the co-factor. The data in this investigation suggest that guanylate cyclase may play a role in the mechanism of action of prolactin.
D000818:Animals; D002412:Cations; D006152:Cyclic GMP / Q000032:analysis; D004789:Enzyme Activation; D005260:Female; D006162:Guanylate Cyclase / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008297:Male; D008321:Mammary Glands, Animal / Q000201:enzymology; D010053:Ovary / Q000201:enzymology; D011388:Prolactin / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013737:Testis / Q000201:enzymology
D002412:Cations; D011388:Prolactin; D006162:Guanylate Cyclase; D006152:Cyclic GMP