Blockade of prolactin action by an antiserum to its receptors.
A guinea pig antiserum to prolactin receptors selectively inhibited the binding of [125I] prolactin to its membrane receptors as well as prolactin-mediated incorporation of [3H] leucine into casein and transport of [14C] aminoisobutyric acid, but was without effect on the binding of [125I] insulin and insulin-mediated events in explants of rabbit mammary glands maintained in culture. These findings provide direct evidence for an obligatory functional role of a membrane receptor in mediating the action of a polypeptide hormone.
D000621:Aminoisobutyric Acids / Q000378:metabolism; D000818:Animals; D000906:Antibodies; D000937:Antigen-Antibody Reactions; D002364:Caseins / Q000096:biosynthesis; D005947:Glucose / Q000378:metabolism; D007328:Insulin / Q000494:pharmacology; D008321:Mammary Glands, Animal / Q000378:metabolism; D009924:Organ Culture Techniques; D011388:Prolactin / Q000276:immunology / Q000378:metabolism* / Q000502:physiology; D011817:Rabbits; D011956:Receptors, Cell Surface
D000621:Aminoisobutyric Acids; D000906:Antibodies; D002364:Caseins; D007328:Insulin; D011956:Receptors, Cell Surface; D011388:Prolactin; D005947:Glucose