Early Action of Prolactin on Ornithine Decarboxylase Activity Is Not Essential for the Subsequent Actions of Prolactin on Casein and Lipid Biosynthesis

Abstract

The actions of prolactin (PRL) on casein and lipid biosynthesis in cultured mouse mammary gland explants require the ongoing synthesis of the polyamines. This is supported by the fact that (MGBG) methylglyoxal bis(guanylhydrazone), a drug that inhibits the conversion of putrescine to spermidine, abolishes the effects of PRL on casein and lipid biosynthesis; the inhibitory effects of MGBG are reversed by the addition of spermidine to the culture medium. alpha-Difluoro methyl ornithine (DFMO), an irreversible inhibitor of ornithine decarboxylase activity, reduces the PRL-stimulated ornithine decarboxylase (ODC) activity by more than 95%, and yet does not suppress the effects of PRL on RNA, casein or lipid synthesis. These observations suggest that PRL's early action on ODC activity is not essential for the subsequent actions of PRL on the synthesis of certain of the components of milk.