Abstract
The stimulatory actions of prolactin on RNA and casein synthesis in mouse mammary gland explants were shown to be significantly reduced or abolished by incubation with p-bromophenacyl bromide (BPB) at concentrations of 0.05 mM or greater. Since BPB was shown to be an inhibitor of phospholipase A2 activity, the inhibition of prolactin''s actions by BPB provides further support for the proposal that at least certain of the actions of prolactin in the mammary gland may be initiated by a stimulation of membrane-associated phospholipase A2 activity.

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