Prolactin Actions on Casein and Lipid Biosynthesis in Mouse and Rabbit Mammary Gland Explants are Abolished by p-Bromphenacyl Bromide and Quinacrine, Phospholipase A2 Inhibitors

J. A. Rillema; R. N. Etindi; C. M. Cameron

doi:10.1055/s-2007-1012403

Hormone and Metabolic Research, Table of Contents

Horm Metab Res 1986; 18(10): 672-674
DOI: 10.1055/s-2007-1012403

ORIGINALS

Basic
© Georg Thieme Verlag, Stuttgart · New York

Prolactin Actions on Casein and Lipid Biosynthesis in Mouse and Rabbit Mammary Gland Explants are Abolished by p-Bromphenacyl Bromide and Quinacrine, Phospholipase A₂ Inhibitors

J. A. Rillema, R. N. Etindi, C. M. Cameron

Wayne State University, School of Medicine, Department of Physiology, Detroit, Michigan, U.S.A.

Abstract

PDF Download

Summary

p-Bromphenacyl bromide (BPB) at concentrations of 50 μM and above and quinacrine (50 μM) abolished the actions of prolactin (PRL) on casein and lipid biosynthesis in cultured mouse mammary gland explants. In cultured rabbit mammary gland explants, 100 μM BPB or quinacrine abolished the PRL stimulation of casein synthesis, while 50 μM BPB or 250 μM quinacrine abolished the PRL stimulation of lipid biosynthesis. Since BPB and quinacrine are known to inhibit the enzyme phospholipase A₂ (PLA₂), it is possible that ongoing PLA₂ activity is essential for prolactin to express its actions on at least certain lactogenic processes.

Key-Words

Prolactin - Phospholipase A ₂ - Casein Synthesis - Lipid Synthesis - p-Bromphenacyl Bromide - Quinacrine

PDF (316 kb)