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

1984

1985

Publication Date:
14 March 2008 (online)

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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