Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases

https://doi.org/10.1016/0006-291X(87)90799-6Get rights and content

Abstract

Progesterone receptors were immunoprecipitated with monoclonal antibodies KD68 from lysates of human breast carcinoma T47D cells labelled to steady state specific activity with 32Pi. The 120 kDa 32P-labelled progesterone receptor band was resolved by polyacrylamide gel electrophoresis and identified by autoradiography. Phosphoamino acid analysis revealed serine phosphorylation, but no threonine or tyrosine phosphorylation. Treatment of the 32Pi-labelled cells with EGF, TPA or dibutyryl cAMP had no significant quantitative effect on progesterone receptor phosphorylation, though the EGF receptor and the cAMP-dependent protein kinases have been reported to catalyze phosphorylation of purified avian progesterone receptor preparations in cell free systems. Progesterone receptor phosphorylation on serine residues was increased by 2-fold in cells treated with 10 nM progesterone; EGF had no effect on progesterone-mediated progesterone receptor phosphorylation.

References (18)

  • N.L. Weigel et al.

    Biochem. Biophys. Res. Comm

    (1981)
  • D.D.L. Woo et al.

    J. Biol. Chem

    (1986)
  • T. Hunter et al.

    Cell

    (1981)
  • B.M. Sefton et al.

    Cell

    (1980)
  • J.M. Gershoni et al.

    Anal. Biochem

    (1983)
  • H. Loosfelt et al.

    J. Biol. Chem

    (1984)
  • F. Logeat et al.

    Biochem. Biophys. Res. Comm

    (1985)
  • K.V.S. Rao et al.

    Biochem. Biophys. Res. Comm

    (1987)
  • J.J. Dougherty
There are more references available in the full text version of this article.

Cited by (27)

  • Mechanism of progesterone receptor action in the brain

    2009, Hormones, Brain and Behavior Online
  • Phosphorylation of steroid hormone receptors

    1990, BBA - Molecular Cell Research
View all citing articles on Scopus
View full text