Phosphorylation of calf uterus 17β-estradiol receptor by endogenous Ca2+-stimulated kinase activating the hormone binding of the receptor

A. Migliaccio, S. Lastoria, B. Moncharmont, A. Rotondi, F. Auricchio

Research output: Contribution to journalArticle

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Abstract

Direct evidence is presented that uterus 17β-estradiol receptor is phosphorylated in, vitro by an endogenous kinase. Nuclear phosphatase, cytosol Ca2+-stimulated kinase (the former inactivating and the latter reactivating the hormone binding of the 17β-estradiol receptor) and receptor were purified from calf uterus. 17β-estradiol binding was inactivated by phosphatase, then reactivated by kinase in the presence of [γ-32P] ATP, Ca2+ and calmodulin, and the receptor was examined by various methods. The results of gel electrophoresis in non denaturating and denaturating conditions, and of centrifugation through sucrose gradients of receptor preincubated with monoclonal antibodies showed that the receptor is phosphorylated.

Original languageEnglish
Pages (from-to)1002-1010
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume109
Issue number3
DOIs
Publication statusPublished - Dec 15 1982

Fingerprint

Estradiol Receptors
Phosphorylation
Uterus
Phosphotransferases
Hormones
Phosphoric Monoester Hydrolases
Centrifugation
Calmodulin
Electrophoresis
Cytosol
Sucrose
Estradiol
Adenosine Triphosphate
Gels
Monoclonal Antibodies

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phosphorylation of calf uterus 17β-estradiol receptor by endogenous Ca2+-stimulated kinase activating the hormone binding of the receptor. / Migliaccio, A.; Lastoria, S.; Moncharmont, B.; Rotondi, A.; Auricchio, F.

In: Biochemical and Biophysical Research Communications, Vol. 109, No. 3, 15.12.1982, p. 1002-1010.

Research output: Contribution to journalArticle

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