Phosphorylation of the chicken progesterone receptor

Larry Denner, William E. Bingman, Geoffrey L. Greene, Nancy L. Weigel

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

We have examined the phosphorylation of the chicken progesterone receptor in tissue slices and in vitro. The receptor is phosphorylated in tissue slices and this phosphorylation is stimulated by progesterone. As others have reported, partially purified receptor preparations contain a kinase activity which phosphorylates histones and receptor. We have shown that this activity can be separated from the receptor. The receptor is a substrate for several kinases, including the catalytic subunit of the cAMP-dependent protein kinase and PPdPK, a polypeptide-dependent protein kinase. Phosphorylation by the cAMP-dependent protein kinase results in an apparent increase in the molecular weight of the receptor when the receptor is analyzed by SDS-PAGE. These results are consistent with apparent changes in molecular weight observed for rabbit and human progesterone receptor upon treatment of tissues or cells with hormone.

Original languageEnglish (US)
Pages (from-to)235-243
Number of pages9
JournalJournal of Steroid Biochemistry
Volume27
Issue number1-3
DOIs
StatePublished - 1987
Externally publishedYes

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Phosphorylation
Progesterone Receptors
Chickens
Tissue
Cyclic AMP-Dependent Protein Kinases
Phosphotransferases
Molecular Weight
Molecular weight
Histones
Protein Kinases
Progesterone
Polyacrylamide Gel Electrophoresis
Catalytic Domain
Hormones
Rabbits
Peptides
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

Cite this

Phosphorylation of the chicken progesterone receptor. / Denner, Larry; Bingman, William E.; Greene, Geoffrey L.; Weigel, Nancy L.

In: Journal of Steroid Biochemistry, Vol. 27, No. 1-3, 1987, p. 235-243.

Research output: Contribution to journalArticle

Denner, Larry ; Bingman, William E. ; Greene, Geoffrey L. ; Weigel, Nancy L. / Phosphorylation of the chicken progesterone receptor. In: Journal of Steroid Biochemistry. 1987 ; Vol. 27, No. 1-3. pp. 235-243.
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