Effect of dexamethasone on nucleolar casein kinase II activity and phosphorylation of nucleolin in lymphosarcoma P1798 cells

Noriaki Suzuki, Toshikazu Suzuki, Aoi Uchida, E Aubrey Thompson, Toichiro Hosoya

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Ribosomal RNA (rRNA) synthesis in murine P1798 lymphosarcoma cells is reversibly inhibited by glucocorticoids. The effects of dexamethasone upon nucleolin phosphorylation and upon the amount and activity of casein kinase II have been examined. P1798 cells were exposed to 0.1 μM dexamethasone for 36 h. Cells were labeled in vivo with [32P]orthophosphate followed by immunoprecipitation with anti-nucleolin antibody. Nucleolin phosphorylation was reduced by 60% in dexamethasone-treated cells. Nucleoli were isolated and labeled with [γ-32P]ATP in vitro. Nucleolin protein was reduced to 40% of control in nuclei from dexamethasone-treated cells. Nucleolin phosphorylation was reduced to 20% of control. Nucleolar casein kinase II activity and protein were also reduced (30-55% and 35-50% of control, respectively) by treatment with dexamethasone. Cycloheximide (10 μg/ml for 3 h) reduced the amount and activity of casein kinase II, but did not cause a decrease in nucleolin protein. These observations are discussed relative to the hypothesis that glucocorticoids regulate the amount or activity of proteins of short biological half-life that are involved in the regulation of rRNA synthesis.

Original languageEnglish (US)
Pages (from-to)305-312
Number of pages8
JournalJournal of Steroid Biochemistry and Molecular Biology
Volume42
Issue number3-4
DOIs
StatePublished - 1992
Externally publishedYes

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Casein Kinase II
Phosphorylation
Non-Hodgkin's Lymphoma
Dexamethasone
Glucocorticoids
Proteins
Cells
Ribosomal RNA
Cycloheximide
Immunoprecipitation
Half-Life
nucleolin
Anti-Idiotypic Antibodies
Adenosine Triphosphate
Phosphates
Antibodies

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

Cite this

Effect of dexamethasone on nucleolar casein kinase II activity and phosphorylation of nucleolin in lymphosarcoma P1798 cells. / Suzuki, Noriaki; Suzuki, Toshikazu; Uchida, Aoi; Thompson, E Aubrey; Hosoya, Toichiro.

In: Journal of Steroid Biochemistry and Molecular Biology, Vol. 42, No. 3-4, 1992, p. 305-312.

Research output: Contribution to journalArticle

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AU - Suzuki, Toshikazu

AU - Uchida, Aoi

AU - Thompson, E Aubrey

AU - Hosoya, Toichiro

PY - 1992

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AB - Ribosomal RNA (rRNA) synthesis in murine P1798 lymphosarcoma cells is reversibly inhibited by glucocorticoids. The effects of dexamethasone upon nucleolin phosphorylation and upon the amount and activity of casein kinase II have been examined. P1798 cells were exposed to 0.1 μM dexamethasone for 36 h. Cells were labeled in vivo with [32P]orthophosphate followed by immunoprecipitation with anti-nucleolin antibody. Nucleolin phosphorylation was reduced by 60% in dexamethasone-treated cells. Nucleoli were isolated and labeled with [γ-32P]ATP in vitro. Nucleolin protein was reduced to 40% of control in nuclei from dexamethasone-treated cells. Nucleolin phosphorylation was reduced to 20% of control. Nucleolar casein kinase II activity and protein were also reduced (30-55% and 35-50% of control, respectively) by treatment with dexamethasone. Cycloheximide (10 μg/ml for 3 h) reduced the amount and activity of casein kinase II, but did not cause a decrease in nucleolin protein. These observations are discussed relative to the hypothesis that glucocorticoids regulate the amount or activity of proteins of short biological half-life that are involved in the regulation of rRNA synthesis.

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