Down-regulation of protein kinase CKII activity by sodium butyrate

Gian Luigi Russo, Valentina Della Pietra, Ciro Mercurio, Fulvio Della Ragione, Daniel R. Marshak, Adriana Oliva, Vincenzo Zappia

Research output: Contribution to journalArticle

Abstract

Butyrate, a dietary fiber derivative, is a well-known differentiating agent in cultured cell lines. In addition, its antineoplastic activity toward colon-rectum cancers has been documented both in vivo and in vitro. Despite the large amount of information on the potential clinical efficacy of butyrate, its mechanism of action at the molecular level has only been partially investigated. Here, we show that serine/threonine protein kinase CKII is a target of butyrate activity. In the human adenocarcinoma cell line, HT29, treated with 2 mM sodium butyrate, CKII activity decreases 50% at 24 and 48 hours after drug addition. The enzyme downregulation is not due to changes in protein amount since the levels of the different CKII subunits remain constant during butyrate treatment. The data reported provide the first evidence that CKII down-regulation is involved in the signal transduction pathway started by butyrate.

Original languageEnglish
Pages (from-to)673-677
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume233
Issue number3
DOIs
Publication statusPublished - Apr 28 1997

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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  • Cite this

    Russo, G. L., Pietra, V. D., Mercurio, C., Ragione, F. D., Marshak, D. R., Oliva, A., & Zappia, V. (1997). Down-regulation of protein kinase CKII activity by sodium butyrate. Biochemical and Biophysical Research Communications, 233(3), 673-677. https://doi.org/10.1006/bbrc.1997.6515