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Down-regulation of protein kinase CKII activity by sodium butyrate (Articolo in rivista)

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Down-regulation of protein kinase CKII activity by sodium butyrate (Articolo in rivista) (literal)

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Russo, G.L., Della Pietra, V., Mercurio, C., Della Ragione, F., Marshak, D.R., Oliva, A., and Zappia, V. (1997)
Down-regulation of protein kinase CKII activity by sodium butyrate
in Biochemical and biophysical research communications (Print); Elsevier Inc., San Diego (Stati Uniti d'America)
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Russo, G.L., Della Pietra, V., Mercurio, C., Della Ragione, F., Marshak, D.R., Oliva, A., and Zappia, V. (literal)

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I.S.A. Inst. of Food Sci. and T., National Research Council, Avellino, Italy; Inst. of Biochem. of Macromolecules, Second University of Naples, Naples, Italy; Osiris Therapeutics Inc., Baltimore, MA 21231, United States; Ist. Scienze Dell'AlimentazioneCNR, via Roma 52 A-C, 83100, Avellino, Italy; European Institute of Oncology, 20141, Milan, Italy (literal)

Titolo

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. (literal)

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