Butyrate activates the WAF1/Cip1 gene promoter through Sp1 sites in a p53-negative human colon cancer cell line - PubMed (original) (raw)

. 1997 Aug 29;272(35):22199-206.

doi: 10.1074/jbc.272.35.22199.

T Mizuno, Y Sowa, T Orita, T Yoshino, Y Okuyama, T Fujita, N Ohtani-Fujita, Y Matsukawa, T Tokino, H Yamagishi, T Oka, H Nomura, T Sakai

Affiliations

• PMID: 9268365
• DOI: 10.1074/jbc.272.35.22199

Free article

Butyrate activates the WAF1/Cip1 gene promoter through Sp1 sites in a p53-negative human colon cancer cell line

K Nakano et al. J Biol Chem. 1997.

Free article

Abstract

Butyrate is a well known colonic luminal short chain fatty acid, which arrests cell growth and induces differentiation in various cell types. We examined the effect of butyrate on the expression of WAF1/Cip1, a potent inhibitor of cyclin-dependent kinases, and its relation to growth arrest in a p53-mutated human colon cancer cell line WiDr. Five millimolar butyrate completely inhibited the growth of WiDr and caused G1-phase arrest. WAF1/Cip1 mRNA was rapidly induced within 3 h by treatment with 5.0 mM butyrate, and drastic WAF1/Cip1 protein induction was detected. Using several mutant WAF1/Cip1 promoter fragments, we found that the butyrate-responsive elements are two Sp1 sites at -82 and -69 relative to the transcription start site. We also found that a TATA element at -46 and two overlapping consensus Sp1 sites at -60 and -55 are essential for the basal promoter activity of WAF1/Cip1. These findings suggest that butyrate arrests the growth of WiDr by activating the WAF1/Cip1 promoter through specific Sp1 sites in a p53-independent fashion.

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