Sp1 acetylation is associated with loss of DNA binding at promoters associated with cell cycle arrest and cell death in ... View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2010-12

AUTHORS

Jennifer S Waby, Haridasan Chirakkal, ChenWei Yu, Gareth J Griffiths, Roderick SP Benson, Colin D Bingle, Bernard M Corfe

ABSTRACT

Butyrate, a known histone deacetylase inhibitor (HDACi) and product of fibre fermentation, is postulated to mediate the protective effect of dietary fibre against colon cancer. The transcription factor Sp1 is a target of acetylation and is known to be associated with class I HDACs, including HDAC1. Sp1 is a ubiquitous transcription factor and Sp1-regulated genes include those involved in cell cycle regulation, apoptosis and lipogenesis: all major pathways in cancer development. The only known acetylated residue of Sp1 is lysine703 which resides in the DNA binding domain. Here we show that acetylated Sp1 loses p21- and bak-promoter -binding function in vitro. Furthermore treatment with a panel of HDAC inhibitors showed clustering of activities for a subset of inhibitors, causing G2 cell cycle arrest, Sp1 acetylation, p21 and Bak over-expression, all with very similar EC50 concentrations. These HDACi activities were not distributed according to the molecular class of compound. In order to mimic loss of binding, an siRNA strategy was used to reduce Sp1 expression. This resulted in altered expression of multiple elements of the p53/p21 pathway. Taken together our data suggest a mechanistic model for the chemopreventive actions of butyrate in colon epithelial cells, and provide new insight into the differential activities some classes of HDAC inhibitors. More... »

PAGES

275

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1476-4598-9-275

DOI

http://dx.doi.org/10.1186/1476-4598-9-275

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022150761

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20950428


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