Abstract

Abstract Histone deacetylases (HDACs) are a group of enzymes that catalyze removal of acetyl groups from a ε-N-acetyl lysine amino acid on histones. A number of non-histone proteins are also known to be deacetylated by these enzymes. Hence, these proteins are now also being referred to as lysine deacetylases (KDAC). Based on function and DNA sequence similarity, HDAC proteins are classified in four groups; Class I, Class II, Class III and Class IV HDACs. HDAC11, the only member of Class IV HDAC, shows a DNA sequence similarity with both Class I and Class II HDACs. In general, HDAC proteins are known as transcriptional inhibitors and are involved in cellular growth, development and apoptosis. Unlike other HDACs, function of HDAC11 is not widely studied. Although this enzyme is reported as a transcriptional inhibitor, little is known about its role in connection to cell division cycle or cell density. Analysis of our microarray data shows that Balb/C 3T3 cells, stimulated with PDGF and plasma, contain considerably reduced level of HDAC11 transcript compared to that in the quiescent Balb/C 3T3 cells. The protein level under similar conditions mimics the pattern of transcript level. These results indicate that as cells leave quiescence state HDAC11 expression is down-regulated or may be reduction of HDAC11 expression causes quiescent cells to enter cell cycle. It may also be possible that cell-cell contact inhibition positively regulates HDAC11 expression and as the cell grows in presence of PDGF and plasma, the contact inhibitory property is lost which in turn causes the reduction of the protein expression. Further work is in progress to elucidate the role of HDAC11 with respect to cell cycle regulation or cell density. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 2953. doi:10.1158/1538-7445.AM2011-2953

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