Functional significance of histone deacetylase diversity

Khochbin, Saadi; Verdel, André; Lemercier, Claudie; Seigneurin-Berny, Daphné

doi:10.1016/s0959-437x(00)00174-x

Cited by 337 publications

(252 citation statements)

References 48 publications

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“…We therefore speculate that HDAC4 participates, with a HDAC1-dependent co-repressor complex, in p21 WAF1/Cip1 repression. Even if class II HDACs do not seem to participate in class I co-repressor complexes, some reports have shown that HDAC4, HDAC5 and HDAC7 contains class I HDACs, HDAC1, 2 and 3 as well as members of NuRD and Sin3 complexes Kao et al, 2000;Khochbin et al, 2001). Silencing of HDAC1 in addition to HDAC4 did not synergistically increase p21 WAF1/Cip1 expression (Supplementary Figure S2A).…”

Section: Discussionmentioning

confidence: 94%

HDAC4 represses p21WAF1/Cip1 expression in human cancer cells through a Sp1-dependent, p53-independent mechanism

et al. 2008

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Cancer cells have complex, unique characteristics that distinguish them from normal cells, such as increased growth rates and evasion of anti-proliferative signals. Global inhibition of class I and II histone deacetylases (HDACs) stops cancer cell proliferation in vitro and has proven effective against cancer in clinical trials, at least in part, through transcriptional reactivation of the p21 WAF1/Cip1 gene. The HDACs that regulate p21 WAF1/Cip1 are not fully identified. Using small interfering RNAs, we found that HDAC4 participates in the repression of p21 WAF1/Cip1 through Sp1/Sp3-, but not p53-binding sites. HDAC4 interacts with Sp1, binds and reduces histone H3 acetylation at the Sp1/Sp3 binding site-rich p21 WAF1/Cip1 proximal promoter, suggesting a key role for Sp1 in HDAC4-mediated repression of p21 WAF1/Cip1 . Induction of p21 WAF1/Cip1 mediated by silencing of HDAC4 arrested cancer cell growth in vitro and inhibited tumor growth in an in vivo human glioblastoma model. Thus, HDAC4 could be a useful target for new anti-cancer therapies based on selective inhibition of specific HDACs.

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Section: Discussionmentioning

confidence: 94%

HDAC4 represses p21WAF1/Cip1 expression in human cancer cells through a Sp1-dependent, p53-independent mechanism

et al. 2008

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“…Covalent acetylation of specific lysine residues on histone tails by histone acetyltransferases (HATs) promotes chromatin relaxation and transcription, whereas deacetylation by histone deacetylases (HDACs) in a reverse reaction results in chromatin condensation and silencing of gene transcription [10][11][12] . Some chromatin remodeling proteins that share a highly conserved SET domain, originally described in the proteins su(var)-39, enhancer of zeste and trithorax, can methylate unacetylated lysine residues on histone tails, resulting in more permanent silencing of transcription [13][14] or, in some cases, activation of transcription 15 .…”

Section: Introductionmentioning

confidence: 99%

Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis

et al. 2002

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“…In particular, HDAC3 can be found in the nucleus and in the cytoplasm, whereas all other Class I HDAC are strictly nuclear proteins. 25,26 Additionally, unlike HDAC1 and HDAC2, the disruption of HDAC3 gene, which is homologous to yeast protein RPD3, 27 makes DT40 chicken cells non-viable, 25 suggesting specific and non-redundant function of this gene product. Another interesting feature of the human HDAC3 was reported recently by Zhang et al,28 who demonstrated that HDAC3 is necessary and sufficient for silencing the growth-differentiation factor 11 (Gdf11) gene, a TGF-b family member that inhibits cell proliferation.…”

Section: Discussionmentioning

confidence: 99%

Antibody response to a non‐conserved C‐terminal part of human histone deacetylase 3 in colon cancer patients

Shebzukhov

Koroleva

Khlgatian

et al. 2005

Intl Journal of Cancer

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Antibodies to cancer antigens can often be detected in the sera of patients, although the mechanism of the underlying humoral immune response is poorly understood. Using immunoscreening of tumor-derived cDNA expression libraries (SEREX), we identified human histone deacetylase 3 (HDAC3) as serologically defined antigen in colon cancer. Closely related HDAC1 and HDAC2 do not elicit humoral response in colon cancer patients. We show that the C-terminal region of HDAC3 protein lacking the homology to other Class I HDAC contains at least 3 distinct B-cell epitopes that are recognized by the serum antibodies. HDAC3 in combination with other SEREX antigens may become a useful molecular biomarker with diagnostic or prognostic value for a subset of colon cancer patients. (Supplementary material for this article can be found on the International Journal of Cancer website at

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Functional significance of histone deacetylase diversity

Cited by 337 publications

References 48 publications

HDAC4 represses p21WAF1/Cip1 expression in human cancer cells through a Sp1-dependent, p53-independent mechanism

HDAC4 represses p21WAF1/Cip1 expression in human cancer cells through a Sp1-dependent, p53-independent mechanism

Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis

Antibody response to a non‐conserved C‐terminal part of human histone deacetylase 3 in colon cancer patients

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