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Gene Review

HDAC3  -  histone deacetylase 3

Gallus gallus

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Disease relevance of HDAC3


High impact information on HDAC3

  • The chromosomal beta H-globin gene has two 5'-flanking DNAseI hypersensitive sites which bracket two sequences (H and H') bound by erythrocyte and HD3 nuclear protein in vitro [2].
  • The erythroid precursor cell line HD3 has beta A-globin gene sites B and B' binding activities, but binding to site A is detected only after the HD3 cells are induced to differentiate [2].
  • It binds to CAF-1p48, HDAC-1 and 2, but not to CAF-1p60, p46 polypeptide and HDAC-3 [3].
  • Molecular and biochemical events during differentiation of the HD3 chicken erythroblastic cell line [1].
  • Upon shift to the non-permissive temperature in the presence of inducers (hemin and butyric acid), HD3 cells differentiate to an erythrocyte phenotype and provide a model system for analyzing events associated with this process [1].

Chemical compound and disease context of HDAC3


Biological context of HDAC3

  • Erythrocytic differentiation and glyceraldehyde-3-phosphate dehydrogenase expression are regulated by protein phosphorylation and cAMP in HD3 cells [6].
  • In this review, we describe how HD3 differentiation involves changes in plasma membrane composition, metabolism and gene expression that are orchestrated at different levels of control by multiple signaling modalities [1].
  • Growing HD3 cells have much higher levels of transport than native chicken bone marrow cells and this is associated in part with elevation of glucose transporter (GLUT) mRNAs as a consequence of the expression of the v-erbA and v-erbB oncogenes [7].
  • Two chicken monoclonal antibodies (MAbs), HU/Ch2-7 and HU/Ch6-1, against heterophil Hanganutziu-Deicher (HD) antigens with N-glycolylneuraminic acid (NeuGc) at a terminal carbohydrate were established by cell fusions using chicken B cell lines lacking thymidine kinase and spleen cells from chickens immunized with II3NeuGc alpha-LacCer (HD3) [8].
  • The major HD3 protein-binding activity binds to a site (site V) 200 bp upstream from the 'cap' site but, after further fractionation, a second distinct binding activity is detected to a site (site VIII) which contains both the 'CAAT' and 'SP1-binding' consensus sequences [9].

Anatomical context of HDAC3

  • When nuclear extracts from chicken erythroblasts transformed by an AEV ts-mutant (clone HD3) or from adult chicken erythrocytes were compared, different protein factors were found to interact with these DNA motifs in DNase I footprinting and electrophoretic retardation experiments [10].
  • Both native bone marrow red cells and HD3 cells, when incubated in vitro under conditions where maturation occurs, show substantial losses of GLUT mRNA and GLUT proteins [7].
  • The interaction of nuclear sequence-specific DNA-binding proteins from definitive chicken erythrocytes, thymus and proliferating transformed erythroid precursor (HD3) cells with the 700-base-pair (700-bp) DNA 5'-flanking region of the chicken c-myc gene was investigated by in vitro footprint analysis [9].

Associations of HDAC3 with chemical compounds

  • Together these results suggest that multiple pathways (including serine/threonine phosphorylation, tyrosine phosphorylation and elevated cAMP) are involved in the regulation of erythroblastic differentiation, hemoglobin synthesis, GAD gene expression and GAD activity in HD3 cells [6].
  • Addition of 3-isobutyl-1-methyl-xanthine, an activator of phosphatases, caused a decrease or disappearance of almost all phosphotyrosine-containing proteins and, at the same time, prevented the erythroid differentiation of HD3 cells [5].
  • The phosphorylation/dephosphorylation processes are associated with an early event(s) during the differentiation of HD3 cells and may not be connected to tyrosine residues [5].
  • Before induction, the HD3 cell transports glucose and 2-deoxyglucose (2-DG) [11].
  • Treatment of HD3 cells with the phosphatase inhibitors okadaic acid, vanadate or with 3-isobutyl-1-methyl-xanthine induced glucose transport and GLUT mRNAs [12].

Analytical, diagnostic and therapeutic context of HDAC3

  • Expression of heterophile Hanganutziu-Deicher (HD) antigen on the cell surface of various human malignant tumor tissues was studied by membrane immunofluorescence staining with chicken antiserum against N-glycolylneuraminyllactosylceramide (HD3) and fluorescein-conjugated rabbit anti-chicken IgG [13].
  • After treatment of HD3 cells with erythroid-inducing agents (hemin and butyric acid) at 42 degrees C, the profile of phosphotyrosine-containing proteins was altered [5].
  • A human Hanganutziu-Deicher (HD) antibody and a chicken anti-N-glycolyneuroaminyllactosylceramide (HD3) antibody were compared in their reaction against HD antigen-active ganglioside (HD3) and a glycoprotein (GP) by radioimmunoassay (RIA) [14].


  1. Molecular and biochemical events during differentiation of the HD3 chicken erythroblastic cell line. Grdisa, M., White, M.K. Int. J. Biochem. Cell Biol. (2003) [Pubmed]
  2. Characterisation of chicken erythroid nuclear proteins which bind to the nuclease hypersensitive regions upstream of the beta A- and beta H-globin genes. Plumb, M.A., Lobanenkov, V.V., Nicolas, R.H., Wright, C.A., Zavou, S., Goodwin, G.H. Nucleic Acids Res. (1986) [Pubmed]
  3. WD dipeptide motifs and LXXLL motif of chicken HIRA are essential for interactions with the p48 subunit of chromatin assembly factor-1 and histone deacetylase-2 in vitro and in vivo. Ahmad, A., Takami, Y., Nakayama, T. Gene (2004) [Pubmed]
  4. Expression of glyceraldehyde-3-phosphate dehydrogenase during differentiation of HD3 cells. Grdisa, M., White, M.K. Eur. J. Cell Biol. (1996) [Pubmed]
  5. Alteration of phosphotyrosine-containing proteins during differentiation of chicken erythroleukemia cells (HD3). Grdisa, M. Cell Biochem. Funct. (1998) [Pubmed]
  6. Erythrocytic differentiation and glyceraldehyde-3-phosphate dehydrogenase expression are regulated by protein phosphorylation and cAMP in HD3 cells. Grdisa, M., White, M.K. Int. J. Biochem. Cell Biol. (2000) [Pubmed]
  7. Loss of glucose transport in developing avian red cells. Johnstone, R.M., Mathew, A., Setchenska, M.S., Grdisa, M., White, M.K. Eur. J. Cell Biol. (1998) [Pubmed]
  8. Two chicken monoclonal antibodies specific for heterophil Hanganutziu-Deicher antigens. Asaoka, H., Nishinaka, S., Wakamiya, N., Matsuda, H., Murata, M. Immunol. Lett. (1992) [Pubmed]
  9. Sequence-specific DNA-binding proteins which interact with (G + C)-rich sequences flanking the chicken c-myc gene. Lobanenkov, V.V., Nicolas, R.H., Plumb, M.A., Wright, C.A., Goodwin, G.H. Eur. J. Biochem. (1986) [Pubmed]
  10. Analysis of the distribution of protein binding DNA motives in the vicinity of the 3'-side chicken alpha-globin enhancer. Targa, F.R., de Moura Gallo, C.V., Scherrer, K. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  11. Loss of glucose transporters is an early event in differentiation of HD3 cells. Mathew, A., Grdisa, M., Robbins, P.J., White, M.K., Johnstone, R.M. Am. J. Physiol. (1994) [Pubmed]
  12. Regulation of glucose transport in differentiating HD3 cells. Grdisa, M., White, M.K. Cell Biochem. Funct. (2000) [Pubmed]
  13. Tumor-associated expression of glycosphingolipid Hanganutziu-Deicher antigen in human cancers. Higashi, H., Nishi, Y., Fukui, Y., Ikuta, K., Ueda, S., Kato, S., Fujita, M., Nakano, Y., Taguchi, T., Sakai, S. Gann = Gan. (1984) [Pubmed]
  14. Potential use of specific human and chicken antibodies for detection of Hanganutziu-Deicher antigen(s) in sera of cancer patients. Mukuria, C.J., Noguchi, A., Suzuki, E., Naiki, M. Jpn. J. Med. Sci. Biol. (1994) [Pubmed]
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