Disease relevance of HDAC3

• The chicken erythroblast cell line HD3 is transformed by a temperature-sensitive mutant of avian erythroleukemia virus [1].

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

• The chicken erythroblast cell line HD3, which is infected with a temperature-sensitive avian erythroleukemia virus, becomes committed to differentiate to an erythrocyte upon temperature shift in the presence of inducers (hemin and butyric acid) [4].
• Alteration of phosphotyrosine-containing proteins during differentiation of chicken erythroleukemia cells (HD3) [5].

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].

References