Publications by authors named "Chen Hou"

A new chelating resin containing bis[2-(2-benzothiazolylthioethyl)sulfoxide] was synthesized using chloromethylated polystyrene as material and characterized by elemental analysis and infrared spectra. The adsorption capacities of the newly formed resin for Hg(2+), Ag(+), Cu(2+), Zn(2+), Pb(2+), Mn(2+), Ni(2+), Cd(2+) and Fe(3+) were investigated over the pH range 1.0-6.

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Histone deacetylase 2 (HDAC2) is one of the histone-modifying enzymes that regulate gene expression by remodeling chromatin structure. Along with HDAC1, HDAC2 is found in the Sin3 and NuRD multiprotein complexes, which are recruited to promoters by DNA-binding proteins. In this study, we show that the majority of HDAC2 in human breast cancer cells is not phosphorylated.

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Nuclear morphometric descriptors such as nuclear size, shape, DNA content and chromatin organization are used by pathologists as diagnostic markers for cancer. However, our knowledge of events resulting in changes in nuclear shape and chromatin organization in cancer cells is limited. Nuclear matrix proteins, which include lamins, transcription factors (Sp1) and histone modifying enzymes (histone deacetylases), and histone modifications (histone H3 phosphorylation) have roles in organizing chromatin in the interphase nucleus, regulating gene expression programs and determining nuclear shape.

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Background And Purpose: Atopic diseases are thought to be associated with cytokine-mediated immune dysregulation, for example, a T helper cell type 1/2 (Th1/Th2) imbalance. CD30 is proposed to be one of the surrogate markers for Th2 immunity. In this study, we investigated whether CD30 is a good marker for atopy and Th2 predominance in a pediatric population.

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Dynamic histone acetylation has a role in chromatin remodeling and in the regulation of transcription. Histone deacetylases (HDACs) and histone acetyltransferases (HATs) catalyze reversible histone acetylation. HATs and HDACs exist as multiprotein complexes that have coactivator and corepressor activities, respectively.

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Sp1 and Sp3 are ubiquitously expressed mammalian transcription factors that function as activators or repressors. Although both transcription factors share a common domain involved in forming multimers, we demonstrate that Sp1 and Sp3 form separate complexes in estrogen-dependent human breast cancer cells. Sp1 and Sp3 complexes associate with histone deacetylases (HDACs) 1 and 2.

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The process of transcription unfolds the nucleosome. The unfolded nucleosome structure will be maintained as long as the histones are in a highly acetylated state. Typically the cysteine residue at position 110 of histone H3 is buried in the interior of the nucleosome.

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