• 미생물학회지
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• 제40권3호
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• pp.226-229
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• 2004

염색질을 구성하는 histone 단백질 lysine 잔기에 histone acetylase에 의하여 결합된 acetyl기를 제거하는 histone deacetylase (HDAC)는 진핵세포 생물의 염색질 안정 파 및 유전자 발현에 매우 큰 영향을 미친다. 국내에서 분리된 영지의 HDAC 유전자를 클로닝 하고자 cDNA 및 genomic DNA를 대상으로 PCR을 수행한 결과 470bp의 cDNA유전자와, 585 bp, 589 bp 및 630 bp길이의 genomic DNA유전자 조각을 클로닝 하였다. 이들의 염기서열을 근거로 아미노산 서열을 다른 균류의 HDAC와 비교한 결과 59-72％의 상동성을 보였다.

• BMB Reports
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• 제33권3호
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• pp.263-267
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• 2000

We cloned $hda1^+$ (histone deacetylase 1) of fission yeast Schizosaccharomyces pombe. The hda1 of S. pombe was previously reported to encode for an active histone deacetylase (Rundlett et al., 1996; Olsson et al., 1998). The $hda1^+$ is phylogenetically related to the new open reading frame HOS2 of Saccharomyces cerevisiae and only shows a partial homology to the well-known histone deacetylase subclasses, RPD3 and HDA1. A single hda1 mRNA of 1.8 kb was detected at the same level in actively growing and nitrogen-starved cells. When highly over-expressed in S. pombe from an inducible promoter, $hda1^+$ inhibited cell proliferation and caused defects in morphology and cell division. The increased histone deacetylase activity was detected in hdar over-expressing cells. These results suggest that the Hda1p should function on the regulation of cell division possibly by (Allfrey, 1966) direct deacetylation of cytoskeletal (Wade et al., 1997) and cell division regulatory proteins, (Wolffe, 1997) or by controlling their gene expressions.

• Bulletin of the Korean Chemical Society
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• 제33권6호
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• pp.2063-2066
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• 2012

• BMB Reports
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• 제36권1호
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• pp.110-119
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• 2003

The acetylation state of histone is reversibly regulated by histone acetyltransferase (HAT) and deacetylase (HDAC). An imbalance of this reaction leads to an aberrant behavior of the cells in morphology, cell cycle, differentiation, and carcinogenesis. Recently, these key enzymes in the gene expression were cloned. They revealed a broad use of this modification, not only in histone, but also other proteins that involved transcription, nuclear transport, and cytoskeleton. These results suggest that HAT/HDAC takes charge of multiple-functions in the cell, not just the gene expression. HDAC is especially known to play an important role in carcinogenesis. The enzyme has been considered a target molecule for cancer therapy. The inhibition of HDAC activity by a specific inhibitor induces growth arrest, differentiation, and apoptosis of transformed or several cancer cells. Some of these inhibitors are in a clinical trial at phase I or phase II. The discovery and development of specific HDAC inhibitors are helpful for cancer therapy, and decipher the molecular mode of action for HDAC.

• 대한약리학회:학술대회논문집
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• 대한약리학회 2006년도 58th Annual Meeting of The Korean Society of Pharmacology
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• pp.42-42
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• 2006

• 한국환경성돌연변이발암원학회:학술대회논문집
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• 한국환경성돌연변이발암원학회 2003년도 추계학술대회
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• pp.166-166
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• 2003

• 한국환경성돌연변이발암원학회:학술대회논문집
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• 한국환경성돌연변이발암원학회 2004년도 춘계학술대회
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• pp.109-109
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• 2004

• KSBB Journal
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• 제30권1호
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• pp.44-51
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• 2015

Chinese hamster ovary (CHO) cells are the most widely used mammalian host for the commercial production of recombinant proteins. However, they show relatively low yields of recombinant proteins in comparison with microbial cells. Various strategies have been tried to overcome this drawback. The acetyl moieties are attached to the N-terminus of histone by histone acetyltransferase (HAT) while histone deacetylase (HDAC) removes histone-bound acetyl groups. HDAC inhibitor (HDACi), such as sodium butyrate, sodium propionate and valproic acid, can enhance specific productivity of CHO cells. Human albumin-erythropoietin (Alb-EPO) is a novel 105 kDa protein comprising recombinant human EPO fused to human albumin. In this study, we examined the effects of HDACi on the production of Alb-EPO in CHO cells with various concentrations in the range of 0-1 mM. The results showed that sodium butyrate was found to be the best HDACi for enhancing productivity. It enhanced not only the production of Alb-EPO but also the apoptosis of recombinant CHO cells.

• 대한약학회:학술대회논문집
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• 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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• pp.184.1-184.1
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• 2003

HDAC and HAT (histone acetyltransferase) are involved in co-regulation in chromatin remodeling and the functional regulation of gene transcription. Abnormal recruitment of HDAC is related to carcinogenesis. Thus, the identification of potent histone deacetylase (HDAC) inhibitor has been considered as very intriguing approach for development for cancer chemotherapy. More recently, anti-inflammatory activity of SAHA cytokines was reported via reduction of proinflammatory cytokinres in vitro and in vivo. (omitted)

• Biomolecules & Therapeutics
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• 제14권2호
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• pp.67-74
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• 2006

EoL-1 cells differentiate into eosinophils in the presence of n-butyrate, but the mechanism has remained to be elucidated. Because n-butyrate can inhibit histone deacetylases, we hypothesized that the inhibition of histone deacetylases induces the differentiation of EoL-1 cells into eosinophils. In this study, using n-butyrate and two other histone deacetylase inhibitors, apicidin and trichostatin A, we have analyzed the relationship between the inhibition of histone deacetylases and the differentiation into eosinophils in EoL-1 cells. It was demonstrated that apicidin and n-butyrate induced a continuous acetylation of histones H4 and H3, inhibited the proliferation of EoL-1 cells, and induced the expression of markers for mature eosinophils such as integrin ${\beta}7$, CCR1, and CCR3 on EoL-1 cells, while trichostatin A evoked a transient acetylation of his tones and induced no differentiation into eosinophils. These findings suggest that the continuous inhibition of histone deacetylases in EoL-1 cells induces the differentiation into mature eosinophils.