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( Gwang Hyeon Eom ),( Hyun Kook ) 생화학분자생물학회 2015 BMB Reports Vol.48 No.3
Cardiac hypertrophy is a form of global remodeling, although the initial step seems to be an adaptation to increased hemodynamic demands. The characteristics of cardiac hypertrophy include the functional reactivation of the arrested fetal gene program, where histone deacetylases (HDACs) are closely linked in the development of the process. To date, mammalian HDACs are divided into four classes: I, II, III, and IV. By structural similarities, class II HDACs are then subdivided into IIa and IIb. Among class I and II HDACs, HDAC2, 4, 5, and 9 have been reported to be involved in hypertrophic responses; HDAC4, 5, and 9 are negative regulators, whereas HDAC2 is a pro-hypertrophic mediator. The molecular function and regulation of class IIa HDACs depend largely on the phosphorylation-mediated cytosolic redistribution, whereas those of HDAC2 take place primarily in the nucleus. In response to stresses, posttranslational modification (PTM) processes, dynamic modifications after the translation of proteins, are involved in the regulation of the activities of those hypertrophy-related HDACs. In this article, we briefly review 1) the activation of HDAC2 in the development of cardiac hypertrophy and 2) the PTM of HDAC2 and its implications in the regulation of HDAC2 activity.[BMB Reports 2015; 48(3): 131-138]
Eom, Gwang Hyeon,Nam, Yoon Seok,Oh, Jae Gyun,Choe, Nakwon,Min, Hyun-Ki,Yoo, Eun-Kyung,Kang, Gaeun,Nguyen, Vu Hong,Min, Jung-Joon,Kim, Jong-Keun,Lee, In-Kyu,Bassel-Duby, Rhonda,Olson, Eric N.,Park, Woo Grune & Stratton 2014 Circulation research Vol.114 No.7
<P><B><U>Rationale:</U></B></P><P>Histone deacetylases (HDACs) are closely involved in cardiac reprogramming. Although the functional roles of class I and class IIa HDACs are well established, the significance of interclass crosstalk in the development of cardiac hypertrophy remains unclear.</P><P><B><U>Objective:</U></B></P><P>Recently, we suggested that casein kinase 2α1–dependent phosphorylation of HDAC2 leads to enzymatic activation, which in turn induces cardiac hypertrophy. Here we report an alternative post-translational activation mechanism of HDAC2 that involves acetylation of HDAC2 mediated by p300/CBP-associated factor/HDAC5.</P><P><B><U>Methods and Results:</U></B></P><P>Hdac2 was acetylated in response to hypertrophic stresses in both cardiomyocytes and a mouse model. Acetylation was reduced by a histone acetyltransferase inhibitor but was increased by a nonspecific HDAC inhibitor. The enzymatic activity of Hdac2 was positively correlated with its acetylation status. p300/CBP-associated factor bound to Hdac2 and induced acetylation. The HDAC2 K75 residue was responsible for hypertrophic stress–induced acetylation. The acetylation-resistant Hdac2 K75R showed a significant decrease in phosphorylation on S394, which led to the loss of intrinsic activity. Hdac5, one of class IIa HDACs, directly deacetylated Hdac2. Acetylation of Hdac2 was increased in Hdac5-null mice. When an acetylation-mimicking mutant of Hdac2 was infected into cardiomyocytes, the antihypertrophic effect of either nuclear tethering of Hdac5 with leptomycin B or Hdac5 overexpression was reduced.</P><P><B><U>Conclusions:</U></B></P><P>Taken together, our results suggest a novel mechanism by which the balance of HDAC2 acetylation is regulated by p300/CBP-associated factor and HDAC5 in the development of cardiac hypertrophy.</P>
폐렴구균에 의한 지역사회 획득 폐렴에서 페니실린 내성률과 내성에 따른 임상경과에 관한 연구
홍지현 ( Hong Ji Hyeon ),이형석 ( Lee Hyeong Seog ),정승현 ( Jeong Seung Hyeon ),김규원 ( Kim Gyu Won ),엄광석 ( Eom Gwang Seog ),이재명 ( Lee Jae Myeong ),장승훈 ( Jang Seung Hun ),김동규 ( Kim Dong Gyu ),현인규 ( Hyeon In Gyu 대한결핵 및 호흡기학회 2003 Tuberculosis and Respiratory Diseases Vol.54 No.3
Mechanism of Knee Adduction Moment Reduction Through Contralateral Cane Use in Healthy Subjects
Hyeon-Soo Shin,Jun-Young Lee,Yeong-Jun Cho,Min-Jae Kim,Gwang-Moon Eom 한국정밀공학회 2023 International Journal of Precision Engineering and Vol.24 No.12
The use of a contralateral cane has demonstrated a reduction in the external knee adduction moment (KAM) in patients with knee osteoarthritis. However, the underlying mechanism remains unclear. This study aimed to investigate the specific mechanism in healthy young subjects. Sixteen healthy young participants were included in this study. They walked on a floor under three loading conditions: no cane and with cane loads equivalent to 5% and 10% of body weight. Change in posture and kinetic features of ipsilateral leg were examined at two instants of ground reaction force (GRF) peaks. The results revealed a substantial decrease (40–55%) in both KAM and moment arm, whereas only 12% decrease was observed in GRF with 10% cane loading. Furthermore, KAM was strongly correlated with moment arm (r = 0.97, p < 0.01), but not with GRF (p > 0.05). The reduction in moment arm could be attributed to a medial shift of knee joint and/or a lateral shift of GRF. At the maximum cane loading, medial shift in the knee joint center was significant (p < 0.001), while any shift in GRF was insignificant (p > 0.80). The results suggest that the primary factor contributing to the reduction in KAM is the decrease in moment arm among healthy young subjects. Importantly, the reduction in moment arm was primarily induced by a medial shift of the knee joint center, emphasizing the significance of postural changes.
Heart failure with preserved ejection fraction: present status and future directions
Somy Yoon,Gwang Hyeon Eom 생화학분자생물학회 2019 Experimental and molecular medicine Vol.51 No.-
The clinical importance of heart failure with preserved ejection fraction (HFpEF) has recently become apparent. HFpEF refers to heart failure (HF) symptoms with normal or near-normal cardiac function on echocardiography. Common clinical features of HFpEF include diastolic dysfunction, reduced compliance, and ventricular hypokinesia. HFpEF differs from the better-known HF with reduced ejection fraction (HFrEF). Despite having a “preserved ejection fraction,” patients with HFpEF have symptoms such as shortness of breath, excessive tiredness, and limited exercise capability. Furthermore, the mortality rate and cumulative survival rate are as severe in HFpEF as they are in HFrEF. While betablockers and renin-angiotensin-aldosterone system modulators can improve the survival rate in HFrEF, no known therapeutic agents show similar effectiveness in HFpEF. Researchers have examined molecular events in the development of HFpEF using small and middle-sized animal models. This review discusses HFpEF with regard to etiology and clinical features and introduces the use of mouse and other animal models of human HFpEF.
Controlling the magnetic properties of layered Cr₂Te₃ ultra-thin film via ex-situ annealing
In Hak Lee,Yeong Gwang Khim,Jae Un Eom,Jung Yun Kee,Hyuk Jin Kim,Byoung Ki Choi,Min Jay Kim,Younghak Kim,Byeong-hyeon Lee,Sung Ok Won,Hoyoung Suh,Hye Jung Chang,Ryung Kim,Minyoung Jung,Kyeong Jun Lee 한국자기학회 2022 한국자기학회 학술연구발표회 논문개요집 Vol.32 No.2
Regulation of MDM2 E3 ligase-dependent vascular calcification by MSX1/2
권덕화,Choe Nakwon,신세라,Ryu Juhee,김낙성,Eom Gwang Hyeon,Nam Kwang-Il,Kim Hyung Seok,Ahn Youngkeun,김영국,Park Woo Jin,Mendrysa Susan M.,Kook Hyun 생화학분자생물학회 2021 Experimental and molecular medicine Vol.53 No.-
Vascular calcification increases morbidity and mortality in patients with cardiovascular and renal diseases. Previously, we reported that histone deacetylase 1 prevents vascular calcification, whereas its E3 ligase, mouse double minute 2 homolog (MDM2), induces vascular calcification. In the present study, we identified the upstream regulator of MDM2. By utilizing cellular models and transgenic mice, we confirmed that E3 ligase activity is required for vascular calcification. By promoter analysis, we found that both msh homeobox 1 (Msx1) and msh homeobox 2 (Msx2) bound to the MDM2 promoter region, which resulted in transcriptional activation of MDM2. The expression levels of both Msx1 and Msx2 were increased in mouse models of vascular calcification and in calcified human coronary arteries. Msx1 and Msx2 potentiated vascular calcification in cellular and mouse models in an MDM2-dependent manner. Our results establish a novel role for MSX1/MSX2 in the transcriptional activation of MDM2 and the resultant increase in MDM2 E3 ligase activity during vascular calcification.