http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Bone Remodeling: Histone Modifications as Fate Determinants of Bone Cell Differentiation
Yi, Sun-Ju,Lee, Hyerim,Lee, Jisu,Lee, Kyubin,Kim, Junil,Kim, Yeojin,Park, Jae-Il,Kim, Kyunghwan MDPI AG 2019 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol.20 No.13
<P>The bone tissue is a dynamic complex that constitutes of several interdependent systems and is continuously remodeled through the concerted actions of bone cells. Osteoblasts are mononucleated cells, derived from mesenchymal stem cells, responsible for bone formation. Osteoclasts are large multinucleated cells that differentiate from hematopoietic progenitors of the myeloid lineage and are responsible for bone resorption. The lineage-specific differentiation of bone cells requires an epigenetic regulation of gene expressions involving chromatin dynamics. The key step for understanding gene regulatory networks during bone cell development lies in characterizing the chromatin modifying enzymes responsible for reorganizing and potentiating particular chromatin structure. This review covers the histone-modifying enzymes involved in bone development, discusses the impact of enzymes on gene expression, and provides future directions and clinical significance in this area.</P>
Histone tail cleavage as a novel epigenetic regulatory mechanism for gene expression
( Sun-ju Yi ),( Kyunghwan Kim ) 생화학분자생물학회(구 한국생화학분자생물학회) 2018 BMB Reports Vol.51 No.5
Chromatin is an intelligent building block that can express either external or internal needs through structural changes. To date, three methods to change chromatin structure and regulate gene expression have been well-documented: histone modification, histone exchange, and ATP-dependent chromatin remodeling. Recently, a growing body of literature has suggested that histone tail cleavage is related to various cellular processes including stem cell differentiation, osteoclast differentiation, granulocyte differentiation, mammary gland differentiation, viral infection, aging, and yeast sporulation. Although the underlying mechanisms suggesting how histone cleavage affects gene expression in view of chromatin structure are only beginning to be understood, it is clear that this process is a novel transcriptional epigenetic mechanism involving chromatin dynamics. In this review, we describe the functional properties of the known histone tail cleavage with its proteolytic enzymes, discuss how histone cleavage impacts gene expression, and present future directions for this area of study. [BMB Reports 2018; 51(5): 211-218]
Yi, Sun-Ju,Kim, Kyung Hwan,Choi, Hyun Jung,Yoo, Je Ok,Jung, Hyo-Il,Han, Jeong-A,Kim, Young-Myeong,Suh, In Bum,Ha, Kwon-Soo Korean Society of Molecular Biology 2006 Molecules and cells Vol.21 No.1
<P>Maitotoxin (MTX) is known as one of the most potent marine toxins involved in Ciguatera poisoning, but intracellular signaling pathways caused by MTX was not fully understood. Thus, we have investigated whether intracellular reactive oxygen species (ROS) are involved in MTX-induced cellular responses in human umbilical vein endothelial cells. MTX induced a dose-dependent increase of intracellular [Ca(2+)]. MTX stimulated the production of intracellular ROS in a dose- and time-dependent manner, which was suppressed by BAPTA-AM, an intracellular Ca(2+) che-lator. Ionomycin also elevated the ROS production in a dose-dependent manner. MTX elevated transamidation activity in a time-dependent manner and the activation was largely inhibited by transfection of tissue transglutaminase siRNA. The activation of tissue transglutaminase and ERK1/2 by MTX was sup-pressed by BAPTA-AM or ROS scavengers. In addition, MTX-induced cell death was significantly de-layed by BAPTA-AM or a ROS scavenger. These results suggest that [Ca(2+)]-dependent generation of in-tracellular ROS, at least in part, play an important role in MTX-stimulated cellular responses, such as activation of tTGase, ERK phosphorylation, and in-duction of cell death, in human umbilical vein endothelial cells.</P>
Yi, Sun-Ju,Hwang, Seong Yun,Oh, Myung-ju,Kim, Kyunghwan,Jhun, Byung H. ZOOLOGICAL SOCIETY OF KOREA 2018 ANIMAL CELLS AND SYSTEMS Vol.22 No.2
<P><B>ABSTRACT</B></P><P>p130 Crk-associated substrate (Cas) is an adaptor protein associating with many other signaling proteins and regulates a various biological processes including cell adhesion, migration, and growth factor stimulation. However, the exact functional role of Cas in growth factor signaling pathway was poorly understood. Here we investigated the role of Cas and its domains in the effects of insulin, EGF, and IGF-1 on c-Jun gene expression, DNA synthesis, cytoskeletal reorganization. We found that microinjection of anti-Cas antibody and C-terminal domain of Cas (Cas-CT) specifically inhibited EGF-induced, but not insulin- or IGF-1-induced, c-Jun expression. Cell cycle progression and cytoskeleton reorganization induced by insulin and EGF, but not by IGF-1, were inhibited by microinjected anti-Cas and Cas-CT. In contrast, microinjection of the substate domain (Cas-SD) of Cas did not have any inhibitory effects. These results revealed that the Cas-CT is differentially implicated in insulin and EGF-mediated, but not IGF-1-mediated, c-Jun expression, DNA synthesis and membrane ruffling.</P>
Adverse effects of farnesyltransferase inhibitors on insulin actions
Sun-Ju Yi,Byung Hak Jhun,Kyunghwan Kim 충북대학교 동물의학연구소 2017 Journal of Biomedical and Translational Research Vol.18 No.3
Ras activates a series of downstream effectors, including the mitogen-activated protein kinase pathway and the Rac/Rho pathway after insulin stimulation. Mutations in Ras are found in approximately 30% of all human cancers and are critical factors in tumor initiation and maintenance. There are four Ras proteins with 80-90% amino acid sequence homology with major differences in the carboxyl termini. Ras proteins undergo farnesylation on their carboxyl termini catalyzed by the enzyme protein farnesyltransferase (FTase), which facilitates localization of Ras proteins to the inner surface of the plasma membrane. Because inhibition of FTase would prevent Ras from processing into its active form, FTase is viewed as a potential therapeutic target. A variety of FTase inhibitors have showed great potency against tumor cells in preclinical studies. Although many farnesyltransferase inhibitors have been developed, their adverse effects on the mitogenic and metabolic actions of insulin are not completely understood. Here we show that YH3096, a farnesyltransferase inhibitor, inhibits insulin-mediated DNA synthesis in HIRc-B cells without affecting c-Jun expression and membrane ruffling in HIRc-B cells. Moreover, YH3096 and its derivatives did not affect insulin-induced glucose uptake in 3T3-L1 adipocytes. Our results provide a laboratory evaluation of the effects of Ras inhibitors on insulin functions.