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심운택,이동배,조영채,이영수,윤창규 충남대학교 의과대학 지역사회의학연구소 1991 충남의대잡지 Vol.18 No.1
For the purpose to estimate the exposure levels of heavy metals and to present a basis of occupational health managements to the industrial workers exposed to heavy metals, this study conducted to know the lead and chromium levels of whole blood of industrial workers. The study population were divided into three groups to the exposure levels ; directed exposure group, indirect exposure group and non-exposure group, and the sample number of workers who exposed to lead were 80, chromium were 77, and control group were 31. The contents of lead and chromium were analyzed by atomic absorption spectrophotometer. The results were summerized as follows : 1. Sex distribution of studied group were 77.1 % in male, and 22.9 % in female. Age distribution were 74.4% in 30-49 age group. The work in years were 43.1 % in 5-10 years, 29.8% in 1-4 years. 2. Mean blood level of lead were 33.53㎍/㎗ in direct exposure, 23.84㎍/㎗ in indirect exposure group and 11.77㎍/㎗ in control group. 3. Mean blood levels of chromium were 1.9㎍/㎗ in direct exposure, 1.51㎍/㎗ in indirect groups and 0.95㎍/㎗ in control group. 4. Mean lead levels of direct exposure group was higher in male than female as 36.44㎍/㎗, 27.35㎍/㎗ respectively, but there was no difference in indirect and control group by sex. Mean chromium levels of direct exposure group were higher levels 2.26㎍/㎗ in female than 1.84㎍/㎗ in male, but there were no difference in indirect and control group by sex. 5. The age group of 29 or younger among the direct exposed had high level of lead and chromium as 35.7㎍/㎗ 2.41㎍/㎗ respectively, but that age group had no evident difference in the level of lead and chromium among the indirect exposed and non-exposed.
Regulation of Myoblast Motility and Fusion by the CXCR4-associated Sialomucin, CD164
Bae, Gyu-Un,Gaio, Ursula,Yang, Youn-Joo,Lee, Hye-Jin,Kang, Jong-Sun,Krauss, Robert S. American Society for Biochemistry and Molecular Bi 2008 The Journal of biological chemistry Vol.283 No.13
<P>Myoblast fusion is fundamental to the development and regeneration of skeletal muscle. To fuse, myoblasts undergo cell-cell recognition and adhesion and merger of membranes between apposing cells. Cell migration must occur in advance of these events to bring myoblasts into proximity, but the factors that regulate myoblast motility are not fully understood. CD164 is a cell surface sialomucin that is targeted to endosomes and lysosomes via its intracellular region. In hematopoietic progenitor cells, CD164 forms complexes with the motility-stimulating chemokine receptor, CXCR4, in response to the CXCR4 ligand, CXCL12/SDF-1 (Forde, S., Tye, B. J., Newey, S. E., Roubelakis, M., Smythe, J., McGuckin, C. P., Pettengell, R., and Watt, S. M. (2007) Blood 109, 1825-1833). We have previously shown that CD164 stimulates myotube formation in vitro. We report here that CD164 is associated with CXCR4 in C2C12 myoblasts. Cells in which CD164 levels are increased or decreased via overexpression or RNA interference-mediated knockdown, respectively, show enhanced or reduced myotube formation and cell migration, the latter both basally and in response to CXCL12/SDF-1. Furthermore, expression of CD164 cytoplasmic tail mutants that alter the endosome/lysosome targeting sequence and, consequently, the subcellular localization in myoblasts, reveals a similar correlation between cell motility and myotube formation. Finally, Cd164 mRNA is expressed in the dorsal somite (the early myogenic compartment of the mouse embryo) and in premuscle masses. Taken together, these results suggest that CD164 is a regulator of myoblast motility and that this property contributes to its ability to promote myoblast fusion into myotubes.</P>
Bae, Gyu-Un,Kim, Bok-Geon,Lee, Hye-Jin,Oh, Ji-Eun,Lee, Su-Jae,Zhang, Wei,Krauss, Robert S.,Kang, Jong-Sun American Society for Microbiology 2009 Molecular and cellular biology Vol.29 No.15
<B>ABSTRACT</B><P>The p38 mitogen-activated protein kinase (MAPK) pathway is required for differentiation of skeletal myoblasts, but how the pathway is activated during this process is not well understood. One mechanism involves the cell surface receptor Cdo (also known as Cdon), which binds to Bnip-2 and JLP, scaffold proteins for Cdc42 and p38, respectively; formation of these complexes results in Bnip-2/Cdc42-dependent activation of p38. It has been reported that the tyrosine kinase Abl promotes myogenic differentiation in a manner dependent on its cytoplasmic localization, but the cytoplasmic signaling proteins with which it interacts to achieve this effect are unidentified. We report that Abl associates with both Cdo and JLP during myoblast differentiation. Abl binds a proline-rich motif in Cdo via its SH3 domain, and these regions of Abl and Cdo are required for their promyogenic effects. Cdo is important for full Abl kinase activity, and Abl is necessary for full activation of p38 MAPK, during myogenic differentiation. As seen with myoblasts depleted of Cdo, the diminished differentiation displayed by Abl-depleted cells is rescued by the expression of an activated form of the immediate upstream p38-activating kinase MAPK kinase 6. Abl's promyogenic effect is therefore linked to a multiprotein cell surface complex that regulates differentiation-dependent p38 activation.</P>
Hydrogen Peroxide Activates p70^S6k Signaling Pathway
Bae, Gyu-Un,Seo, Dong-Wan,Kwon, Hyoung-Keun,Lee, Hoi Young,Hong, Sungyoul,Lee, Zee-Won,Ha, Kwon-Soo,Lee, Hyang-Woo,Han. Jeung-Whan 성균관대학교 약학연구소 1999 成均藥硏論文集 Vol.11 No.-
We investigated a possible role of reactive oxygen species (ROS) in p70^S6k activation, which plays an important role in the progression of cells from G_0/G_1 to S phase of the cell cycle by translational up-regulation of a family of mRNA transcripts that encode for components of the protein synthetic machinery. Treatment of mouse epidermal cell JB6 with H_2O_2 generated extracellularly by glucose/glucose oxidase led to the activation of p70^S6k and p90^Rsk and to phosphorylation of p42^MAPK/p44^MAPK. The activation of p70^S6k and p90^Rsk was dose-dependent and transient, maximal activities being in extracts treated for 15 and 30 min, respectively. Further characterization of ROS-induced activation of p70^S6k using specific inhibitors for p70^S6k signaling pathway, rapamycin, and wortmannin revealed that ROS acted up-stream of the rapamycin-sensitive component FRAP/RAFT and wortmannin-sensitive component phosphatidylinositol 3-kinase, because both inhibitors caused the inhibition of ROS-induced p70^S6k activity. In addition, Ca^2+ chelation also inhibited ROS-induced activation of p70^S6k, indicating that Ca^2+ is a mediator of p70^S6k activation by ROS. However, down-regulation of 12-O-tetradecanoylphorbol-13-acetate (TPA)-responsive protein kinase C (PKC) by chronic pretreatment with TPA or a specific PKC inhibitor Ro-31-8220 did not block the activation of p70^S6k by ROS, indicating that the activation of TPA-responsive PKC was not required for stimulation of p70^S6k activity by H_2O_2 in JB6 cells. Exposure of JB6 cells to platelet-derived growth factor or epidermal growth factor led to a rapid increase in H_2O_2, phosphorylation, and activation of p70^S6k, which were antagonized by the pretreatment of catalase. Taken together, the results suggest that ROS act as a messenger in growth factor-induced p70^S6k signaling pathway.
Bae, Gyu-Un,Domené,, Sabina,Roessler, Erich,Schachter, Karen,Kang, Jong-Sun,Muenke, Maximilian,Krauss, Robert ,S. Elsevier 2011 American journal of human genetics Vol.89 No.2
<P>Holoprosencephaly (HPE), a common human congenital anomaly defined by a failure to delineate the midline of the forebrain and/or midface, is associated with diminished Sonic hedgehog (SHH)-pathway activity in development of these structures. SHH signaling is regulated by a network of ligand-binding factors, including the primary receptor PTCH1 and the putative coreceptors, CDON (also called CDO), BOC, and GAS1. Although binding of SHH to these receptors promotes pathway activity, it is not known whether interactions between these receptors are important. We report here identification of missense <I>CDON</I> mutations in human HPE. These mutations diminish CDON's ability to support SHH-dependent gene expression in cell-based signaling assays. The mutations occur outside the SHH-binding domain of CDON, and the encoded variant CDON proteins do not display defects in binding to SHH. In contrast, wild-type CDON associates with PTCH1 and GAS1, but the variants do so inefficiently, in a manner that parallels their activity in cell-based assays. Our findings argue that CDON must associate with both ligand and other hedgehog-receptor components, particularly PTCH1, for signaling to occur and that disruption of the latter interactions is a mechanism of HPE.</P>
Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation
Bae, Gyu-Un,Lee, Jae-Rin,Kim, Bok-Geon,Han, Ji-Won,Leem, Young-Eun,Lee, Hey-Jin,Ho, Seok-Man,Hahn, Myong-Joon,Kang, Jong-Sun The American Society for Cell Biology 2010 Molecular biology of the cell Vol.21 No.14
<P>Cell–cell interactions between muscle precursors are required for myogenic differentiation; however, underlying mechanisms are largely unknown. Promyogenic cell surface protein Cdo functions as a component of multiprotein complexes containing other cell adhesion molecules, Boc, Neogenin and N-cadherin, and mediates some of signals triggered by cell–cell interactions between muscle precursors. Cdo activates p38MAPK via interaction with two scaffold proteins JLP and Bnip-2 to promote myogenesis. p38MAPK and Akt signaling are required for myogenic differentiation and activation of both signaling pathways is crucial for efficient myogenic differentiation. We report here that APPL1, an interacting partner of Akt, forms complexes with Cdo and Boc in differentiating myoblasts. Both Cdo and APPL1 are required for efficient Akt activation during myoblast differentiation. The defective differentiation of Cdo-depleted cells is fully rescued by overexpression of a constitutively active form of Akt, whereas overexpression of APPL1 fails to do so. Taken together, Cdo activates Akt through association with APPL1 during myoblast differentiation, and this complex likely mediates some of the promyogenic effect of cell–cell interaction. The promyogenic function of Cdo involves a coordinated activation of p38MAPK and Akt via association with scaffold proteins, JLP and Bnip-2 for p38MAPK and APPL1 for Akt.</P>
( Un Taek Hwang ),( Junsoo Bae ),( Taekyeong Lee ),( Sung-yun Hwang ),( Jong-chan Kim ),( Jinseok Park ),( In-gyu Choi ),( Hyo Won Kwak ),( Sung-wook Hwang ),( Hwanmyeong Yeo ) 한국목재공학회 2021 목재공학 Vol.49 No.3
본 논문에서는 열수 탄화(hydrothermal carbonization)에 의해 제조된 리그닌 하이드로차의 탄화 특성을 조사하였고, 근적외선 분광법과 부분 최소 제곱(partial least squares) 회귀를 이용하여 탄화 거동을 예측하기 위한 모델을 수립하였다. 온도 200℃에서 열수 탄화된 리그닌의 탄소 함량은 무처리 시료 보다 약 3 wt% 높았으며 가열 시간이 증가할수록 탄소 함량도 서서히 증가하는 경향이 나타났다. 열수 탄화는 리그닌을 더욱 탄소 집약적으로 변화시키고 마이크로 파티클을 제거하여 더욱 균질한 특성을 부여하였다. 근적외선 분광법과 부분 최소 제곱 회귀를 이용한 판별 및 예측 모델은 수열 탄화의 적용 여부를 완벽히 구분했으며 높은 정확도로 열수 탄화 리그닌의 탄소 함량을 예측하였다. 본 연구로부터 근적외선 분광법과 결합된 부분 최소 제곱 회귀 모델을 이용하여 열수 탄화에 의해 제조된 리그닌 하이드로차의 탄화 특성을 빠르고 비파괴적으로 예측할 수 있다는 것이 확인되었다.
甘豆湯 및 加味甘豆湯 전탕액이 배양 심근세포의 LDH 활성도에 미치는 영향
박준배,권강범,김우경,오광수,김인규,이호섭,김영운,금경수,류도곤 대한동의병리학회 2001 동의생리병리학회지 Vol.15 No.5
To test the protective effect of herbal medicine on myocardial damage against adriamycin-induced myocardiotoxicity, cytotoxicity of adriamycin was examined using NR and LDH activity assay in the presence of water extract of Gamdu-tang, Gamigamdu-tang, or single constituents of these prescriptions. Myocardial toxicity was evaluated in neonatal mouse myocardiocytes in cultures. The results of these experiments were obtained as follows ; Adriamycin resulted in a decrease in viability, increases in LDH activity in cultured myocardial cells. Gamdu-tang water extract shows effects of protection from the cardiocyte toxicity induced by adriamycin treatment such as decreases in lactate dehydrogenase activity. Gamigamdutang water extract shows the similar protective elect as shown in gamdutang treatment on the cardiotoxicity induced by adriamycin. Single constuents of these prescriptions shows a significant effect of protection for cardiotoxicity induced by adriamycin in cultured myocardial cells. These results show that adriamycin elicits toxic effects in cultured myocardial cells derived from neonatal mouse, and suggest that water extract of gamdu-tang, gamigamdu-tang, Radix Glycyrrhizae, Semen Glycine, or Folium Phyllostachyos is very effective in the prevention of adriamycin-induced cardiotoxicity.