Phil Young Lee
Korea University
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Publication
Featured researches published by Phil Young Lee.
Nature Communications | 2015
Chul-Su Yang; Jwa-Jin Kim; Tae Sung Kim; Phil Young Lee; Soo Yeon Kim; Hyemi Lee; Dong-Min Shin; Loi T. Nguyen; Moo-Seung Lee; Hyo Sun Jin; Kwang-Kyu Kim; Chul-Ho Lee; Myung Hee Kim; Sung Goo Park; Jin-Man Kim; Hueng-Sik Choi; Eun-Kyeong Jo
Excessive activation of the NLRP3 inflammasome results in damaging inflammation, yet the regulators of this process remain poorly defined. Herein, we show that the orphan nuclear receptor small heterodimer partner (SHP) is a negative regulator of NLRP3 inflammasome activation. NLRP3 inflammasome activation leads to an interaction between SHP and NLRP3, proteins that are both recruited to mitochondria. Overexpression of SHP competitively inhibits binding of NLRP3 to apoptosis-associated speck-like protein containing a CARD (ASC). SHP deficiency results in increased secretion of proinflammatory cytokines IL-1β and IL-18, and excessive pathologic responses typically observed in mouse models of kidney tubular necrosis and peritoneal gout. Notably, the loss of SHP results in accumulation of damaged mitochondria and a sustained interaction between NLRP3 and ASC in the endoplasmic reticulum. These data are suggestive of a role for SHP in controlling NLRP3 inflammasome activation through a mechanism involving interaction with NLRP3 and maintenance of mitochondrial homeostasis.
Experimental and Molecular Medicine | 2008
Won Kon Kim; Hyang‐Ran Hwang; Do Hyung Kim; Phil Young Lee; Yu Jung In; Hye-Young Ryu; Sung Goo Park; Kwang-Hee Bae; Sang Chul Lee
Atopic dermatitis (AD) is an inflammatory skin disorder that is both uncomfortable and distressing to patients, and its prevalence has been steadily increasing. It is obvious that the identification of efficient markers of AD in plasma would offer the possibility of effective diagnosis, prevention, and treatment strategies. In this study, a proteomic approach was used to analyze plasma glycoproteins from both children with AD and healthy child donors. Several protein spots showing significant quantitative changes in the AD patients were identified. Through sequential studies, it was confirmed that CD5L and ApoE were significantly up-regulated or down-regulated, respectively, in the plasma from AD patients compared with that from healthy donors. In addition, we suggest that the up-regulated CD5L in AD patients causes eosinophilia by inhibiting apoptosis or promoting the proliferation of eosinophils either in combination with or without IL-5. The glycoproteomic data in this study provides clues to understanding the mechanism of atopic alterations in plasma and suggests AD-related proteins can be used as candidate markers for AD.
Proteomics | 2009
Sunyoung Kim; Phil Young Lee; Hye-Jun Shin; Do Hyung Kim; Sunghyun Kang; Hyung-Bae Moon; Sang Won Kang; Jin-Man Kim; Sung Goo Park; Byoung Chul Park; Dae-Yeul Yu; Kwang-Hee Bae; Sang Chul Lee
The hepatitis B virus X‐protein (HBx), a multifunctional viral regulator, participates in the viral life cycle and in the development of hepatocellular carcinoma (HCC). We previously reported a high incidence of HCC in transgenic mice expressing HBx. In this study, proteomic analysis was performed to identify proteins that may be involved in hepatocarcinogenesis and/or that could be utilized as early detection biomarkers for HCC. Proteins from the liver tissue of HBx‐transgenic mice at early stages of carcinogenesis (dysplasia and hepatocellular adenoma) were separated by 2‐DE, and quantitative changes were analyzed. A total of 22 spots displaying significant quantitative changes were identified using LC‐MS/MS. In particular, several proteins involved in glucose and fatty acid metabolism, such as mitochondrial 3‐ketoacyl‐CoA thiolase, intestinal fatty acid‐binding protein 2 and cytoplasmic malate dehydrogenase, were differentially expressed, implying that significant metabolic alterations occurred during the early stages of hepatocarcinogenesis. The results of this proteomic analysis provide insights into the mechanism of HBx‐mediated hepatocarcinogenesis. Additionally, this study identifies possible therapeutic targets for HCC diagnosis and novel drug development for treatment of the disease.
Journal of Biochemistry and Molecular Biology | 2013
Jin Hwa Cho; Phil Young Lee; Woo-Chan Son; Seung-Wook Chi; Byoung Chul Park; Jeong-Hoon Kim; Sung Goo Park
Apoptosis, programmed cell death, is a process involved in the development and maintenance of cell homeostasis in multicellular organisms. It is typically accompanied by the activation of a class of cysteine proteases called caspases. Apoptotic caspases are classified into the initiator caspases and the executioner caspases, according to the stage of their action in apoptotic processes. Although caspase-3, a typical executioner caspase, has been studied for its mechanism and substrates, little is known of caspase-6, one of the executioner caspases. To understand the biological functions of caspase-6, we performed proteomics analyses, to seek for novel caspase-6 substrates, using recombinant caspase-6 and HepG2 extract. Consequently, 34 different candidate proteins were identified, through 2-dimensional electrophoresis/MALDI-TOF analyses. Of these identified proteins, 8 proteins were validated with in vitro and in vivo cleavage assay. Herein, we report that HAUSP, Kinesin5B, GEP100, SDCCAG3 and PARD3 are novel substrates for caspase-6 during apoptosis. [BMB Reports 2013; 46(12): 588-593]
Molecules and Cells | 2011
Phil Young Lee; Kwang Hee Bae; Dae Gwin Jeong; Seung Wook Chi; Jeong Hee Moon; Seongman Kang; Sayeon Cho; Sang Chul Lee; Byoung Chul Park; Sung Goo Park
Glutathione peroxidases (Gpxs) are the key anti-oxidant enzymes found in Saccharomyces cerevisiae. Among the three Gpx isoforms, glutathione peroxidase 3 (Gpx3) is ubiquitously expressed and modulates the activities of redox-sensitive thiol proteins involved in various biological reactions. By using a proteomic approach, glyceraldehyde-3-phosphate dehydrogenase 2 (GAPDH2; EC 1.2.1.12) was found as a candidate protein for interaction with Gpx3. GAPDH, a key enzyme in glycolysis, is a multi-functional protein with multiple intracellular localizations and diverse activities. To validate the interaction between Gpx3 and GAPDH2, immunoprecipitation and a pull-down assay were carried out. The results clearly showed that GAPDH2 interacts with Gpx3 through its carboxyl-terminal domain both in vitro and in vivo. Additionally, Gpx3 helps to reduce the S-nitrosylation of GAPDH upon nitric oxide (NO) stress; this subsequently increases cellular viability. On the basis of our findings, we suggest that Gpx3 protects GAPDH from NO stress and thereby contributes to the maintenance of homeostasis during exposure to NO stress.
Biochemical and Biophysical Research Communications | 2009
Hana Lee; Seung Wook Chi; Phil Young Lee; Sunghyun Kang; Sayeon Cho; Chong-Kil Lee; Kwang-Hee Bae; Byoung Chul Park; Sung Goo Park
Dihydroxyacetone (DHA) induces the formation of advanced glycation endproducts (AGEs), which are involved in several diseases. Earlier, we identified dihydroxyacetone kinase 1 (Dak1) as a candidate glutathione peroxidase 3 (Gpx3)-interacting protein in Saccharomyces cerevisiae. This finding is noteworthy, as no clear evidence on the involvement of oxidative stress systems in DHA-induced AGE formation has been found to date. Here, we demonstrate that Gpx3 interacts with Dak1, alleviates DHA-mediated stress by upregulating Dak activity, and consequently suppresses AGE formation. Based on these results, we propose that defense systems against oxidative stress and DHA-induced AGE formation are related via interactions between Gpx3 and Dak1.
Journal of Biochemistry and Molecular Biology | 2016
Phil Young Lee; Byoung Chul Park; Seung Wook Chi; Kwang Hee Bae; Sunhong Kim; Sayeon Cho; Seongman Kang; Jeong-Hoon Kim; Sung Goo Park
Granzyme A (GzmA) was first identified as a cytotoxic T lymphocyte protease protein with limited tissue expression. A number of cellular proteins are known to be cleaved by GzmA, and its function is to induce apoptosis. Histones H1, H2B, and H3 were identified as GzmA substrates during apoptotic cell death. Here, we demonstrated that histone H4 was cleaved by GzmA during staurosporine-induced cell death; however, in the presence of caspase inhibitors, staurosporine-treated Raji cells underwent necroptosis instead of apoptosis. Furthermore, histone H4 cleavage was blocked by the GzmA inhibitor nafamostat mesylate and by GzmA knockdown using siRNA. These results suggest that histone H4 is a novel substrate for GzmA in staurosporine-induced cells. [BMB Reports 2016; 49(10): 560-565]
Folia Microbiologica | 2013
Seo Young Bang; Jeong-Hoon Kim; Phil Young Lee; Seung-Wook Chi; Sayeon Cho; Gwan-Su Yi; Pyung Keun Myung; Byoung Chul Park; Kwang-Hee Bae; Sung Goo Park
In Saccharomyces cerevisiae, the Yap family of basic leucine zipper (bZip) proteins contains eight members. The Yap family proteins are implicated in a variety of stress responses; among these proteins, Yap1 acts as a major regulator of oxidative stress responses. However, the functional roles of the remaining Yap family members are poorly understood. To elucidate the function of Yap2, we mined candidate target genes of Yap2 by proteomic analysis. Among the identified genes, FRM2 was previously identified as a target gene of Yap2, which confirmed the validity of our screening method. YNL134C and YDL124W were also identified as candidate Yap2 target genes. These genes were upregulated in strains overexpressing Yap2 and possess Yap2 target sequences in their promoter regions. Furthermore, chromatin immunoprecipitation assays showed that YNL134C and YDL124W have Yap2 binding motif. These data will help to elucidate the functional role of Yap2.
Proteomics | 2007
Tae Hyuk Kang; Kwang-Hee Bae; Min‐jung Yu; Won-Kon Kim; Hyang‐Ran Hwang; Hyeyun Jung; Phil Young Lee; Sunghyun Kang; Tae-Sung Yoon; Sung Goo Park; Seong Eon Ryu; Sang Chul Lee
Journal of Microbiology and Biotechnology | 2008
Phil Young Lee; Kwang Hee Bae; Chang Won Kho; Sunghyun Kang; Do Hee Lee; Sayeon Cho; Seongman Kang; Sang Chul Lee; Byoung Chul Park; Sung Goo Park
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Korea Research Institute of Bioscience and Biotechnology
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