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- 저자 : ( Pyong Gon Moon ) (검색결과 15 건)
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Moon, Pyong-Gon,Hwang, Hyun-Ho,Boo, Yong Chool,Kwon, Joseph,Cho, Je-Yoel,Baek, Moon-Chang WILEY-VCH Verlag 2008 Electrophoresis Vol.29 No.21
<P>Many different types of urine proteome studies have been done, but urine glycoprotein studies are insufficient. Therefore, we studied the glycoproteins from rat urine, which could be used to identify biomarkers in an animal model. First, urinary proteins were prepared by using the dialysis and lyophilizing methods from rat urine. Glycoproteins enriched with lectin affinity purification, concanavalin A, jacalin and wheat germ agglutinin from the urinary proteins were separated by means of reverse-phase fast protein LC (FPLC) or 1-D PAGE. Each FPLC fraction and 1-D PAGE gel band were trypsin-digested and analyzed by means of nanoLC-MS/MS. LC-MS/MS analyses were carried out by using linear ion trap MS. A total of 318 rat urinary glycoproteins were identified from the FPLC fractions and gel bands; approximately 90% of identified proteins were confirmed as glycoproteins in Swiss-Prot. Many glycoproteins, known as biomarkers, including C-reactive protein, uromodulin, amyloid beta A4 protein, alpha-1-inhibitor 3, vitamin D-binding protein, kallikrein 3 and fetuin-A were identified in this study. By studying urinary glycoproteins collected from rat, these results may help to assist in identifying urinary biomarkers regarding various types of disease models.</P>
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단백체 분석을 위한 일차원 및 이차원 역상크로마토그래피의 비교
문평곤(Pyong-Gon Moon),조영은(Young-Eun Cho),백문창(Moon-Chang Baek) 大韓藥學會 2010 약학회지 Vol.54 No.5
Single-dimensional (1-D) and two-dimensional (2-D) LC methods were utilized to separate peptides from various sources followed by MS/MS analysis. Two-dimensional ultra-high performance liquid chromatography is a useful tool for proteome analysis, providing a greater peak capacity than 1-D LC. The most popular 2-D LC approach used today for proteomic research combines strong cation exchange and reversed-phase LC. We have evaluated an alternative mode for 2-D LC of peptides using 2-D RP-RP nano UPLC Q-TOF Mass Spectrometry, employing reversed-phase columns in both separation dimensions. As control experiments, we identified 129 proteins in 1-D LC and 322 proteins in 2-D LC from E.coli extract peptides. Furthermore, we applied this method to rat primary hepatocyte and a total of 170 proteins were identified from 1-D LC, and 527 proteins were identified from all 2-D LC system. The in-depth protein profiling established by this 2-D LC MS/MS from rat primary hepatocyte could be a very useful reference for future applications in regards to drug induced liver toxicity.
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( Mi Na Song ),( Pyong Gon Moon ),( Jeong Eun Lee ),( Minkyun Na ),( Wonku Kang ),( Yee Soo Chae ),( Ji Young Park ),( Hoyong Park ),( Moon Chang Baek ) 영남대학교 약품개발연구소 2013 영남대학교 약품개발연구소 연구업적집 Vol.23 No.0
This study presents a proteomic method that differentiates between matched normal and breast tumor tissues from ductal carcinoma in situ (DCIS) and invasive carcinoma from Korean women, to identify biomarker candidates and to understand pathogenesis of breast cancer in protein level. Proteins from tissues obtained by biopsy were extracted by RIPA buffer, digested by the gel-assisted method, and analyzed by nano-UPLC-MS/MS. From proteomic analysis based on label-free quantitation strategy, a non-redundant list of 298 proteins was identified from the normal and tumor tissues, and 244 proteins were quantified using IDEAL-Q software. Hierarchical clustering analysis showed two patterns classified as two groups, invasive carcinoma and DCIS, suggesting a difference between two carcinoma at the protein expression level as expected. Differentially expressed proteins in tumor tissues compared to the corresponding normal tissues were related to three biological pathways: antigen-processing and presentation, glycolysis/gluconeogenesis, and complement and coagulation cascades. Among them, the up-regulation of calreticulin (CRT) and protein disulfide isomerase A3 (PDIA3) was confirmed by Western blot analysis. In conclusion, this study showed the possibility of identifying biomarker candidates for breast cancer using tissues and might help to understand the pathophysiology of this cancer at the protein level.
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( Eun Jung Lee ),( Pyong Gon Moon ),( Moon Chang Baek ),( Hee Sun Kim ) 한국응용약물학회 2014 Biomolecules & Therapeutics(구 응용약물학회지) Vol.22 No.5
Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that regulate cell-matrix composition and are also involved in processing various bioactive molecules such as cell-surface receptors, chemokines, and cytokines. Our group recently reported that MMP-3, -8, and -9 are upregulated during microglial activation and play a role as proinflammatory mediators (Lee et al., 2010, 2014). In particular, we demonstrated that MMP-8 has tumor necrosis factor alpha (TNF-α)-converting enzyme (TACE) activity by cleaving the prodomain of TNF-α and that inhibition of MMP-8 inhibits TACE activity. The present study was undertaken to compare the effect of MMP-8 inhibitor (M8I) with those of inhibitors of other MMPs, such as MMP-3 (NNGH) or MMP-9 (M9I), in their regulation of TNF-α activity. We found that the MMP inhibitors suppressed TNF-α secretion from lipopolysaccharide (LPS)- stimulated BV2 microglial cells in an order of efficacy: M8I>NNGH>M9I. In addition, MMP inhibitors suppressed the activity of recombinant TACE protein in the same efficacy order as that of TNF-α inhibition (M8I>NNGH>M9I), proving a direct correlation between TACE activity and TNF-α secretion. A subsequent pro-TNF-α cleavage assay revealed that both MMP-3 and MMP-9 cleave a prodomain of TNF-α, suggesting that MMP-3 and MMP-9 also have TACE activity. However, the number and position of cleavage sites varied between MMP-3, -8, and -9. Collectively, the concurrent inhibition of MMP and TACE by NNGH, M8I, or M9I may contribute to their strong anti-inflammatory and neuroprotective effects.
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Differentiation of N-Glycans Released from Urinary ExosomeBetween IgA Nephropathy and TBMN
Nayoung Yun,Seunghyup Jeong,Pyong-Gon Moon,Moon Chang Baek,Hyun Joo An 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
IgA Nephropathy and thin basement membrane nephropathy (TBMN) have identical hematuria symptom but different seriousness. In general, the biopsy of the kidney is performed to distinguish between IgAN and TBMN. There are a lot of needs for clinician to have a sensitive and specific biomarker for diseases diagnosis. Glycosylation is highly sensitive to the biological environment changes and considerably affected by disease states. Glycan is known as playing key roles in cancer metastasis and intracellular recognition. Therefore, the examination of glycosylation change in urinary exosome may be a new way for potential biomarkers to differentiate TBMN and IgAN. In this study, we have analyzed 18 individuals exosomes secreted into urine from renal epithelial cells. Samples were consisted of three different groups, mainly TBMN, IgAN patients, and healthy volunteers. Briefly, N-glycans from urinary exosomes were released by PNGase F digestion and then enriched by solid phase extraction using a porous graphitized carbon cartridge. N-glycans were eluted with three different solution (10% ACN, 20% ACN, 40% ACN with 0.05% TFA in H2O) based on the glycan size and polarity. Enriched glycans were analyzed using MALDI-TOF/TOF mass spectrometry and nanoLCchip/QTOF mass spectrometry for qualitative and quantitative profiling, respectively. We found that high mannose glycans are high in abundance in neutral fractions while complex type glycans consisting of [Hex]n=4-6 [HexNAc]n=4-5[Fuc]n=0-1[NeuAc]1 are high in abundance in acidic fractions.
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Identification of Potential Serum Biomarkers in Mercury-Treated Mice Using a Glycoproteomic Approach
Kim, Bong-Hwa,Moon, Pyong-Gon,Lee, Jeong-Eun,Lee, Soyoung,Kim, Sook-Kyung,Lee, Jong Kwon,Kim, Sang-Hyun,Baek, Moon-Chang SAGE Publications 2013 International journal of toxicology Vol.32 No.5
<P>Mercury is a well-recognized health hazard and a deleterious environmental contaminant. Exposure to mercury can cause neurotoxic manifestations, nephrotoxicity, and immune function alterations; however, the mechanisms and related proteins responsible for these effects are still unclear. Our goal is to understand the relationship between the toxicity of mercury and the proteins affected by this toxic heavy metal and to define biomarkers for mercury intoxication. Two different forms of mercury, organic methylmercury or inorganic mercury sulfide, were orally administered to the mice for 4 weeks. To reduce complexity of the serum proteome, we enriched glycoproteins from mice serum with lectin concanavalin A resin, and the tryptic peptides of the purified glycoproteins were subjected to nanoultra performance liquid chromatography-Quadrupole time-of-flight for identification and label-free quantification. In this study, we characterized approximately 209 proteins from mice serum, and, among them, 21 proteins were differentially expressed in organic methylmercury-treated mice serum compared with the control group. Two proteins, serum amyloid P component (SAP) and inter α-trypsin inhibitor heavy chain 4 (ITI-H4), were upregulated in organic methylmercury-treated mice and confirmed with different doses of both types of mercury by Western blot analysis. Results of immunohistochemistry also confirmed the validity of SAP and ITI-H4 as biomarker candidates for organic methylmercury exposure. Findings of this study may assist in understanding the relationship between toxicity of mercury and upregulated proteins in mouse serum. Furthermore, the proteins identified here might be used as biomarker candidates in mercury intoxication.</P>
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Glycosylation on Urinary Exosome for Biomarker Discovery
Nayoung Yun,Seunghyup Jeong,Pyong-Gon Moon,Moon Chang Baek,Hyun Joo An 한국당과학회 2013 한국당과학회 학술대회 Vol.2013 No.1
IgA Nephropathy (IgAN) and thin basement membrane nephropathy (TBMN) have identical hematuria symptom but different seriousness in renal function. In case of TBMN, renal function is usually normal but IgAN is the most common cause of end-stage renal failure. In general, the biopsy of the kidney is performed to distinguish between IgAN and TBMN. There are a lot of needs for clinicians to have a sensitive and specific biomarker for differentiation IgAN and TBMN. Exosomes which are small cell-derived vesicles have been suggested as potential biomarkers in diagnosis of disease because these are secreted from original cell with intracellular fluids and apical membrane. Urinary exosomes, 40-100nm vesicles secreted to urine by renal cells, may provide non-invasive diagnosis manner of kidney disease. Glycosylation is highly sensitive to the biological environment changes and considerably affected by disease states. Glycan is known as playing key roles in cancer metastasis and intracellular recognition. Therefore, the examination of glycosylation change in urinary exosome may be a new way for potential biomarkers to differentiate TBMN and IgAN. In this study, we have analyzed 18 individuals exosomes secreted into urine from renal epithelial cells. Samples were composed of three different groups, mainly TBMN, IgAN patients, and healthy volunteers. Briefly, N-glycans from urinary exosomes were released by PNGase F digestion and then enriched by solid phase extraction using a porous graphitized carbon cartridge. N-glycans were eluted with three different solution (10% ACN, 20% ACN, and 40% ACN with 0.05% TFA in H2O) based on the glycan size and polarity. Enriched glycans were analyzed for qualitative and quantitative profiling using high resolution MALDI-TOF/TOF mass spectrometry and performed tandem MS to obtain extensive structure information. We also separated isomer-specific glycans by nano-LC chip/Q-TOF mass spectrometry. We found that high mannose glycans are high in abundance in normal group. Complex, non-sialylated fucosylated tri-, and tetraantennary glycans are significantly different between normal and patients, which suggest the potential biomarker.
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Lee, Jeong-Eun,Moon, Pyong-Gon,Lee, In-Kyu,Baek, Moon-Chang Springer-Verlag 2015 The Protein Journal Vol.34 No.3
<P>Extracellular vesicles (EVs) such as exosomes are secretory vesicles that act as autocrine, paracrine, or endocrine messengers; mediate intercellular cross-talk; and carry a cargo of various proteins. Because EVs can be transported to recipient cells via circulation, many researchers have been studying EVs from immune cells or cancer cells. Adipocytes are also considered endocrine cells and secrete adipokines such as adiponectin, regulating a variety of intracellular signaling pathways. Expansion of adipose tissue in obesity alters adipokine secretion, thereby increasing the risk of metabolic diseases. Characterization of adipocyte-derived exosomes is necessary to explain the communication between adipocytes and other cell types. In the present study, to identify proteins associated with adipocyte-derived exosomes, we isolated exosomes from adipose tissue of obese diabetic and obese nondiabetic rats. We identified proteins by analyzing exosomes from obese rats with type 2 diabetes and their matched control littermates using nano-liquid chromatography with tandem mass spectrometry coupled with label-free relative quantification. We identified 509 proteins from adipocytes including 81 known adipokines; ~78% of all the identified proteins were categorized as exosome-associated proteins. Among the protein profiles, we uncovered 128 upregulated and 72 downregulated proteins, which are differentially expressed in OLETF adipocyte-derived exosomes. This study seems to demonstrate for the first time hundreds of proteins in exosomes released by adipocytes in obese rats and rats with type 2 diabetes. Thus, protein profiles of exosomes from adipocytes possibly indicate the transmission of signals as part of cell-cell communication and should further our understanding of obesity- and diabetes-related diseases.</P>
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( Young Eun Cho ),( Pyong Gon Moon ),( Jeong Eun Lee ),( Thoudam S K Singh ),( Wonku Kang ),( Hyun Chul Lee ),( Myung Hoon Lee ),( Sang Hyun Kim ),( Moon Chang Baek ) 영남대학교 약품개발연구소 2013 영남대학교 약품개발연구소 연구업적집 Vol.23 No.0
Hepatocytes are used widely as a cell model for investigation of xenobiotic metabolism and the toxic mechanism of drugs. Simvastatin is the first statin drug used extensively in clinical practice for control of elevated cholesterol or hypercholesterolemia. However, it has also been reported to cause adverse effects in liver due to cellular damage. In this study, for proteomic and transcriptomic analysis, rat primary hepatocytes were exposed to simvastatin at IC20 concentration for 24 h. Among a total of 607 differentially expressed proteins, 61 upregulated and 29 downregulated proteins have been identified in the simvastatin-treated group. At the mRNA level, results of transcriptomic analysis revealed 206 upregulated and 41 downregulated genes in the simvastatin-treated group. Based on results of transcriptomic and proteomic analysis, NRF2-mediated oxidative stress response, xenobiotics by metabolism of cytochrome P450, fatty acid metabolism, bile metabolism, and urea cycle and inflammation metabolism pathways were focused using IPA software. Genes (FASN, UGT2B, ALDH1A1, CYP1A2, GSTA2, HAP90, IL-6, IL-1, FABP4, and ABC11) and proteins (FASN, CYP2D1, UG2TB, ALDH1A1, GSTA2, HSP90, FABP4, and ABCB11) related to several important pathways were confirmed by real-time PCR andWestern blot analysis, respectively. This study will provide new insight into the potential toxic pathways induced by simvastatin.
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