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Jiyeong Lee,EunJeong Joo,HeeJoung Lim,JongMoon Park,KyuYoung Lee,Arum Park,AeEun Seok,HooKeun Lee,HeeGyoo Kang 대한신경정신의학회 2015 PSYCHIATRY INVESTIGATION Vol.12 No.2
Objective-Currently, there are a few biological markers to aid in the diagnosis and treatment of depression. However, it is not sufficient for diagnosis. We attempted to identify differentially expressed proteins during depressive moods as putative diagnostic biomarkers by using quantitative proteomic analysis of serum. Methods-Blood samples were collected twice from five patients with major depressive disorder (MDD) at depressive status before treatment and at remission status during treatment. Samples were individually analyzed by liquid chromatography-tandem mass spectrometry for protein profiling. Differentially expressed proteins were analyzed by label-free quantification. Enzyme-linked immunosorbent assay (ELISA) results and receiver-operating characteristic (ROC) curves were used to validate the differentially expressed proteins. For validation, 8 patients with MDD including 3 additional patients and 8 matched normal controls were analyzed. Results-The quantitative proteomic studies identified 10 proteins that were consistently upregulated or downregulated in 5 MDD patients. ELISA yielded results consistent with the proteomic analysis for 3 proteins. Expression levels were significantly different between normal controls and MDD patients. The 3 proteins were ceruloplasmin, inter-alpha-trypsin inhibitor heavy chain H4 and complement component 1qC, which were upregulated during the depressive status. The depressive status could be distinguished from the euthymic status from the ROC curves for these proteins, and this discrimination was enhanced when all 3 proteins were analyzed together. Conclusion-This is the first proteomic study in MDD patients to compare intra-individual differences dependent on mood. This technique could be a useful approach to identify MDD biomarkers, but requires additional proteomic studies for validation.
Tran, Trang Huyen,Park, SunYoung,Lee, Hyunjin,Park, Sungsuk,Kim, Bora,Kim, Ok-Hee,Oh, Byung-chul,Lee, Dongil,Lee, Hookeun The Royal Society of Chemistry 2012 The Analyst Vol.137 No.4
<P>In recent years, gold nanoparticles have been increasingly utilized as a promising material for biomedical analysis. We report here for the first time the synthesis of ultrasmall gold nanoparticles with core diameter of 1.2 nm functionalized with hydrazide groups and their use in isolation/enrichment of N-glycosylated peptides. Hydrazide-functionalized gold nanoparticles showed excellent stability in biological samples and exhibited a large capacity for peptide capturing. The captured peptides from tested standard glycoproteins were found to be highly specific as determined by Agilent HPLC chip and quadrupole time-of-flight (Q-TOF) mass spectrometer. The hydrazide-functionalized gold nanoparticles were successfully utilized in the isolation of a real proteome complex, which showed that more than 90% of captured product was glycopeptide. These results demonstrate that the ultrasmall gold nanoparticles can be used for a high-throughput analysis platform of glycoproteins.</P> <P>Graphic Abstract</P><P>Glycopeptide capturing using novel hydrazide-functionalization of glutathione-protected Au<SUB>25</SUB> ultrasmall nanoparticle is developed and demonstrated in tissue proteome analysis. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c1an15810d'> </P>
Zahra, Zahra,Kim, Seok-Young,Kim, Hye-Youn,Lee, Hwanhui,Lee, Heayyean,Jeon, Jun-Yeong,Kim, Dong-Min,Kim, Dong-Myung,Hong, Seong-Joo,Cho, Byung-Kwan,Lee, Hookeun,Lee, Choul-Gyun,Arshad, Muhammad,Choi, American Chemical Society 2018 Journal of agricultural and food chemistry Vol.66 No.32
<P>This study aimed to improve the production of phycobiliproteins using TiO<SUB>2</SUB> nanoparticles (NPs) in <I>Synechocystis</I> sp. PCC 6803. The growth characteristics of <I>Synechocystis</I> cells were not affected by TiO<SUB>2</SUB> NPs treatment, but this treatment increased the chlorophyll content significantly by 62.2% (14.6 mg/L) compared to that of control (9.0 mg/L) on day 16. Phycocyanin production was increased by 33.8% (29.3 g/L) compared to that of control (21.9 g/L) on day 8. Allophycocyanin production was increased by 55.0% (6.2 g/L) compared to that of control (4.0 g/L) on day 8, and by 22.4% (16.4 g/L) compared to that of control (13.4 g/L) on day 16. Direct infusion mass spectrometry revealed that TiO<SUB>2</SUB> NPs treatment significantly increased the levels of major thylakoid membranes of monogalactosyldiacylglycerols (18:2/18:3, 18:2/18:2, 18:1/18:2), phosphatidylglycerol (16:0/16:1), and sulfoquinovosyldiacylglycerols (16:0/16:1, 16:0:18:4) on day 8. These findings indicate that TiO<SUB>2</SUB> NPs have potential for commercial applications in <I>Synechocystis</I> species or other microalgal strains.</P> [FIG OMISSION]</BR>
HIF-1-Dependent Induction of Jumonji Domain-Containing Protein (JMJD) 3 under Hypoxic Conditions
Lee, Ho-Youl,Choi, Kang,Oh, Hookeun,Park, Young-Kwon,Park, Hyunsung Korean Society for Molecular and Cellular Biology 2014 Molecules and cells Vol.37 No.1
Jumonji domain-containing proteins (JMJD) catalyze the oxidative demethylation of a methylated lysine residue of histones by using $O_2$, ${\alpha}$-ketoglutarate, vitamin C, and Fe(II). Several JMJDs are induced by hypoxic stress to compensate their presumed reduction in catalytic activity under hypoxia. In this study, we showed that an H3K27me3 specific histone demethylase, JMJD3 was induced by hypoxia-inducible factor (HIF)-$1{\alpha}/{\beta}$ under hypoxia and that treatment with Clioquinol, a HIF-$1{\alpha}$ activator, increased JMJD3 expression even under normoxia. Chromatin immunoprecipitation (ChIP) analyses showed that both HIF-$1{\alpha}$ and its dimerization partner HIF-$1{\beta}$/Arnt occupied the first intron region of the mouse JMJD3 gene, whereas the HIF-$1{\alpha}/{\beta}$ heterodimer bound to the upstream region of the human JMJD3, indicating that human and mouse JMJD3 have hypoxia-responsive regulatory regions in different locations. This study shows that both mouse and human JMJD3 are induced by HIF-1.
Jang, Inae,Lee, Sun Young,Hwangbo, Song,Kang, Dukjin,Lee, Hookeun,Kim, Hugh I.,Moon, Bongjin,Oh, Han Bin Springer US 2017 Journal of the American Society for Mass Spectrome Vol.28 No.1
<P>The present study demonstrates that one-step peptide backbone fragmentations can be achieved using the TEMPO [2-(2,2,6,6-tetramethyl piperidine-1-oxyl)]-assisted free radical-initiated peptide sequencing (FRIPS) mass spectrometry in a hybrid quadrupole time-of-flight (Q-TOF) mass spectrometer and a Q-Exactive Orbitrap instrument in positive ion mode, in contrast to two-step peptide fragmentation in an ion-trap mass spectrometer (reference Anal. Chem. <B>85</B>, 7044-7051 ((30))). In the hybrid Q-TOF and Q-Exactive instruments, higher collisional energies can be applied to the target peptides, compared with the low collisional energies applied by the ion-trap instrument. The higher energy deposition and the additional multiple collisions in the collision cell in both instruments appear to result in one-step peptide backbone dissociations in positive ion mode. This new finding clearly demonstrates that the TEMPO-assisted FRIPS approach is a very useful tool in peptide mass spectrometry research.</P> [FIG OMISSION]</BR>
HIF-1-Dependent Induction of Jumonji Domain-Containing Protein (JMJD) 3 under Hypoxic Conditions
Ho-Youl Lee,Kang Choi,Hookeun Oh,박영권,박현성 한국분자세포생물학회 2014 Molecules and cells Vol.37 No.1
Jumonji domain-containing proteins (JMJD) catalyze the oxidative demethylation of a methylated lysine residue of histones by using O2, a-ketoglutarate, vitamin C, and Fe(II). Several JMJDs are induced by hypoxic stress to compensate their presumed reduction in catalytic activity under hypoxia. In this study, we showed that an H3K27me3 specific histone demethylase, JMJD3 was induced by hypoxia-inducible factor (HIF)-1a/b under hypoxia and that treatment with Clioquinol, a HIF-1a activator, increased JMJD3 expression even under normoxia. Chromatin immunoprecipitation (ChIP) analyses showed that both HIF-1a and its dimerization partner HIF-1b/Arnt occu-pied the first intron region of the mouse JMJD3 gene, whereas the HIF-1a/b heterodimer bound to the upstream region of the human JMJD3, indicating that human and mouse JMJD3 have hypoxia-responsive regulatory regions in different locations. This study shows that both mouse and human JMJD3 are induced by HIF-1.
A Proteomics Approach for the Human milk-derived Glycated Peptides using LC-MS/MS
Seong-Hyeon Cho,Jong-Moon Park,Hookeun Lee,Jun Hwan Song,Nam Mi Kang 한국분석과학회 2021 학술대회논문집 Vol.2021 No.11
Many studied have so far shown that AGEs and glycation adducts are significantly linked to changes in aging and disease. In particular, the level of glycation in human milk is important because the intake of AGEs is deeply related to the level of AGEs in infants. In this study, we used human milk samples (IRB 7001355-202108-E-153) obtained from 4 mothers with first baby and 4 mothers with not first baby. We isolated proteins using acetone preparation and TCA preparation. A total of 67 glycated proteins and 122 glycated peptides were quantified; among them, 19 glycated differentially expressed peptides were found. Through these results, we confirmed that there was a difference in the degree of glycation according to fertility. The study will pave the way for future studies to use proteomics for the evaluation of the mother’s human milk quality and the link between maternal health and human milk quality.
Jong-Moon Park,Na-Young Han,Hookeun Lee 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
Glycan play key roles in protein folding, cell-cell recognition, cancer metastasis, and the immune system. In cell, glycosylation comprise that many kinds of glycan structures associated with a specific glycoprotein have different functions. So, the biological meaning of glycosylation has made them a prime target for discovering biomarker in diseases. Identifying the numerous glycan, we have used new method to assess the diversity of the N-linked oligosaccharides without derivatization has been developed using on-line nano-liquid chromatography (nanoLC) and high resolution time-of-flight mass spectrometry. In three times MS/MS results, chips offered good sensitivity and reproducibility in separating a intact protein. In tandem mass spectra, glycan fragment ions were identified as N-glycan sequences for mining glycoproteome. As a result, we have identified several N-glycan structures from monoclonal antibody.