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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.
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.
An Automated High Throughput Proteolysis and Desalting Platform for Quantitative Proteomic Analysis
( Albert Baskar Arul ),( Na Young Han ),( Hookeun Lee ) 한국질량분석학회 2013 Mass spectrometry letters Vol.4 No.2
Proteomics for biomarker validation needs high throughput instrumentation to analyze huge set of clinical samples for quantitative and reproducible analysis at a minimum time without manual experimental errors. Sample preparation, a vital step in proteomics plays a major role in identification and quantification of proteins from biological samples. Tryptic digestion a major check point in sample preparation for mass spectrometry based proteomics needs to be more accurate with rapid processing time. The present study focuses on establishing a high throughput automated online system for proteolytic digestion and desalting of proteins from biological samples quantitatively and qualitatively in a reproducible manner. The present study compares online protein digestion and desalting of BSA with conventional off-line (in-solution) method and validated for real time sample for reproducibility. Proteins were identified using SEQUEST data base search engine and the data were quantified using IDEALQ software. The present study shows that the online system capable of handling high throughput samples in 96 well formats carries out protein digestion and peptide desalting efficiently in a reproducible and quantitative manner. Label free quantification showed clear increase of peptide quantities with increase in concentration with much linearity compared to off line method. Hence we would like to suggest that inclusion of this online system in proteomic pipeline will be effective in quantification of proteins in comparative proteomics were the quantification is really very crucial.
The impact of freeze-drying on the glycoproteomic profiles of human milk
Won-Ho Hahn,Seong Phil Bae,Hookeun Lee,Jong-Moon Park,Suyeon Park,이주현,강남미 한국분석과학회 2020 분석과학 Vol.33 No.4
Human milk (HM) glycoproteins play important roles protecting infants against various pathogens. Recently, freezing HM is reported to affect some glycoproteins and freeze-drying is suggested as an alternative method. However, the effects of freeze-drying on HM glycoproteins were not evaluated yet. Six fresh HM samples were collected from three healthy mothers at 15 and 60th days of lactation from each mother. Each sample was divided into frozen and freeze-dried subgroups yielding totally 12 samples, and the glycoproteomic analysis was performed by liquid chromatography mass spectrometry. The results were compared between samples of 15 and 60th days of lactation, and before and after the freeze-drying. Totally, 203 glycoproteins were detected. The glycoprotein levels were not different between two groups of 15/60th day of lactation and before/after freeze-drying groups (P > 0.050). In addition, significant correlation of glycoprotein levels was found between the different lactation stages (r = 0.897, P < 0.001) and the status of freeze-drying (r = 0.887, P < 0.001) in a partial correlation analysis. As no significant change of HM glycoproteins was not found after the freezedrying, we hope that introducing freeze-drying to HM banks is supported by the present study. This work was supported by the National Research Foundation (NRF) of Korea grant funded by the Korea government (MSIP) (No.2017R1D1A1B03034270; No.2020R1A2C1005082).
An Automated High Throughput Proteolysis and Desalting Platform for Quantitative Proteomic Analysis
Arul, Albert-Baskar,Han, Na-Young,Lee, Hookeun Korean Society for Mass Spectrometry 2013 Mass spectrometry letters Vol.4 No.2
Proteomics for biomarker validation needs high throughput instrumentation to analyze huge set of clinical samples for quantitative and reproducible analysis at a minimum time without manual experimental errors. Sample preparation, a vital step in proteomics plays a major role in identification and quantification of proteins from biological samples. Tryptic digestion a major check point in sample preparation for mass spectrometry based proteomics needs to be more accurate with rapid processing time. The present study focuses on establishing a high throughput automated online system for proteolytic digestion and desalting of proteins from biological samples quantitatively and qualitatively in a reproducible manner. The present study compares online protein digestion and desalting of BSA with conventional off-line (in-solution) method and validated for real time sample for reproducibility. Proteins were identified using SEQUEST data base search engine and the data were quantified using IDEALQ software. The present study shows that the online system capable of handling high throughput samples in 96 well formats carries out protein digestion and peptide desalting efficiently in a reproducible and quantitative manner. Label free quantification showed clear increase of peptide quantities with increase in concentration with much linearity compared to off line method. Hence we would like to suggest that inclusion of this online system in proteomic pipeline will be effective in quantification of proteins in comparative proteomics were the quantification is really very crucial.
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.