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Kim, Young Jun,Kim, Hackyoung,Noh, Kwangmo Korean Society for Mass Spectrometry 2014 Mass spectrometry letters Vol.5 No.3
Microglia are the confined immune cells of the central nervous system (CNS). In response to injury or infection, microglia readily become activated and release proinflammatory mediators that are believed to contribute to microglia-mediated neurodegeneration. In the present study, inflammation was induced in the immortalized murine microglial cell line BV-2 by lipopolysaccharide (LPS) treatment. We firstly performed phosphoproteomics analysis and phosphoinositide lipidomics analysis with LPS activated microglia in order to compare phosphorylation patterns in active and inactive microglia and to detect the pattern of changes in phosphoinositide regulation upon activation of microglia. Mass spectrometry analysis of the phosphoproteome of the LPS treatment group compared to that of the untreated control group revealed a notable increase in the diversity of cellular phosphorylation upon LPS treatment. Additionally, a lipidomics analysis detected significant increases in the amounts of phosphoinositide species in the LPS treatment. This investigation could provide an insight for understanding molecular mechanisms underlying microglia-mediated neurodegenerative diseases.
( Young Jun Kim ),( Hackyoung Kim ),( Kwangmo Noh ) 한국질량분석학회 2014 Mass spectrometry letters Vol.5 No.3
Microglia are the confined immune cells of the central nervous system (CNS). In response to injury or infection, microglia readily become activated and release proinflammatory mediators that are believed to contribute to microglia-mediated neurodegeneration. In the present study, inflammation was induced in the immortalized murine microglial cell line BV-2 by lipopolysaccharide (LPS) treatment. We firstly performed phosphoproteomics analysis and phosphoinositide lipidomics analysis with LPS activated microglia in order to compare phosphorylation patterns in active and inactive microglia and to detect the pattern of changes in phosphoinositide regulation upon activation of microglia. Mass spectrometry analysis of the phosphoproteome of the LPS treatment group compared to that of the untreated control group revealed a notable increase in the diversity of cellular phosphorylation upon LPS treatment. Additionally, a lipidomics analysis detected significant increases in the amounts of phosphoinositide species in the LPS treatment. This investigation could provide an insight for understanding molecular mechanisms underlying microglia-mediated neurodegenerative diseases.
Analysis of Phosphatidylinositol 3,4,5-Trisphosphates of PTEN Expression on Mammalian Cells
Jahan, Nusrat,Park, Taeseong,Kim, Young Hwan,Lee, Dongsun,Kim, Hackyoung,Noh, Kwangmo,Kim, Young Jun Korean Society for Mass Spectrometry 2013 Mass spectrometry letters Vol.4 No.3
The goal of this study is to find an experimental condition which enables us to perform enzymatic studies on the cellular behavior of PTEN (phosphatase and tensine homolog) through identification of molecular species of phosphatidylinositol 3,4,5-trisphosphates and their quantitative analysis in a mammalian cell line using mass spectrometry. We initially exployed a two-step extraction process using HCl for extraction of phosphatidylinositol 3,4,5-trisphosphates from two mammalian cell lines and further analyzed the extracted phosphatidylinositol 3,4,5-trisphosphates using tandem mass spectrometry for the identification of them. We finally quantified the concentration of phosphatidylinositol 3,4,5-trisphosphates using internal standard calibration. From these observation, we found that HEK 293-T cells is a good model to examine the enzymatic behavior of PTEN in a cell, and the minimum amount of phosphatidylinositol 3,4,5-trisphosphates is more than 50 pmol for quantification in a mass spectrometer. These results suggest that the well-optimized experimental conditions are required for the investigation of the cellular PTEN in terms of the catalytic mechanism and further for the detailed identification of cellular substrates.
Analysis of Phosphatidylinositol 3,4,5-Trisphosphates of PTEN Expression on Mammalian Cells
( Nusrat Jahan ),( Taeseong Park ),( Young Hwan Kim ),( Dongsun Lee ),( Hackyoung Kim ),( Kwangmo Noh ),( Young Jun Kim ) 한국질량분석학회 2013 Mass spectrometry letters Vol.4 No.3
The goal of this study is to find an experimental condition which enables us to perform enzymatic studies on the cellular behavior of PTEN (phosphatase and tensine homolog) through identification of molecular species of phosphatidylinositol 3,4,5- trisphosphates and their quantitative analysis in a mammalian cell line using mass spectrometry. We initially exployed a two-step extraction process using HCl for extraction of phosphatidylinositol 3,4,5-trisphosphates from two mammalian cell lines and further analyzed the extracted phosphatidylinositol 3,4,5-trisphosphates using tandem mass spectrometry for the identification of them. We finally quantified the concentration of phosphatidylinositol 3,4,5-trisphosphates using internal standard calibration. From these observation, we found that HEK 293-T cells is a good model to examine the enzymatic behavior of PTEN in a cell, and the minimum amount of phosphatidylinositol 3,4,5-trisphosphates is more than 50 pmol for quantification in a mass spectrometer. These results suggest that the well-optimized experimental conditions are required for the investigation of the cellular PTEN in terms of the catalytic mechanism and further for the detailed identification of cellular substrates.
임종수(Chongsu Lim),배학영(Hackyoung Bae),김주형(Juhyung Kim) 한국국방우주학회 2023 한국국방우주학회지 Vol.1 No.1
우리나라 나로우주센터는 지리적으로 중위도에 위치하고 있고, 주변국에 둘러싸여 있어 우주발사체 발사방위가 크게 제한받는다. 본 논문에서는 이러한 지형적인 문제점을 극복하는 방안으로 해상발사체계의 유용성을 주장하였다. 해상발사체계는 탑재 중량을 증가시킬 수 있는 동향발사가 가능하고, 발사 실패로 인한 2차 피해를 감소시킬 수 있으며, 폭증하고 있는 국내외 위성 발사 수요를 감당할 수 있는 시대에 걸맞은 매력적인 옵션이다. 그동안 새로운 발사장과 발사체계의 필요성에 대한 논의는 많았지만, 구체적인 대안으로 해상발사체계의 가능성에 대해 의견을 제시한 논문은 찾아보기 힘들다. 아직 국내에서는 제대로 논의가 이루어지지 않은 해상발사체계에 대해 담론을 제기하는 만큼, 구체적인 구현방법과 사업화 전략에 대한 논의에는 한계가 있지만, 이 논문으로 말미암아 앞으로 해상발사체계에 대한 구체적이고 활발한 연구가 진행되기를 기대한다. Korea's Naro Space Center is located in mid-latitude and is surrounded by neighboring countries, so the launc h direction is greatly restricted. In this paper, the usefulness of the maritime launch system was argued as a way to overcome this problem. It is expected that the use of maritime launch systems will enable the launch to increase payload, reduce secondary damage due to possible failure, and meet the rapidly increasing demand for satellite launches from domestic and international companies. Although there have been many discussions o n the need for a new launch site and launch system, it is difficult to find a paper that presents an opinion o n the possibility of a maritime launch system as a specific alternative. As we are raising a discourse on the maritime launch system, which has not yet been properly discussed in Korea, there are limitations in discussin g specific implementation methods and commercialization strategies. However, It is hoped that this paper will lead to detailed and active research on marine launch systems in the future.
Invited Mini Review : The diverse roles of RNA polymerase II C-terminal domain phosphatase SCP1
( Harikrishna Reddy R ),( Hackyoung Kim ),( Kwangmo Noh ),( Young Jun Kim ) 생화학분자생물학회(구 한국생화학분자생물학회) 2014 BMB Reports Vol.47 No.4
RNA polymerase II carboxyl-terminal domain (pol II CTD) phosphatases are a newly emerging family of phosphatases that are members of DXDX (T/V). The subfamily includes Small CTD phosphatases, like SCP1, SCP2, SCP3, TIMM50, HSPC129 and UBLCP. Extensive study of SCP1 has elicited the diversified roles of the small C terminal domain phosphatase. The SCP1 plays a vital role in various biological activities, like neuronal gene silencing and preferential Ser5 dephosphorylation, acts as a cardiac hypertrophy inducer with the help of its intronic miRNAs, and has shown a key role in cell cycle regulation. This short review offers an explanation of the mechanism of action of small CTD phosphatases, in different biological activities and metabolic processes. [BMB Reports 2014; 47(4): 192-196]
( Rallabandi Harikrishna Reddy ),( Hackyoung Kim ),( Seungbin Cha ),( Bongsoo Lee ),( Young Jun Kim ) 한국미생물 · 생명공학회 2017 Journal of microbiology and biotechnology Vol.27 No.5
Phosphorylation, a critical mechanism in biological systems, is estimated to be indispensable for about 30% of key biological activities, such as cell cycle progression, migration, and division. It is synergistically balanced by kinases and phosphatases, and any deviation from this balance leads to disease conditions. Pathway or biological activity-based abnormalities in phosphorylation and the type of involved phosphatase influence the outcome, and cause diverse diseases ranging from diabetes, rheumatoid arthritis, and numerous cancers. Protein tyrosine phosphatases (PTPs) are of prime importance in the process of dephosphorylation and catalyze several biological functions. Abnormal PTP activities are reported to result in several human diseases. Consequently, there is an increased demand for potential PTP inhibitory small molecules. Several strategies in structure-based drug designing techniques for potential inhibitory small molecules of PTPs have been explored along with traditional drug designing methods in order to overcome the hurdles in PTP inhibitor discovery. In this review, we discuss druggable PTPs and structure-based virtual screening efforts for successful PTP inhibitor design.