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        유아·놀이 중심 개정 누리과정에 대한 사회적 인식 네트워크 분석

        서영숙 ( Seo¸ Youngsuk ),한기순 ( Han¸ Kisoon ) 미래유아교육학회 2021 미래유아교육학회지 Vol.28 No.4

        본 연구는 개정 누리과정의 유아중심ㆍ놀이중심 교육과정에 관한 사회적 인식을 확인하고자 2019개정 누리과정과 관련하여 국내 유입률 1위인 Naver 포털 사이트의 뉴스에 등록된 기사 제목이나 ‘유아중심ㆍ놀이중심 교육과정’ 홍보물 등의 댓글을 대상으로 온라인 사용자들의 반응을 분석하였다. 이를 위해 Excel과 NetMiner 4.0을 활용하여 총 557건의 관련 기사와 홍보물 10건의 댓글에서 사용된 단어들을 중심으로 네트워크 분석한 결과 1072개의 주제어를 추출하였으며 빈도가 높은 상위 39개의 주제어들을 정제하였다. 영향력이 높은 단어 확인을 위해 중심성 분석 실시 결과 ‘유아·놀이 중심’, ‘유아기’, ‘교육’, ‘교사’ 등으로 나타났다. 이에 영향력 있는 단어와 응집도가 높은 단어들을 확인하기 위해 커뮤니티 분석과 공유 의미 구조 및 상이한 의미 체계를 분석하기 위해 에고 네트워크 분석을 실시한 결과 개정 누리과정의 운영적인 부분에서 유아교육현장의 목소리와 부모의 다양한 요청이 있었으며, 유아·놀이 중심교육의 필요성과 중요성에는 공감하지만 준비과정 및 학습적인 측면에서 우려의 의견을 확인할 수 있었다. ‘2019 개정 누리과정’은 유아가 놀이의 주체이며 놀이의 중심이 되어 더불어 놀이가 교육과정의 중심이 되어야 한다. 유아가 놀이를 통해 자연스럽게 배우고 자랄 수 있는 ‘놀이 권’을 되찾아주고자 개편한 교육과정의 목적이 실현될 수 있도록 유아교육 현장안착을 위한 실질적인 지원이 필요하다. 이와 더불어 구체적인 계획 및 실천 방향을 제시함으로써 유아가 놀이 경험을 통해 자율성과 창의성이 신장되어 놀이의 재미와 행복에 몰입되기를 기대한다. In this study, in order to to examine the social perception of the early childhood-based and play-based curriculum, this study analyzed online user comments and news articles registered on the Naver portal site, the No. 1 website in Korea. The responses of online users were analyzed for comments such as ‘process’ promotional materials. For this, 1072 keywords were extracted as a result of network analysis focusing on words used in a total of 557 related articles and 10 comments on promotional materials using Excel and NetMiner 4.0, and the top 39 keywords with high frequency were refined. As a result of centrality analysis to identify high-impact words, ‘early childhood-based / play-based’, ‘early childhood’, ‘education’, and ‘teacher’ were found. In order to identify influential words and words with high cohesion, community analysis and ego network analysis were conducted to analyze shared semantic structures and different semantic systems. There was a request, and although we sympathized with the necessity and importance of early childhood and play-oriented education, they were able to confirm opinions of concern in terms of the preparation process and learning. In the ‘2019 Revision Nuri Curriculum’, children should be the subject of play and the center of play, and play should be the center of the curriculum. Practical support is needed for the establishment of early childhood education so that the purpose of the reorganized curriculum can be realized in order to regain the ‘right to play’ that children can learn and grow naturally through play. In addition, it is expected that children will be immersed in the fun and happiness of play by increasing their autonomy and creativity through play experiences by suggesting specific plans and action directions.

      • Investigation of <i>O</i>-glycosylation heterogeneity of recombinant coagulation factor IX using LC–MS/MS

        Seo, Youngsuk,Park, Gyeong Mi,Oh, Myung Jin,An, Hyun Joo 'Future Science, LTD' 2017 Bioanalysis Vol.9 No.18

        <P>Recombinant coagulation factor IX (rFIX) has extraordinarily multiple post-translational modifications including N-glycosylation and O-glycosylation which have a drastic effect on biological functions and in vivo recovery. Unlike N-glycosylation extensively characterized, there are a few studies on O-glycosylation due to its intrinsic complexity. In-depth O-glycosylation analysis is necessary to better understand and assess pharmacological activity of rFIX. Results: We determined unusual O-glycosylations including O-fucosylation and O-glucosylation which were located at Serine 53 and 61, respectively in EGF domain. Other O-glycosylations bearing core 1 glycan moiety were found on activation peptide. Conclusion: This is the first comprehensive study to characterize O-glycosylation of rFIX using MS-based glycomic and glycoproteomic approaches. Site-specific profiling will be a powerful platform to determine bioequivalence of biosimilars.</P>

      • Comprehensive Characterization of Biotherapeutics by Selective Capturing of Highly Acidic Glycans Using Stepwise PGC-SPE and LC/MS/MS

        Seo, Youngsuk,Oh, Myung Jin,Park, Jin Young,Ko, Jae Kyoung,Kim, Jin Young,An, Hyun Joo American Chemical Society 2019 ANALYTICAL CHEMISTRY - Vol.91 No.9

        <P>The glycosylation of biologics is an important factor in pharmacological functions such as efficacy, safety, and biological activity and is easily affected by subtle changes in the cellular environment. Hence, comprehensive and in-depth glycomic characterization of biological products should be performed to ensure product quality and process consistency prior to regulatory approval, but it is still highly challenging due to glycan microheterogeneity produced by enzymatic machinery. In this study, we have developed a systematic methodology for the separation and characterization of various glycans of biotherapeutics using the combination of solid-phase extraction (SPE) and high resolution LC/MS. Neutral and multiple-acidic glycans were selectively fractionated by SPE with a porous graphitized carbon (PGC) cartridge according to their molecule size and polarity (acidity, p<I>K</I><SUB>a</SUB>). Subsequent LC-MS and -MS/MS analyses enabled us to obtain glycan compositions, structures, and quantitative information. Indeed, we have successfully performed glycomic characterization of agalsidase-beta, a representative therapeutic enzyme containing both phosphorylated and sialylated glycans. In addition, a comparative analysis of functional glycans released from different batches of enzymes was performed to verify our method. These results suggest that stepwise PGC-SPE and LC/MS/MS pairwise assays can be used as an efficient tool to detect glycosylation changes of therapeutic glycoproteins including abundant acidic species in biologics or biosimilar development.</P> [FIG OMISSION]</BR>

      • SCOPUSKCI등재

        MS Platform for Erythropoietin Glycome Characterization

        ( Youngsuk Seo ),( Unyong Kim ),( Myung Jin Oh ),( Na Young Yun ),( Hyun Joo An ) 한국질량분석학회 2015 Mass spectrometry letters Vol.6 No.3

        Recombinant erythropoietins (EPOs) are an important class of biotherapeutics that stimulate red blood cell production. The quality, safety, and potency of EPO variants are determined largely by their glycosylation, which makes up nearly half their mass. Thus, detailed glycomic analyses are important to assess biotherapeutic quality and establish the equivalency of biosimilar EPOs now coming to market. High-resolution mass spectrometry (MS) has recently emerged as the premier tool for glycan analysis in EPOs. Using the accurate mass measurements provided by high-resolution MS, the compositions of even large, complex glycans can easily be determined. When combined with a nano-LC separation, differentiation of structural isomers also becomes a possibility. These components, together, provide a comprehensive picture of biotherapeutic glycosylation. In this review, we provide an overview of MS-based analytical platform for glycomic characterization of EPO biotherapeutics and biosimilars.

      • SCOPUSKCI등재

        MS Platform for Erythropoietin Glycome Characterization

        Seo, Youngsuk,Kim, Unyong,Oh, Myung Jin,Yun, Na Young,An, Hyun Joo Korean Society for Mass Spectrometry 2015 Mass spectrometry letters Vol.6 No.3

        Recombinant erythropoietins (EPOs) are an important class of biotherapeutics that stimulate red blood cell production. The quality, safety, and potency of EPO variants are determined largely by their glycosylation, which makes up nearly half their mass. Thus, detailed glycomic analyses are important to assess biotherapeutic quality and establish the equivalency of biosimilar EPOs now coming to market. High-resolution mass spectrometry (MS) has recently emerged as the premier tool for glycan analysis in EPOs. Using the accurate mass measurements provided by high-resolution MS, the compositions of even large, complex glycans can easily be determined. When combined with a nano-LC separation, differentiation of structural isomers also becomes a possibility. These components, together, provide a comprehensive picture of biotherapeutic glycosylation. In this review, we provide an overview of MS-based analytical platform for glycomic characterization of EPO biotherapeutics and biosimilars.

      • Novel O-glycomic Characterization on Biotherapeutics by MS-based Approach

        Youngsuk Seo,Nayoung Yun,Myung Jin Oh,Gyeong Mi Park,Hyun Joo An 한국당과학회 2017 한국당과학회 학술대회 Vol.2017 No.01

        Glycan modifications of therapeutic glycoproteins influence on pharmacological functions including efficacy, safety, and biological activity. MS-based analytical tools for N-glycan chracterization have been intensively developed and now N-glycans including various variants (O-Acetylation, mannose-phosphates, and polylactosamines) on biotherapeutics are readily identified. However, there are few studies for the characterization of O-glycans because of the absence of analytical platform. Here, we have characterized novel O-glycosylation on therapeutic factor IX using nanoLC/MS and tandem MS. Interestingly, we could determine O-fucosylation and O-glucosylation as well as typical O-glycosylation having a core 1. Using tandem MS, we found that O-fucosylated glycans consisted of Fuc, GlcNAc, and Gal w/wo NeuAc while O-glucosylated glycans included Glc, Xyl, and Hex w/wo NeuAc. In addition the O-glycopeptide analysis showed that O-glucosylation and O-fucosylation were present at specific O-glycosylation sites of growth factor domain, respectively 53Ser and 61Ser. In previous studies the O-fucosylation of growth factor domain was known as an important factor to modulate signal transduction by the interaction with other proteins. Thus this study on the identification of O-glycan modifications could be useful for proving the correlation between glycosylation and drug efficacy.

      • Site-specific O-Glycosylation Characterization of Recombinant Coagulation Factor IX using LC-MS/MS

        Youngsuk Seo,Myung Jin Oh,Hyun Joo An 한국당과학회 2018 한국당과학회 학술대회 Vol.2018 No.01

        Recombinant coagulation factor IX (rFIX) is an extremely heterogeneous glycoprotein having multiple N-and O-glycosylation which influence on pharmacological functions including biological activity and in vivo stability. The study of glycosylation on rFIX has mainly focused on N-glycans due to an inherent complexity of O-glycosylation and the absence of analytical platform. Here, we comprehensively characterized the O-glycosylation on recombinant coagulation factor IX (rFIX) using MS-based glycomic and glycoproteomic approach. Briefly, O-glycans were chemically released using β-elimination while O-glycopeptides were prepared by pronase digestion to determine site-specific O-glycosylation distribution. Successfully we could identify unique O-glycosylation modifications such as O-fucosylation and O-glucosylation as well as a typical O-glycosylation on rFIX using nanoLC/MS and Tandem MS. Particularly, through O-glycopeptide analysis, we demonstrated that O-glucosylation and O-fucosylation were uniformly displayed on O-sites Serine 53 and 61 of EGF domain, respectively. While core 1-type O-glycosylations were overwhelmingly distributed across other O-sites (Threonine 159, 169, 172, and 179) in activation peptide of rFIX. Site-specific profiling including micro-and macro-heterogeneity could provide macroscopic aspect to figure out O-glycosylation pattern decorated on rFIX.

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