Hyun Joo An

Chungnam National University

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Carlito B. Lebrilla

University of California, Davis

Jae‐Han Kim

Chungnam National University

Myung Jin Oh

Chungnam National University

Serenus Hua

Moderna Therapeutics (United States)

Nari Seo

Korea Information System (South Korea)

변

변명우

Jong Shin Yoo

Korea Basic Science Institute

윤

윤수현

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Süreyya Özcan

Middle East Technical University

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박경진

Cooperative Institutions

Chungnam National University

166

University of California, Davis

107

Seoul National University

Princeton University

Yonsei University

Korea Basic Science Institute

Korea University

Sungkyunkwan University

Korea Advanced Institute of Science and Technology

Korea Research Institute of Bioscience and Biotechnology

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Analytical platform for glycomic characterization of recombinant erythropoietin biotherapeutics and biosimilars by MS

Bioanalysis (2013)

Myung Jin Oh Serenus Hua Bum Jin Kim Ha Neul Jeong Seung Hyup Jeong

Erythropoietin is a therapeutic glycoprotein that stimulates red blood cell production. The quality, safety and potency of recombinant erythropoietins are determined largely by their glycosylation. Small variations in cell culture conditions can significantly affect the glycosylation, and therefore the efficacy, of recombinant erythropoietins. Thus, detailed glycomic analyses are necessary to assess biotherapeutic quality. We have developed a platform for qualitative and quantitative glycomic analysis of recombinant erythropoietins.The platform was used to profile native N-glycans from three production batches of darbepoetin alfa (also known as NESP), a common form of recombinant erythropoietin. Darbepoetin alfa was found to contain an abundance of large, multi-antennary N-glycans with high levels of sialylation, O-acetylation and dehydration. Results were verified by independent orthogonal analysis with both MALDI-TOF and nano-LC/Q-TOF MS.This platform may be applied to QC and batch analysis of not only recombinant erythropoietin, but also other complex, glycosylated biotherapeutics and biosimilars.

Biosimilar

Darbepoetin alfa

10.4155/bio.12.327

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Glycosylated proteins preserved over millennia: N-glycan analysis of Tyrolean Iceman, Scythian Princess and Warrior

Scientific Reports (2014)

Süreyya Özcan Bum Jin Kim Grace S. Ro Jae‐Han Kim Thomas Bereuter

An improved understanding of glycosylation will provide new insights into many biological processes. In the analysis of oligosaccharides from biological samples, a strict regime is typically followed to ensure sample integrity. However, the fate of glycans that have been exposed to environmental conditions over millennia has not yet been investigated. This is also true for understanding the evolution of the glycosylation machinery in humans as well as in any other biological systems. In this study, we examined the glycosylation of tissue samples derived from four mummies which have been naturally preserved: – the 5,300 year old “Iceman called Oetzi”, found in the Tyrolean Alps; the 2,400 year old “Scythian warrior” and “Scythian Princess”, found in the Altai Mountains; and a 4 year old apartment mummy, found in Vienna/Austria. The number of N-glycans that were identified varied both with the age and the preservation status of the mummies. More glycan structures were discovered in the contemporary sample, as expected, however it is significant that glycan still exists in the ancient tissue samples. This discovery clearly shows that glycans persist for thousands of years and these samples provide a vital insight into ancient glycosylation, offering us a window into the distant past.

10.1038/srep04963

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하지 심부 정맥 혈젅ㅇ에서 하대 정맥 필터 삽입술

윤정철 최기용 Hyun Joo An 서은정 김광준

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아시아 하계 몬순 지역의 계절내 변동 및 장마 현상

한국기상학회 학술대회 논문집 (1997)

Hyun Joo An 박순웅

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Antimicrobial Agents and Chemotherapy

Science (1966)

Hyun Joo An

Antimicrobial chemotherapy

Anti-Infective Agents

10.1126/science.152.3718.108.b

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Citations (260)

조선시대 임진왜란 이전 전라도의 서적출판에 관한 고찰

서지학연구 (2010)

Hyun Joo An

이 연구에서는 조선시대 임진왜란 이전의 전남지역의 출판문화를 파악하는데 목표를 두고, 서목을 작성하여 시기별, 간행지역별, 주제별, 편저자별 분석을 시도하였다. 전남지역에서는 156종의 서적을 간행하였으며, 명종조 이후부터 서적의 간행이 활발하였다. 또한 현존본들의 간기를 통해 서적의 대부분이 관판본으로 간행되었음을 알 수 있다. 간행의 주도자들은 관찰사, 목사, 현감 등 지방관들이었고, 간행된 서적의 주요저자는 주희, 김안국, 이정, 이황, 당대의 명현들이었다. 광주목, 나주목, 순천부, 능성현, 담양부 등이 주요 간행지였으며, 이들은 당시 행정의 중심지였다. 주제별로는 유가류, 별집류, 소학류, 총집류, 예술류, 전기류, 의가류, 사서류, 예류, 병가류의 서적이 많이 간행되었다.

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Analysis of secretome and N-glycosylation of Chlorella species

Algal Research (2021)

Juyoung Choi Jun‐Hye Shin Hyun Joo An Myung Jin Oh Seong‐Ryong Kim

Chlorella vulgaris

10.1016/j.algal.2021.102466

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Biopurification of Oligosaccharides by Immobilized Kluyveromyces Lactis

Applied Sciences (2019)

In‐Seok Yeo Yeojin Yoon Nari Seo Hyun Joo An Jae‐Han Kim

Oligosaccharides with diverse and complex structures such as milk oligosaccharides have physiological functions including modulating intestinal microbiota or stimulating immune cell responses. However, milk carbohydrates include about 40–50% of lactose which requires a cost-effective method to separate. We developed a new method to purify the oligosaccharides from carbohydrate mixtures such as human milk oligosaccharides (HMOs) and galactooligosaccharides (GOSs) by exploiting immobilized Kluyveromyces lactis as microbial catalysts. Evaluation of media components exhibited no significant differences in the lactose removal efficiency when nutrient-rich media, minimal salt media, and distilled water without any media components were used. With the immobilization on alginate beads, the lactose removal efficiency was increased 3.4 fold compared to that of suspension culture. When the immobilized cells were reused to design a continuous process, 4 h of pre-activation enhanced the lactose eliminating performance 2.5 fold. Finally, immobilized K. lactis was used as microbial catalysts for the biopurification of HMOs and GOSs, and lactose was effectively removed without altering the overall distribution of oligosaccharides.

Kluyveromyces lactis

Oligosaccharide

Prebiotic

10.3390/app9142845

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Abstract 2316: Therapeutic targeting of novel human stem cell and cancer associated glycans

Cancer Research (2011)

Mary R. Saunders Hyun Joo An David J. Olivos Yoshiko Maeda Ryan G. Lim

Abstract Host and tumor surface glycans are important in regulating pivotal pathophysiological events during the development of cancer and tumor progression. Changes in glycosylation allow tumorigenic cells to seize control over developmental processes which allow cells to proliferate, invade, promote angiogenesis, and metastasize. Malignant transformation is accompanied by the expression of oncofetal antigens which are expressed on embryonic cells, tumor cells, and a few adult cells. Glycans common to human embryonic stem cells and cancer cells can be targeted using combinatorial chemistry. Several peptidomimetic ligands have been discovered using One Bead One Compound (OBOC) and One Bead Two Compound (OB2C) methods. These cell adhering ligands possess the potential to target tumorigenic cells and mediate intracellular signaling events by binding to high mannose glycans expressed on the surface of Jurkat, TK6, Her2 expressing MCF7, chemoresistant MCF7, HeLa, and SiHa cell lines. Three lead linear peptides with alternating natural and unnatural amino acids have been investigated for their in vivo targeting potential in the lymphoid leukemia, breast, and cervical cancer mouse xenograph models. In vitro and in vivo stem and cancer cell experiments, which demonstrate genetically altered glycan function, are currently being investigated for their anticancer potential. These novel agents may be used alone or in combination with chemoradiation and anti-angiogenesis strategies for treating cancer. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 2316. doi:10.1158/1538-7445.AM2011-2316

Jurkat cells

10.1158/1538-7445.am2011-2316

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Supplementary Figures S1-S12 and Supplementary Tables S1-S3 from Novel Glycosylated VEGF Decoy Receptor Fusion Protein, VEGF-Grab, Efficiently Suppresses Tumor Angiogenesis and Progression

Jung‐Eun Lee Chan Kim Hannah Yang Intae Park Nuri Oh

<p>Supplementary Figure S1. Sequence Alignment of VEGF-Grab1, VEGF-Grab3, and VEGF-Trap; Supplementary Figure S2. Analysis of N-linked Glycosylation for VEGF-Grabs and VEGF-Trap; Supplementary Figure S3. Analysis of O-linked Glycosylation in VEGF-Grab1; Supplementary Figure S4. VEGF-Grab3 displays low binding to tumor ECM; Supplementary Figure S5. Pharmacokinetic profile of VEGF-Grab1 and VEGF-Grab3; Supplementary Figure S6. Tissue accumulation of VEGF-Trap and VEGF-Grab3; Supplementary Figure S7. VEGF-Grabs or VEGF-Trap have no effects on VEGFR2 signalling, EC survival, migration, and tube formation in the absence of VEGFA; Supplementary Figure S8. Dose-dependent Inhibition of VEGFR2 Signalling with Anti-VEGF Therapy; Supplementary Figure S9. Histologic Analyses of Vital Organs after Anti-VEGF Therapy; Supplementary Figure S10. VEGF-Grab effectively suppresses the growth of established bulky macroscopic tumors; Supplementary Figure S11. Histological analyses of the kidney and liver after dose dependent anti-VEGF therapy; Supplementary Figure S12. Combination Therapy of VEGF-Grab3 and Cisplatin Enhances Intratumoral Apoptosis; Supplementary Table S1. Primer sequences for site-directed mutagenesis; Supplementary Table S2. Primer sequences for Quantitative Real Time PCR; Supplementary Table S3. Antibodies.</p>

10.1158/1535-7163.22504209.v1

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