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In-depth characterization of the xeno-antigen glycans on porcine aorta endothelial cells using LC/MS/MS

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2022 한국당과학회 연례학술대회 (2022.07)바로가기
  • 페이지
    pp.86-86
  • 저자
    Jong Hyun Yoon, Ji Eun Park, Myung Jin Oh, Hyun Joo An
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A415491

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원문정보

초록

영어
Xenotransplantation using porcine organs is a potential solution to bridge the gap between donors and recipients, but difference in glycosylation between humans and porcine limit successful clinical trials. Recent studies have shown that representative non-human glycan moieties such as galactose-α1,3-galactose(α-gal), NeuGc, and SDa antigens act as epitopes triggering antibody-mediated rejection (AMR). NeuGc leads to several inflammatory disorders and α-gal is known to cause more severe hypersensitivity reactions. Furthermore, it is essential to identify the glycan antigens adorned on the surface because endothelial cells interact first with the recipient's immune component during the xenotransplantation process. Despite the emphasis on the importance of glycans in the immune system, studies on comprehensive characterization of glycosylation including the structure of xeno-glycan antigens in porcine, a representative xenotransplantation model, are insufficient. Here, we performed overall glycan profiling and structural analysis of glycans with non-human moieties in porcine aorta endothelial cells. We could identify various glycan isomers and heterogeneity characteristics by accurate masses, retention times, LC/MS/MS, and exoglycosidase digestion. The major components were di-NeuAc-sialylated glycans in endothelial cells. In particular, non-human glycans, which can cause problems during transplantation, were present in a small amount less than 10%. NeuGc-sialylated glycan ratios in cell are around 4%, A glycosylated unique form in which sialic acid attached to antennal N-acetyl glucosamine (HexNAc) is identified in aorta endothelial cells. The α-gal containing glycans were confirmed by not only MS/MS spectra but also α-gal glycan removal using galactosidase that breaks gal α1-3 linkages at the terminal in LC/MS chromatogram. Our data could be the reference for monitoring changes in glycan antigens in glycoengineering models for xenotransplantation and providing information for mammalian glycome studies.

저자

  • Jong Hyun Yoon [ Graduate School of Analytical Science and Technology, Chungnam National University, Asia-Pacific Glycomics Reference Site, Daejeon, 34134, Korea ]
  • Ji Eun Park [ Graduate School of Analytical Science and Technology, Chungnam National University, Asia-Pacific Glycomics Reference Site, Daejeon, 34134, Korea ]
  • Myung Jin Oh [ Graduate School of Analytical Science and Technology, Chungnam National University, Asia-Pacific Glycomics Reference Site, Daejeon, 34134, Korea ]
  • Hyun Joo An [ Graduate School of Analytical Science and Technology, Chungnam National University, Asia-Pacific Glycomics Reference Site, Daejeon, 34134, Korea ] Corresponding Author

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    한국당과학회 [Korean Society for Glycoscience]
  • 설립연도
    2006
  • 분야
    의약학>약학
  • 소개
    본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.

간행물

  • 간행물명
    한국당과학회 학술대회
  • 간기
    연간
  • 수록기간
    2006~2022
  • 십진분류
    KDC 517 DDC 614

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