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Effects of high-mannose-type glycans of Maackia amurensis leukoagglutinin on sialic acid-binding activity

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2016 한국당과학회 동계학술대회 (2016.01)바로가기
  • 페이지
    pp.47-47
  • 저자
    Hye Seong Hwang, Heajin Park, Jihye Kim, Haesung Kim, Hyun Il Oh, Jai Yeon Choi, Ha Hyung Kim
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A294700

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원문정보

초록

영어
Maackia amurensis leukoagglutinin (MAL) is a glycoprotein and sialic acid-binding lectin that is used widely in the detection and characterization of sialoglycoconjugates and human cancer cells. However, its N-linked glycan structure and role have yet to be determined. The N-linked glycans were analyzed using high-performance liquid chromatography with matrix assisted laser desorption/ionization time-of-flight mass spectrometry, and the secondary structure was investigated using circular dichroismanalysis. A hemagglutination assay was performed. Furthermore, surface plasmon resonance analysis, and fluorescence microscopy and fluorescence-activated cell-sorting analysiswere conducted to assess the sialoglycoprotein-binding ability and its usefulness in the detection of human breast cancer MCF-7 cells, respectively. Analysis of the N-linked glycan structure ofMAL confirmed the presence of eight glycans, comprising two α1,3-fucosylated paucimannosidic-type and six high-mannose-type glycans. Glycan analysis of MAL that had been treated with peptide N-glycosidase F (de-M-MAL) revealed that while the two α1,3-fucosylated paucimannosidic glycans remained attached following the treatment, the six high-mannose-type glycans had been completely cleaved from the original MAL. There were almost no secondary structural changes between MAL and de-M-MAL; however, the lectin activities exhibited by MAL, such as hemagglutination and binding to a sialoglycoprotein, were completely absent in de-M-MAL, and the ability to detect human breast cancer MCF-7 cells was 77% lower in de-M-MAL than in MAL. The high-mannose-type glycans in intact MAL are closely associated with its lectin activities. This is the first report of the N-linked glycan structure of MAL and the effect of high mannose-type glycans on lectin activities.

저자

  • Hye Seong Hwang [ Biotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University ]
  • Heajin Park [ Biotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University ]
  • Jihye Kim [ Biotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University ]
  • Haesung Kim [ Biotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University ]
  • Hyun Il Oh [ Biotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University ]
  • Jai Yeon Choi [ Biotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University ]
  • Ha Hyung Kim [ Biotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University ]

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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