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Branched I antigen regulated cell susceptibility against natural killer cytotoxicity through its N-linked glycosylation and overall expression.

Authors
  • Wu, Yu-Xuan1
  • Lu, Hsu-Feng2, 3
  • Lin, Yen-Hsi1, 4
  • Chuang, Hui-Yu1
  • Su, Shih-Chi5, 6
  • Liao, Yi-Jen7
  • Twu, Yuh-Ching1
  • 1 Department of Biotechnology and Laboratory Science in Medicine, National Yang-Ming University, Taipei, Taiwan. , (Taiwan)
  • 2 Department of Clinical Pathology, Cheng Hsin General Hospital, Taipei, Taiwan. , (Taiwan)
  • 3 Department of Restaurant, Hotel and Institutional Management, Fu-Jen Catholic University, New Taipei, Taiwan. , (Taiwan)
  • 4 Department of Clinical Laboratory, Chung Shan Medical University Hospital, Taichung, Taiwan. , (Taiwan)
  • 5 Whole-Genome Research Core Laboratory of Human Diseases, Chang Gung Memorial Hospital, Keelung, Taiwan. , (Taiwan)
  • 6 Central Research Laboratory, Xiamen Chang Gung Hospital, Xiamen, China. , (China)
  • 7 School of Medical Laboratory Science and Biotechnology, College of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan. , (Taiwan)
Type
Published Article
Journal
Glycobiology
Publisher
Oxford University Press
Publication Date
Jan 05, 2021
Identifiers
DOI: 10.1093/glycob/cwaa117
PMID: 33403394
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Cell surface glycosylation has been known as an important modification process that can be targeted and manipulated by malignant cells to escape from host immunosurveillance. We previously showed the blood group branched I antigen on the leukemia cell surface can regulate the cell susceptibility against natural killer (NK) cell-mediated cytotoxicity through interfering target-NK interaction. In this work, we first identified N-linkage as the major glycosylation linkage type for branched I glycan formation on leukemia cells, and this linkage was responsible for cell sensitivity against therapeutic NK-92MI targeting. Secondly, by examining different leukemia cell surface death receptors, we showed death receptor Fas had highest expressions in both Raji and TF-1a cells. Mutations on two Fas extracellular N-linkage sites (118 and 136) for glycosylation impaired activation of Fas-mediated apoptosis during NK-92MI cytotoxicity. Last, we found that the surface I antigen expression levels enable leukemia cells to respond differently against NK-92MI targeting. In low I antigen expressing K-562 cell, reduction of I antigen presence greatly reduced leukemia cell susceptibility against NK-92MI targeting. But in other high I antigen expressing leukemia cells, similar reduction in I antigen expression did not affect cell susceptibility. © The Author(s) 2021. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: [email protected]

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