Article open access publication

Protein Paucimannosylation Is an Enriched N‐Glycosylation Signature of Human Cancers

Proteomics, Wiley, ISSN 1615-9853

Volume 19, 21-22, 2019

DOI:10.1002/pmic.201900010, Dimensions: pub.1120337611, PMID: 31419058,



  1. (1) Macquarie University, grid.1004.5
  2. (2) Hospital Clinic of Barcelona, grid.410458.c
  3. (3) University of Sao Paulo, grid.11899.38
  4. (4) Griffith University, grid.1022.1
  5. (5) University of Gothenburg, grid.8761.8
  6. (6) Institute of Biological Chemistry, Academia Sinica, grid.506934.d
  7. (7) Medical College of Wisconsin, grid.30760.32
  8. (8) University of Sydney, grid.1013.3
  9. (9) University of South Australia, grid.1026.5
  10. (10) University of British Columbia, grid.17091.3e
  11. (11) Rudolf‐Becker‐Laboratory, Institute of Pathology, University Hospital Bonn, Bonn, 53127, Germany
  12. (12) National University of Singapore, grid.4280.e
  13. (13) University of Southern Denmark, grid.10825.3e, SDU
  14. (14) Hiroshima University, grid.257022.0
  15. (15) Boston University School of Medicine, grid.475010.7
  16. (16) Beth Israel Deaconess Medical Center, Department of Surgery and Harvard Medical School Center for Glycoscience, Harvard Medical School, Boston, MA, 02215, USA
  17. (17) Bioprocessing Technology Institute, grid.452198.3
  18. (18) University of Bonn, grid.10388.32
  19. (19) Royal North Shore Hospital, grid.412703.3
  20. (20) Royal Adelaide Hospital, grid.416075.1


While aberrant protein glycosylation is a recognized characteristic of human cancers, advances in glycoanalytics continue to discover new associations between glycoproteins and tumorigenesis. This glycomics-centric study investigates a possible link between protein paucimannosylation, an under-studied class of human N-glycosylation [Man1-3 GlcNAc2 Fuc0-1 ], and cancer. The paucimannosidic glycans (PMGs) of 34 cancer cell lines and 133 tissue samples spanning 11 cancer types and matching non-cancerous specimens are profiled from 467 published and unpublished PGC-LC-MS/MS N-glycome datasets collected over a decade. PMGs, particularly Man2-3 GlcNAc2 Fuc1 , are prominent features of 29 cancer cell lines, but the PMG level varies dramatically across and within the cancer types (1.0-50.2%). Analyses of paired (tumor/non-tumor) and stage-stratified tissues demonstrate that PMGs are significantly enriched in tumor tissues from several cancer types including liver cancer (p = 0.0033) and colorectal cancer (p = 0.0017) and is elevated as a result of prostate cancer and chronic lymphocytic leukaemia progression (p < 0.05). Surface expression of paucimannosidic epitopes is demonstrated on human glioblastoma cells using immunofluorescence while biosynthetic involvement of N-acetyl-β-hexosaminidase is indicated by quantitative proteomics. This intriguing association between protein paucimannosylation and human cancers warrants further exploration to detail the biosynthesis, cellular location(s), protein carriers, and functions of paucimannosylation in tumorigenesis and metastasis.


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