Send to

Choose Destination
Proteomics. 2019 Aug 16:e1900010. doi: 10.1002/pmic.201900010. [Epub ahead of print]

Protein Paucimannosylation is an Enriched N-glycosylation Signature of Human Cancers.

Author information

S. Chatterjee, L. Y. Lee, R. Kawahara, J. L. Abrahams, M. Anugraham, C. Ashwood, Z. Sumer-Bayraktar, J. H.L. Chik, A. Everest-Dass, H. Hinneburg, I. Loke, E. S.X. Moh, M. Nakano, M. K. Sethi, K. Stavenhagen, K. Wongtrakul-Kish, M. P. Molloy, N. H. Packer, M. Thaysen-Andersen, Department of Molecular Sciences and Biomolecular Discovery and Design Research Centre (BDDRC), Macquarie University, Sydney, Australia.
L. Y. Lee, ISGlobal, Barcelona Centre for International Health Research (CRESIB), Hospital Clínic -Universitat de Barcelona, Barcelona, Spain.
R. Kawahara, G. Palmisano, Department of Parasitology, Institute of Biomedical Sciences, University of Sau Paulo, Brazil.
J. L. Abrahams, A. Everest-Dass, D. Kolarich, N. H. Packer, Institute for Glycomics, Griffith University, Gold Coast, Australia.
B. Adamczyk, N. G. Karlsson, Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
M. Anugraham, Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
C. Ashwood, Department of Biochemistry, Medical College of Wisconsin, Milwaukee, USA.
Z. Sumer-Bayraktar, School of Life and Environmental Sciences, Charles Perkins Centre (CPC), The University of Sydney, Sydney, Australia.
M. T. Briggs, P. Hoffmann, Future Industries Institute, Mawson Lakes Campus, University of South Australia, Adelaide, Australia.
J. H.L. Chik, International Collaboration On Repair Discoveries (ICORD), Vancouver Coastal Health Research Institute and Department of Pathology and Laboratory Medicine, The University of British Columbia, Vancouver, Canada.
S. Förster, M. H. Muders, Rudolf-Becker-Laboratory, Institute of Pathology, University Hospital Bonn, Bonn, Germany.
K. R.M. Leite, S. Recuero, M. Srougi, Laboratório de Investigação Médica da Disciplina de Urologia (LIM55), Faculdade de Medicina da FMUSP, Universidade de Sao Paulo, Sao Paulo, Brazil.
I. Loke, Department of Biological Sciences, National University of Singapore, Singapore.
U. Möginger, Institute for Biochemistry and Molecular Biology, University of Southern Denmark.
E. S.X. Moh, N. H. Packer, ARC Centre for Nanoscale Biophotonics, Macquarie University, Sydney, Australia.
M. Nakano, Graduate School of Advanced Sciences of Matter, Hiroshima University, Hiroshima, Japan.
M. K. Sethi, Center for Biomedical Mass Spectrometry, Department of Biochemistry, Boston University School of Medicine, Boston University, Boston, MA, USA.
K. Stavenhagen, Beth Israel Deaconess Medical Center, Department of Surgery and Harvard Medical School Center for Glycoscience, Harvard Medical School, Boston, MA, USA.
V. Venkatakrishnan, Department of Rheumatology & Inflammation Research, Institute of Medicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
K. Wongtrakul-Kish, Bioprocessing Technology Institute (BTI), A*STAR, Singapore, Singapore.
S. Diestel, Institute of Nutrition and Food Sciences, University of Bonn, Bonn, Germany.
M. P. Molloy, Sydney Medical School, Bowel Cancer and Biomarker Laboratory, Kolling Institute, The University of Sydney, Sydney, Australia.
M. K. Oehler, Department of Gynaecological Oncology, Royal Adelaide Hospital, Adelaide, Australia.


While aberrant protein glycosylation is a recognised characteristic of human cancers, advances in glycoanalytics continue to discover new associations between glycoproteins and tumourigenesis. 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 human cancers. The paucimannosidic glycans (PMGs) of 34 cancer cell lines and 133 tissue samples spanning 11 cancer types and matching non-cancerous specimens were profiled from 467 published and unpublished PGC-LC-MS/MS N-glycome datasets collected over a decade within our laboratories. PMGs, particularly Man2-3 GlcNAc2 Fuc1 , were prominent features of 29 cancer cell lines, but the PMG level varied dramatically across and within the investigated cancer types (1.0%-50.2%). Analyses of paired (tumour/non-tumour) and stage-stratified tissues demonstrated that PMGs are significantly enriched in tumour 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 was demonstrated on human glioblastoma cells using immunofluorescence while biosynthetic involvement of N-acetyl-β-hexosaminidase was 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 tumourigenesis and metastasis. This article is protected by copyright. All rights reserved.


Cancer; glycan; glycomics; paucimannosidic glycan; protein paucimannosylation


Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center