PXD014271

PXD014271 is an original dataset announced via ProteomeXchange.

Title	Protein paucimannosylation is a novel N-glycosylation signature of human cancers
Description	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 [Man1-3GlcNAc2Fuc0-1] and human cancers. The distribution of paucimannosidic glycans (PMGs) within the N-glycome of 34 cancer cell lines and 133 tissue samples spanning 11 prevalent cancer types and matching non-cancerous specimens were accurately determined from 467 PGC-LC-MS/MS datasets collected over a decade within our laboratories. PMGs, particularly the α1,6-fucosylated bi- and tri-mannosylated N-glycans, 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 tissue cohorts demonstrated that PMGs are significantly enriched in tumours from four cancer types including liver and colorectal cancer and increase with prostate cancer and chronic lymphocytic leukaemia progression. Cancer cell surface expression of paucimannosidic proteins was demonstrated using immunofluorescence while biosynthetic involvement of β-hexosaminidase was indicated by quantitative proteomics. The intriguing association between protein paucimannosylation and human cancers reported here warrants further exploration to detail the biosynthesis, cellular location(s), protein carriers and functions of paucimannosylation in tumourigenesis and metastasis.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:19:46.138.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Rebeca Kawahara
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-06-17 02:44:09	ID requested
1	2021-03-07 14:40:36	announced
⏵ 2	2024-10-22 05:19:47	announced	2024-10-22: Updated project metadata.

10.1002/pmic.201900010;

Chatterjee S, Lee LY, Kawahara R, Abrahams JL, Adamczyk B, Anugraham M, Ashwood C, Sumer-Bayraktar Z, Briggs MT, Chik JHL, Everest-Dass A, F, ö, rster S, Hinneburg H, Leite KRM, Loke I, M, ö, ginger U, Moh ESX, Nakano M, Recuero S, Sethi MK, Srougi M, Stavenhagen K, Venkatakrishnan V, Wongtrakul-Kish K, Diestel S, Hoffmann P, Karlsson NG, Kolarich D, Molloy MP, Muders MH, Oehler MK, Packer NH, Palmisano G, Thaysen-Andersen M, Protein Paucimannosylation Is an Enriched N-Glycosylation Signature of Human Cancers. Proteomics, 19(21-22):e1900010(2019) [pubmed]

submitter keyword: Cancer / glycomics / glycan / protein paucimannosylation / paucimannosidic glycan

Morten Thaysen-Andersen
contact affiliation	Department of Molecular Sciences, Macquarie University, Sydney, Australia
contact email	morten.andersen@mq.edu.au
lab head
Rebeca Kawahara
contact affiliation	Department of Molecular Sciences, Macquarie University, Sydney, NSW, Australia
contact email	rebecasakuma@gmail.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/03/PXD014271

PRIDE project URI

• PRIDE
  1. PXD014271
     1. Label: PRIDE project
     2. Name: Protein paucimannosylation is a novel N-glycosylation signature of human cancers