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ProteomicsOn-tissue spatially-resolved glycoproteomics guided by N-glycan imaging reveal global dysregulation of canine glioma glycoproteomic landscape
Here we present an approach to identify N-linked glycoproteins and deduce their spatial localization using a combination of MALDI N-glycan MSI and spatially-resolved glycoproteomics. We subjected glioma biopsies to on-tissue PNGaseF digestion and MALDI-MSI and found that the glycan HexNAc4-Hex5-NeuA...
ORGANISM(S): Canis familiaris (Dog) (Canis lupus familiaris) 
2022-05-04 | PXD025537 | Pride
Glioblastoma Spatially resolved glycoproteomics Glycoproteomics Glycan imaging Haptoglobin Sialic acid Spatially resolved glycoproteomicsglycan imaging Maldi-msi Hypersialylation 
ProteomicsRevealing the human cancer-associated mucinome
Mucin domains are densely O-glycosylated modular protein domains found in a wide variety of cell surface and secreted proteins. Mucin-domain glycoproteins are key players in a host of human diseases, especially cancer, but the scope of the mucinome remains poorly defined. Recently, we characterized ...
ORGANISM(S): Homo sapiens (Human) 
2022-06-29 | PXD024995 | Pride
Mucin Cancer Mucinase Proteomics Mucinome Mass spectrometry Glycoproteomics O-glycosylation 
ProteomicsQuantification and site-specific analysis of co-occupied N- and O-glycopeptides
Protein glycosylation is a complex post-translational modification that is generally classified as N- or O-linked. Site-specific analysis of glycopeptides is accomplished with a variety of fragmentation methods, depending on the type of glycosylation being investigated and the instrumentation availa...
ORGANISM(S): Homo sapiens (Human) 
2025-04-08 | PXD062628 | Pride
Mucin Glycoproteomics O-glycosylation Glycosylation N-glycosylation 
ProteomicsEye opening discoveries: uncovering lacritin glycoforms and the tear fluid glycoproteome
Tear fluid comprises a diverse group of extracellular glycoproteins which are critical for ocular homeostasis. Within the tear fluid glycoproteome, lacritin is highly expressed and plays a key role in immune response, tear secretion, and antimicrobial activity. Importantly, glycosylation constitutes...
ORGANISM(S): Homo sapiens (Human) 
2025-08-25 | PXD064788 | Pride
Glycoproteomics Mucin Mucinase Lacritin Mass spectrometry Immunoglobulin a Tear fluid 
ProteomicsGlycoproteoforms of osteoarthritis-associated lubricin in plasma and synovial fluid
Lubricin or proteoglycan-4 (PRG-4) is a mucinous glycoprotein that lubricates the cartilage and maintains normal tissue function and cell homeostasis. Altered O- glycoproteforms of lubricin have been found in osteoarthritis (OA) synovial fluid (SF), which could ostensibly be used as a biomarker to...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD055049 | Pride
Human Oa Lc-ms Synovial fluid Plasma Lubricin 
ProteomicsGlycosite Mapping and in situ Mass Spectrometry Imaging of MUC2 Glycopeptides via On-slide Mucinase Digestion
Aberrant mucin expression and glycosylation are hallmarks of cancer, but how these changes promote malignant processes are not well understood. Solid tumors are highly heterogeneous in their cellular and molecular composition, and many advanced spatial techniques have emerged in recent years to stud...
ORGANISM(S): Homo sapiens (Human) 
2026-04-06 | PXD055865 | Pride
ProteomicsGalectin-3 binds isoform- and glycoform-specific lacritin in tear fluid
Galectin-3 (Gal-3) is a carbohydrate-binding protein which plays crucial roles in inflammation, immune response, cell migration, autophagy, and signaling. At the ocular surface, Gal-3 is also known to crosslink transmembrane mucins across the epithelial cell glycocalyx, forming lattice structures im...
ORGANISM(S): Homo sapiens (Human) 
2026-04-22 | PXD071066 | Pride
Lc-ms/ms Galectin-3 Tear fluid 
ProteomicsGlycosite mapping and structural dynamics of TIM family immune checkpoints enabled by mucinase SmE
Mucin-domain glycoproteins are densely O-glycosylated and play key roles in a host of biological functions. In particular, the T-cell immunoglobulin and mucin-domain containing family of proteins (TIM-1, 3, 4) decorate immune cells and act as key checkpoint inhibitors in cancer. However, their dense...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-09-27 | PXD039583 | Pride
O-glycoprotein Tim-1 Cancer Mucinase Tim-4 Tim-3 O-glycosylation Immune checkpoint T-cell immunoglobulin and mucin-domain containing Lc-ms/ms Molecular dynamics Mucinome Mucin O-glycoproteomics Mucin domain Checkpoint inhibitor O-glycoprotease 
ProteomicsFalse positive glycopeptide identification through in-FAIMS glycan fragmentation.
Glycosylation is an important post-translational modification characterized by extensive heterogeneity. While mass spectrometry (MS) is the premier technique to characterize glycoproteins, the study of intact glycopeptides presents challenges often not observed in the study of unmodified species. Hi...
ORGANISM(S): Homo sapiens (Human) 
2023-09-11 | PXD041217 | Pride
Glycoproteomics Mucinomics faims Mucin-domain glycoproteomics Enrichment. Ion mobility separation 
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