PXD037990 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Mapping the human chondroitin sulfate glycoproteome reveals an unexpected correlation between glycan sulfation and attachment site characteristics |
Description | Chondroitin sulfate proteoglycans (CSPGs), an important class of carbohydrate-modified proteins, are composed of chondroitin sulfate (CS) polysaccharide(s) attached to different core proteins. CS polysaccharides interact with a multitude of protein ligands to control key events in homeostasis and development. Much effort has been devoted to CS structural characterization, as the specificities of the interactions are considered to be determined by the distribution of sulfate groups along the polysaccharide chains. Owing to their structural complexity however, CS chains are typically characterized after they have been released from their core proteins, which precludes site-specific structural information. Such information would likely assist in assigning CSPG-related functions and provide insights to potential differences in CS structures for different core proteins and their glycosites. Here we utilize a novel glycoproteomic approach for the site-specific sequencing of CS modifications of CSPGs from human urine using a combination of biochemical enrichments, enzymatic digestions, and positive mode nano-scale liquid chromatography tandem mass spectrometry (nLC-MS/MS) analysis. Trypsin-derived CS-glycopeptides were partially depolymerized with chondroitinase ABC, yielding peptide-attached CS chains, ranging from 6 - 18 monosaccharides in length. Software-assisted- and manual analysis revealed that certain core proteins carried CS with abundant sulfate modifications, while others carried CS with lower levels of sulfation. Inspection of the amino acid sequences surrounding the attachment sites indicated that acidity of the attachment site motifs influenced the levels of CS sulfation and statistical analysis confirmed this relationship. These results demonstrate attachment site-specific CS polysaccharides of CSPGs in human urine and indicate that this novel method may assist in elucidating the biosynthesis and functional roles of CSPGs in cellular physiology. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_09:07:24.440.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Jonas Nilsson |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-11-07 09:00:18 | ID requested | |
1 | 2023-10-24 11:18:24 | announced | |
⏵ 2 | 2023-11-14 09:07:31 | announced | 2023-11-14: Updated project metadata. |
Publication List
Noborn F, Nilsson J, Sihlbom C, Nikpour M, Kjell, é, n L, Larson G, Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected Correlation Between Glycan Sulfation and Attachment Site Characteristics. Mol Cell Proteomics, 22(8):100617(2023) [pubmed] |
Keyword List
submitter keyword: glycosaminoglycans |
proteoglycans |
glycoproteomics |
glycopeptides |
Contact List
Fredrik Noborn |
contact affiliation | Department of Laboratory Medicine, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden. |
contact email | fredrik.noborn@clinchem.gu.se |
lab head | |
Jonas Nilsson |
contact affiliation | University of Gothenburg |
contact email | jonas.nilsson@clinchem.gu.se |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD037990
- Label: PRIDE project
- Name: Mapping the human chondroitin sulfate glycoproteome reveals an unexpected correlation between glycan sulfation and attachment site characteristics