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PXD022415 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleMilk glycopeptide across lactation
DescriptionProtein N-glycosylation is an essential post-translational modification (PTM) frequently occurring on human milk proteins. These PTMs assist in protecting the infant's health and function amongst others as competitive inhibitors of pathogen binding and immunomodulators. Due to the individual uniqueness of each mother’s milk and the overall complexity and temporal changes of protein N-glycosylation, analysis of the human milk N-glycoproteome requires longitudinal personalized approaches, providing protein- and N-site-specific quantitative information. Here we describe an automated platform using HILIC-based cartridges enabling the proteome-wide monitoring of N-glycopeptides using just 150 μg of breast milk protein digestion. Reproducibility in enrichment and quantitation is demonstrated in triplicate measurements of milk samples taken along an extended lactation period. Using higher energy c-trap dissociation (HCD) triggered electron-transfer higher-energy collision dissociation (EThcD), we were able to map around 1700 glycopeptides from 110 glycoproteins occurring on 191 glycosites, of which 43 sites were not before reported with experimental evidence. We next quantified many of these glycopeptides using a targeted proteomics approach with scheduled selective ion monitoring (SIM) and parallel reaction monitoring (PRM). In a 90 min gradient, we could quantitatively monitor 318 glycopeptides originating from 51 glycoproteins. Although each glycoprotein, each N-glycosylation site and each glycan attached revealed its own dynamic changes, we did observe a few general trends. Overall fucosylation especially terminal fucosylation increased across the lactation period.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportsupported by repository but incomplete data and/or metadata
PrimarySubmitterJing Zhu
SpeciesList scientific name: Homo sapiens; NCBI TaxID: 9606;
ModificationListHex(9)HexNAc(2); dHex(1)Hex(3)HexNAc(4); dHex(1)Hex(4)HexNAc(3)NeuAc(1); Hex(4)HexNAc(3)NeuAc(1); dHex(1)Hex(4)HexNAc(4)NeuAc(1); Oxidation; dHex(2)Hex(4)HexNAc(4); Hex(4)HexNAc(4)NeuAc(1); dHex(1)Hex(4)HexNAc(5); Carbamidomethyl; Hex(5)HexNAc(3); dHex(1)Hex(5)HexNAc(3); dHex(1)Hex(4)HexNAc(3)NeuGc(1); Hex(5)HexNAc(4); dHex(1)Hex(5)HexNAc(4); dHex(1)Hex(5)HexNAc(4)NeuAc(1); dHex(1)Hex(5)HexNAc(4)NeuAc(2); dHex(2)Hex(5)HexNAc(4); Hex(5)HexNAc(4)NeuAc(1); Hex(5)HexNAc(4)NeuAc(2); Hex(5)HexNAc(5); dHex(1)Hex(5)HexNAc(5); Hex(6)HexNAc(2); Hex(6)HexNAc(3); Hex(7)HexNAc(2); Hex(4)HexNAc(4); dHex(1)Hex(4)HexNAc(4); Hex(5)HexNAc(2); dHex(1)Hex(3)HexNAc(3); dHex(2)Hex(3)HexNAc(3); Hex(8)HexNAc(2); dHex(1)Hex(3)HexNAc(5); Label:13C(6)15N(2); Label:13C(6)15N(4)
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-11-06 20:50:32ID requested
12020-11-07 07:41:17announced
Publication List
Zhu J, Lin YH, Dingess KA, Mank M, Stahl B, Heck AJR, -Glycoproteome of Human Milk from a Single Donor Reveals the Highly Variable Repertoire and Dynamic Site-Specific Changes. J Proteome Res, 19(5):1941-1952(2020) [pubmed]
Keyword List
submitter keyword: Human milk
Contact List
Albert J.R. Heck
contact affiliationAlbert J.R. Heck
contact emaila.j.r.heck@uu.nl
lab head
Jing Zhu
contact affiliationJing Zhu
contact emailj.zhu@uu.nl
dataset submitter
Full Dataset Link List
Panorama Public dataset URI