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PXD048072 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleTargeted Proteomics Reveals Quantitative Differences in Low Abundance Glycosyltransferases of Patients with Congenital Disorders of Glycosylation
DescriptionProtein glycosylation is an essential posttranslational modification in all domains of life. Its impairment in human can result in severe diseases named Congenital Disorders of Glycosylation (CDGs). Most of the glycosyltransferases (GTs) responsible for proper glycosylation are polytopic membrane proteins that represent challenging targets in proteomics. We established a multiple reaction monitoring (MRM) assay to comprehensively quantify GTs involved in the processes of N-glycosylation, O- and C-mannosylation in the endoplasmic reticulum. High robustness was achieved by using an enriched membrane protein fraction of isotopically labeled HEK 293T cells as an internal protein standard. The analysis of primary skin fibroblasts from eight CDG type I patients with impaired ALG1, ALG2, or ALG11 genes revealed substantial reduction in the levels of corresponding proteins. The abundance of the other GTs, however, remained unchanged on transcript as well as on protein level, indicating that there is no fail-safe mechanism for this essential pathway. The established MRM assay is easily shared with the scientific community via the open source Skyline software environment, including Skyline Batch for automated data analysis. We demonstrate that another research group could easily reproduce all analysis steps even while using different LC-MS hardware.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterRoman Sakson
SpeciesList scientific name: Homo sapiens; NCBI TaxID: 9606;
ModificationListCarbamidomethyl; Label:13C(6)15N(2); Label:13C(6)15N(4)
InstrumentQTRAP 5500; nanoACQUITY UPLC; TSQ Vantage
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-12-22 01:06:48ID requested
12024-01-15 16:45:34announced
22024-01-30 09:16:22announced: Added PubMed Id
Publication List
Sakson R, Beedgen L, Bernhard P, Alp KM, L, ü, bbehusen N, R, ö, th R, Niesler B, Luzarowski M, Shevchuk O, Mayer MP, Thiel C, Ruppert T, Targeted Proteomics Reveals Quantitative Differences in Low-Abundance Glycosyltransferases of Patients with Congenital Disorders of Glycosylation. Int J Mol Sci, 25(2):(2024) [pubmed]
Keyword List
submitter keyword: N-glycosylation, glycosylation, endoplasmic reticulum, Congenital disorders of glycosylation
Contact List
Thomas Ruppert
contact affiliationCentre for molecular biology, Heidelberg University
contact emailt.ruppert@zmbh.uni-heidelberg.de
lab head
Roman Sakson
contact affiliationCentre for molecular biology, Heidelberg University (ZMBH)
contact emailroman.sakson@gmx.net
dataset submitter
Full Dataset Link List
Panorama Public dataset URI