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PXD021985

PXD021985 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleMapping sites of carboxymethyllysine modification on proteins reveals consequences for proteostasis and cell proliferation
DescriptionPosttranslational mechanisms play a key role in modifying the abundance and function of cellular proteins. Among these, modification by advanced glycation end products (AGEs) has been shown to accumulate during aging and age-associated diseases but specific protein targets and functional consequences remain largely unexplored. Here, we devised a proteomic strategy to identify specific sites of carboxymethyllysine (CML) modification, one of the most abundant AGEs. We identified over 1000 sites of CML modification in mouse and primary human cells treated with the glycating agent glyoxal. By using quantitative proteomics, we found that protein glycation triggers a proteotoxic response and directly affects the protein degradation machinery. We show that glyoxal induces cell cycle perturbation of primary endothelial cells and that CML modification interferes with acetylation of tubulins and microtubule dynamics. Our data demonstrate the relevance of AGE modification for cellular function and pinpoints specific protein networks that might become compromised during aging.
HostingRepositoryPRIDE
AnnounceDate2021-11-25
AnnouncementXMLSubmission_2021-11-25_07:28:54.731.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAlessandro Ori
SpeciesList scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListiodoacetic acid derivatized residue
InstrumentQ Exactive HF-X
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-10-14 23:32:03ID requested
12021-11-25 07:28:55announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: advanced glycation end products, carboxymethyllysine, posttranslational modification, aging, proteasome, endothelial cell, cell cycle, tubulin, acetylation, mass spectrometry, liver, heart, kidney, glyoxal, mice, microtubules, mitosis
Contact List
Alessandro Ori
contact affiliationLeibniz Institute on Aging – Fritz Lipmann Institute (FLI), 07745 Jena, Germany
contact emailalessandro.ori@leibniz-fli.de
lab head
Alessandro Ori
contact affiliationLeibniz Institute on Aging
contact emailaleori@gmail.com
dataset submitter
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Dataset FTP location
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