PXD032812

PXD032812 is an original dataset announced via ProteomeXchange.

Title	Proteomic Analysis of Methylglyoxal Modifications Reveals Susceptibility of Glycolytic Enzymes to Dicarbonyl Stress
Description	Methylglyoxal (MGO) is a highly reactive cellular metabolite that glycates lysine and arginine residues to form post-translational modifications known as advanced glycation end products. Because of their low abundance and low stoichiometry, few studies have reported their occurrence and site-specific locations in proteins. Proteomic analysis of WIL2-NS B lymphoblastoid cells in the absence and presence of exogenous MGO was conducted to investigate the extent of MGO modi-fications. We found over 500 MGO modified proteins, revealing an over-representation of these modifications on many glycolytic enzymes, as well as ribosomal and spliceosome proteins. Moreover, MGO modifications were observed on the active site residues of glycolytic enzymes that could alter their activity. We similarly observed modification of glycolytic enzymes across several epithelial cell lines and peripheral blood lymphocytes, with modification of fructose bisphosphate aldolase being observed in all samples. These results indicate that glycolytic proteins could be particularly prone to the formation of MGO adducts.
HostingRepository	PRIDE
AnnounceDate	2022-05-20
AnnouncementXML	Submission_2022-05-20_09:32:51.035.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Leigh Donnellan
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	N6-1-carboxyethyl-L-lysine; methylglyoxal arginine adduct (+54 amu)
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2022-03-25 05:14:59	ID requested
⏵ 1	2022-05-20 09:32:51	announced

Donnellan L, Young C, Simpson BS, Dhillon VS, Costabile M, Hoffmann P, Fenech M, Deo P, Methylglyoxal Impairs Sister Chromatid Separation in Lymphocytes. Int J Mol Sci, 23(8):(2022) [pubmed]

submitter keyword: Post-translational modifications, methylglyoxal, glycation, LC-MS/MS

Permal Deo
contact affiliation	Clinical and Health Sciences, Health and Biomedical Innovation , University of South Australia, Adelaide 5000, Australia
contact email	permal.deo@unisa.edu.au
lab head
Leigh Donnellan
contact affiliation	Univeristy of South Australia
contact email	leigh.donnellan@unisa.edu.au
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD032812
     1. Label: PRIDE project
     2. Name: Proteomic Analysis of Methylglyoxal Modifications Reveals Susceptibility of Glycolytic Enzymes to Dicarbonyl Stress