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PXD041212-2

PXD041212 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleGlycated bovine serum albumin for use in animal models – in vitro methodology and characterization of a glycated substrate for feeding trials
DescriptionAdvanced Glycation End-Products (AGEs) are a heterogeneous group of compounds resulting from the non-enzymatic condensation between reducing sugars and amino groups, primarily lysine and arginine moieties (Perrone et al., 2020). The in vivo glycation of proteins is part of normal metabolism, but pathological implications, as well as molecular aging (e.g. protein conformation changes, inflammaging), have been associated with its occurrence (Briceno Noriega et al., 2022). In addition to the important deleterious effects of the endogenous formation of AGEs, the amount acquired from the diet is the subject of concern. In industrial or household cooking processes, the development of appealing aromas, flavors, and colors goes hand-in-hand with the formation of dietary AGEs (dAGEs) (Lund & Ray, 2017). It is well documented that thermally processed foods are a key dietary source of these neo-formed compounds, and high exposure to dAGEs has been associated with the pathogenesis of chronic non-communicable diseases (e.g. diabetes, obesity, and heart failure) (Clarke et al., 2016). Endogenous and dAGEs are thought to exert their pro-inflammatory and pro-oxidative effects at least in part through binding with the Receptor for Advanced Glycation End-products (RAGE) (Nogueira Silva Lima et al., 2021). Our goal here was to compare the efficiency of different reducing agents and carbonyl compounds for dCML fortification of bovine serum albumin (BSA) using a novel combination of quantitative and qualitative methods. Isotope-dilution, high-performance liquid chromatography with tandem mass spectrometric detection (HPLC-MS/MS), western-blot, fluorescence, and proteomics analyses using matrix-assisted laser desorption ionization with time-of-flight MS (MALDI-TOF) and LC with high-resolution MS (LC-HRMS) were all employed to provide an extensive characterization of the possible modifications of BSA promoted by different carbonyl compounds. We further studied the efficiency of the incorporation of protein-bound dCML into mouse feed pellets, their stability over different storage periods, as well as clearance of dCML in mouse feces.
HostingRepositoryPRIDE
AnnounceDate2023-11-14
AnnouncementXMLSubmission_2023-11-14_07:02:26.280.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterBRAY FABRICE
SpeciesList scientific name: Bos taurus (Bovine); NCBI TaxID: 9913;
ModificationListN6-formyl-L-lysine; N6-carboxymethyl-L-lysine; monohydroxylated residue; deaminated residue; iodoacetic acid derivatized residue
InstrumentQ Exactive Plus
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-03-30 06:00:12ID requested
12023-07-06 08:34:09announced
22023-11-14 07:02:26announced2023-11-14: Updated project metadata.
32024-10-22 05:52:20announced2024-10-22: Updated project metadata.
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: carboxymethyllysine, glycation, proteomics, mass spectrometry, glyoxal, BSA
Contact List
fabrice bray
contact affiliationMSAP UAR 3290 CNRS Bâtiment C4 Avenue Paul Langevin Cité Scientifique 59655 Villeneuve D'ascq 03 20 33 71 12 https://msap-lab.fr/
contact emailfabrice.bray@univ-lille.fr
lab head
BRAY FABRICE
contact affiliationMSAP USR 3290
contact emailfabrice.bray@univ-lille.fr
dataset submitter
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