STEAMM study
Ontology highlight
ABSTRACT:
PROVIDER: PRJEB83973 | ENA |
REPOSITORIES: ENA
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Project description:Thermal treatments used in Ultra-Processed Foods (UPFs) lead to advanced glycation end products (AGEs) in food products. UPFs and serum AGEs are both associated with cardiometabolic disease. We explored differential cooking methods as a mechanistic link between UPFs and detrimental health outcomes. We performed a randomized cross-over cooking method trial in healthy subjects provided with identical ingredients.
2025-01-24 | PXD059624 | Pride
Project description:Transcriptome analysis of Advanced glycation end products treated ligament cells
| PRJNA275546 | ENA
Project description:Advanced 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.
2023-07-06 | PXD041212 | Pride
Project description:Podocyte dysfunction is considered as the main contributor to the development and progression of diabetic kidney disease(DKD).High glucose(HG)or advanced glycation end products (AGEs) can lead to podocyte dysfunction.To explore the the molecular mechanism of podocyte dysfunction, we screened the mRNA expression profiles of podocytes treated with HG(50mmol/L)and AGEs(400µg/mL) through transcriptomics.
2024-12-31 | GSE236426 | GEO
Project description:Glyoxalase 1 (Glo1) is a critical enzyme responsible for the clearance of toxic dicarbonyls, which modify proteins to produce advanced glycation end products (AGEs). Glo1 has been recently implicated in the progression of metabolic disorders, however underlying mechanisms are poorly understood. We aim to investigate the role of Glo1 in metabolic perturbations and determine whether AGEs mediate the Glo1 activities in obesity and metabolic health.
2018-08-03 | GSE118034 | GEO
Project description:Descriptive Transcriptome Analysis of Tendon Derived Fibroblasts Following In-Vitro Exposure to Advanced Glycation End Products
| PRJNA842004 | ENA
Project description:Non-enzymatic reactions in glycolysis lead to the accumulation of methylglyoxal (MGO), a reactive precursor to advanced glycation end-products (AGEs), which has been hypothesized to drive obesity and aging-associated pathologies. A combination of nicotinamide, lipoic acid, thiamine, pyridoxamine, and piperine (Gly-Low), was identified to lower glycation by reducing MGO and MGO-derived AGE, MG-H1, in mice. Administration of Gly-Low reduced food consumption, lowered body weight, improved insulin sensitivity, and increased survival in both leptin receptor-deficient (Leprdb) and wild-type C57B6/J mice. Unlike caloric restriction, Gly-Low modulated hypothalamic signaling by upregulating mTOR pathway signaling to inhibit ghrelin-mediated hunger response. Gly-Low also slowed hypothalamic aging and increased survival when administered as a late-life intervention, suggesting its potential benefits in ameliorating age-associated decline by inducing voluntary caloric restriction and reducing glycation.
2025-02-28 | GSE234483 | GEO
Project description:Glycation is a post-translational modification underlied by the interaction of protein amino and guanidino groups with carbonyl compounds like reducing sugars and α-dicarbonyls. In the first steps of this process, the protein amino groups react with reducing carbohydrates yielding the corresponding keto- and aldimines, i.e. Amadori and Heyns compounds, respectively. Further degradation of these products results in the formation of advanced glycation end products (AGEs). Alternatively, some representatives of this heterogeneous compound group can originate from α-dicarbonyl products of monosaccharide autoxidation or primary cellular metabolism. In mammals, AGEs are continuously formed during the life of the organism, and accumulate in the tissues, being well-known markers of ageing and impacting age-related stiffing of tissues, decrease of muscle performance, and atherosclerotic changes. However, although the role of AGEs in the ageing of animal tissues is well-studied, their impact in the age-related molecular alterations in plants is completely unknown. To fill this gap, we present here a comprehensive study of the age-related changes in the plant glycated proteome in terms of affected proteins and individual glycation sites therein. Thereby, we consider the qualitative and quantitative changes in glycation patterns in terms of the general metabolic background, pathways of AGE formation, and the status of plant anti-oxidative/anti-glycative defense. Although the patterns of glycated proteins were only minimally influenced by plant age, the abundances of 96 advanced glycation sites in 71 proteins were significantly affected in an age-dependent manner and clearly indicate the existence of glycation hotspots in the plant proteome, the nature of which is discussed here in the sense of structural considerations.
2017-06-19 | PXD006434 | Pride
Project description:Protein glycation is a type of post-translational modification (PTM) involving complex non-enzymatic reactions of reducing sugars or reactive dicarbonyls with proteins, generating a heterogeneous group of advanced glycation end-products (AGEs) such as carboxymethyllysine (CML). In bottom-up proteomics, 2-iodoacetamide (IAA) is the most commonly used reagent for cysteine alkylation before trypsin digestion, which exogenously gives a carbamidomethylation (CAM) group on the side chain of cysteine residue. However, offisite alkylation of IAA can occur at the protein N-terminus and other amino acid residues such as lysine residue. Here, for the first time, we provided evidence that IAA alkylation can result in false-positive identifications of CML, and N-isopropylacrylamide (NIPAM) can be used as an IAA alternative to avoid these pitfalls.
2023-01-24 | PXD032235 | Pride
Project description:Diabetes is one of the major risk factors for Alzheimer’s disease (AD) development. The role of elevated levels of glucose, methylglyoxal (MGO), and advanced glycation end products (AGEs) in diabetes in the pathogenesis of the AD is not well understood. In this pursuit, we studied the role of methylglyoxal in the pathogenesis of AD in rat models. The elevated plus-maze (EPM) behavioural study indicated that MGO induces anxiety. Treatment of telmisartan (RAGE expression inhibitor) and aminoguanidine (MGO quencher) attenuated MGO induced anxiety. Further, hippocampal proteomics demonstrated that MGO treated rats differentially regulate proteins involved in calcium homeostasis, mitochondrial functioning, and apoptosis which may affect neurotransmission and neuronal plasticity. Hippocampal tau phosphorylation level was increased in MGO treated rats which was reduced in presence in aminoguanidine and telmisartan. Plasma fructosamine level was increased upon MGO treatment. Hippocampal histochemistry showed vascular degeneration and neuronal loss upon MGO treatment. This study provides mechanistic insight into the role of MGO in the diabetes-associated development of AD.
2024-01-26 | PXD037673 | Pride