Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA223224 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Transcriptome analysis of Advanced glycation end products treated ligament cells
| PRJNA275546 | ENA
Project description:Role of microRNA-214-targeting PTEN in advanced glycation end product-induced apoptosis delay of monocytes
| PRJNA132031 | ENA
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: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
Project description:Protein glycation is a highly disease-relevant concentration-dependent non-enzymatic reaction of reducing sugars with amine groups of proteins to form early as well as advanced glycation products (AGEs). To complement our blood proteomics studies in diabetics, we here established higher-energy collisional dissociation (HCD) fragmentation on Orbitrap mass spectrometers for analyzing protein glycation. We evaluated parameters to most efficiently fragment and identify early glycation products on in-vitro glycated model proteins. We then applied our optimized workflow for glycation analysis of the entire HeLa proteome as well as for single-run analysis of undepleted and unenriched blood plasma and whole blood. We conclude that HCD fragmentation is well suited for analyzing glycated peptides when integrating the dominant neutral loss into the analysis and that single-run plasma proteomics measurements have great potential to diagnosing the diabetic status of patients.
2017-01-02 | PXD004182 | Pride
Project description:The effect of resection of mouse livers on survival serve as a model for the effect of resection of human livers, which are performed for both the purposes of removing sick tissue and for transplanting healthy tissue. When less than 70% of a mouse liver is resected, the mouse usually lives. However, when more than 70% is resected, there is an increased probability that the mouse will die. We have found that deletion of Ager (Advanced Glycation End products receptor) (Rage) increases the chance of mouse survival relavtive to WT. Conversely, the deletion of Myd88 decreases the chances of survival, as does the simultaneous deletion of both Ager and Myd88. To understand these genotype/phenotype relations, we performed gene expression measurements.
2012-06-26 | GSE22873 | GEO
Project description:The receptor for advanced glycation end products (RAGE) plays a key role in mammal physiology and in the etiology and progression of inflammatory and oxidative stress-based diseases. In adults, RAGE expression is high only in the lung where the protein concentrates in the basal membrane of Type I alveolar epithelial cells. In diseases, RAGE levels increase in the affected tissues and sustain chronic inflammation. RAGE exists as a single trans-membrane protein with an ectodomain and a short carboxyl-terminal tail essential for signaling, or also as a soluble ectodomain (sRAGE) that acts as a decoy receptor. The ectodomain is composed of a variable and two constant IgG-like domains (V, C1 and C2). VC1 is a single integrated unit responsible for binding of RAGE to the majority of its ligands including the advanced glycation End products (AGEs), S100 proteins and HMGB-1. Here, we report the identification of 20 new RAGE binding partners captured from human plasma and involved in the coagulation and complement processes and in the extracellular matrix. Four proteins contained a -carboxyl glutamic acid (Gla)-domain. Using MicroScale Thermophoresis, we quantified the interaction of prothrombin (PT) with VC1 and with sRAGE. Calcium competed in the binding of PT to sRAGE and PT devoid of the Gla-domain did not bind to sRAGE, providing evidence that the Gla-domain is critical for the interaction. Finally, the presence of VC1 delayed plasma clotting in a dose-dependent manner. We propose that RAGE is involved in modulating blood coagulation presumably in conditions of lung injury.
2020-07-14 | PXD020355 | Pride