Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA132031 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Transcriptome analysis of Advanced glycation end products treated ligament cells
| PRJNA275546 | ENA
Project description:Platelet-secreted microRNA-223 promotes endothelial cell apoptosis induced by advanced glycation end products via targeting the insulin-like growth factor 1 receptor
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Project description:Ossification of the posterior longitudinal ligament (OPLL) is formed by heterogeneous ossification of posterior longitudinal ligament. The patho-mechanism of OPLL is still largely unknown. Recently, disorders of metabolism are thought to be the center of many diseases such as OPLL. Advanced glycation end product (AGE) are accumulated in many extracellular matrixes such as ligament fibers, and it can functions as cellular signal through its receptor (RAGE), contributing to various events such as atherosclerosis or oxidative stress. However, its role in OPLL formation is not yet known. Therefore, we performed high-through-put RNA sequencing on primary posterior longitudinal ligament cells treated with different doses of AGEs (1µM, 5µM and negative control), with or without BMP2 (1µM).
2016-02-16 | GSE65952 | GEO
Project description:Ossification of the posterior longitudinal ligament (OPLL) is formed by heterogeneous ossification of posterior longitudinal ligament. The patho-mechanism of OPLL is still largely unknown. Recently, disorders of metabolism are thought to be the center of many diseases such as OPLL. Advanced glycation end product (AGE) are accumulated in many extracellular matrixes such as ligament fibers, and it can functions as cellular signal through its receptor (RAGE), contributing to various events such as atherosclerosis or oxidative stress. However, its role in OPLL formation is not yet known. Therefore, we performed high-through-put RNA sequencing on primary posterior longitudinal ligament cells treated with different doses of AGEs (1µM, 5µM and negative control), with or without BMP2 (1µM). mRNA profiles of Primary human posterior longitudinal ligament cells stimulated with various stimuli (Control, 1µM AGE-BSA, 5µM AGE-BSA, 1µM AGE-BSA with BMP2, 5µM AGE-BSA with BMP2) were generated by deep sequencing on Ion Proton
2016-02-16 | E-GEOD-65952 | biostudies-arrayexpress
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:Glycation, or non-enzymatic glycosylation, has recently attracted increasing interest in the context of its impact on aging. Advanced glycation end products (AGEs) contribute to various age-related pathological conditions such as inflammation, fibrosis, stem cell aging, etc. However, the molecular mechanisms underlying the glycation-induced disruption of cell-matrix interactions during cellular senescence are not fully understood. The aim of this study was to investigate transcriptomic changes in young and senescent dermal fibroblasts (HdFbs) cultivated in post-glycated 3D collagen type I matrices after 10 and 17 days. Our findings indicate that the D-ribose-mediated glycation increases the accumulation of fluorescent AGEs and the stiffness of the matrices in a dose-dependent manner. The transcriptome alterations encompassed the modulation of age-related genes and signaling pathways, including the activation of genes related to senescence-associated secretory phenotype (SASP) in young cells. Notably, the alterations in the transcriptome profiles due to glycation were more pronounced (in terms of both the number of genes and their fold changes) on day 10 of cultivation compared to day 17 in both passages.
2025-06-04 | GSE293225 | GEO
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: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:To study the impact of the accumulation of glyceraldehyde-derived intracellular protein advanced glycation end products (AGEs) on global proteomic changes in pancreatic ductal epithelial cells. The cells were treated with glyceraldehyde for up to 2 days and changes of protein expressions were assessed through mass spectroscopic analysis.
2025-07-21 | PXD050491 | Pride
Project description:Descriptive Transcriptome Analysis of Tendon Derived Fibroblasts Following In-Vitro Exposure to Advanced Glycation End Products
| PRJNA842004 | ENA