ArticleMatrix biology : journal of the International Society for Matrix Biology2017
Stimulatory effects of advanced glycation endproducts (AGEs) on fibronectin matrix assembly.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 35 citations in OpenAlex.
- Shared mechanisms of musculoskeletal dysfunction in type 2 diabetes mellitus: Insights into future therapeutic directions (Review).International journal of molecular medicine · 2026Review
- Molecular mechanisms and novel therapeutic targets of diabetic kidney disease.Chinese medical journal · 2026Review
- Mechanical Properties of Glycated Cracked Articular Cartilage Under Uniaxial and Cyclic Tensile Loading.Annals of biomedical engineering · 2026Article
- Size-selective glomerular filtration as a hallmark of premature kidney ageing in nondiabetic individuals.Clinical kidney journal · 2025Article
- Mechanisms of assembly and remodelling of the extracellular matrix.Nature reviews. Molecular cell biology · 2024Review
- Proteomic insights into the extracellular matrix: a focus on proteoforms and their implications in health and disease.Expert review of proteomics · 2024Review
- Diabetes Mellitus as a Risk Factor for Spontaneous Preterm Birth in Women with a Short Cervix after Ultrasound-Indicated Cerclage.Journal of clinical medicine · 2024Article
- An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition.Biophysical reviews · 2024Review
- Association Between Advanced Glycation End Products and Sarcopenia: The Mediating Role of Osteoporosis.The Journal of clinical endocrinology and metabolism · 2024Article
- Fibronectin in hyperglycaemia and its potential use in the treatment of diabetic foot ulcers: A review.International wound journal · 2023Review
- Red emissive N-doped carbon dots encapsulated within molecularly imprinted polymers for optosensing of pyrraline in fatty foods.Mikrochimica acta · 2023Article
- JAK/STAT signaling in diabetic kidney disease.Frontiers in cell and developmental biology · 2023Review
- Methylglyoxal and Its Adducts: Induction, Repair, and Association with Disease.Chemical research in toxicology · 2022Review
- Implications of fibrotic extracellular matrix in diabetic retinopathy.Experimental biology and medicine (Maywood, N.J.) · 2022Review
- Modification of Fibronectin by Non-Enzymatic Glycation Impairs KFrontiers in physiology · 2022Article
- Cross-Talking Pathways of Forkhead Box O1 (FOXO1) Are Involved in the Pathogenesis of Alzheimer's Disease and Huntington's Disease.Oxidative medicine and cellular longevity · 2022Article
- Advanced Glycation End-Products in Skeletal Muscle Aging.Bioengineering (Basel, Switzerland) · 2021Review
- Elevated glucose alters global gene expression and tenascin-C alternative splicing in mesangial cells.Matrix biology plus · 2020Article
- Effect of metabolic syndrome on incidence of oral potentially malignant disorder: a prospective cohort study in Taiwan.BMJ open · 2020Article
- Glycation of fibronectin inhibits VEGF-induced angiogenesis by uncoupling VEGF receptor-2-c-Src crosstalk.Journal of cellular and molecular medicine · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Advanced glycation endproducts (AGEs) are a heterogeneous group of compounds that form via non-enzymatic glycation of proteins throughout our lifespan and at a higher rate in certain chronic diseases such as diabetes. AGEs contribute to the progression of fibrosis, in part by stimulating cellular pathways that affect gene expression. Long-lived ECM proteins are targets for non-enzymatic glycation but the question of whether the AGE-modified ECM leads to excess ECM accumulation and fibrosis remains unanswered. In this study, cellular changes due to AGE accretion in the ECM were investigated. Non-enzymatic glycation of proteins in a decellularized fibroblast ECM was achieved by incubating the ECM in a solution of methylglyoxal (MGO). Mass spectrometry of fibronectin (FN) isolated from the glycated matrix identified twenty-eight previously unidentified MGO-derived AGE modification sites including functional sites such as the RGD integrin-binding sequence. Mesangial cells grown on the glycated, decellularized matrix assembled increased amounts of FN matrix. Soluble AGE-modified bovine serum albumin (BSA) also stimulated FN matrix assembly and this effect was reduced by function-blocking antibodies against the receptor for AGE (RAGE). These results indicate that cells respond to AGEs by increasing matrix assembly and that RAGE is involved in this response. This raises the possibility that the accumulation of ECM during the progression of fibrosis may be enhanced by cell interactions with AGEs on a glycated ECM.
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