Advanced glycation end products (AGEs) are potentially harmful and heterogeneous molecules derived from nonenzymatic glycation. The pathological implications of AGEs are ascribed to their ability to promote oxidative stress, inflammation, and apoptosis.
foods, including casein, β-lactoglobulin, soy protein, and meat protein, and in human samples, such as glycated-albumin, hemoglobin, and plasma. Additionally, it explores the metabolic fate of AGEs in the body and the mechanisms of disease associated with metabolic abnormalities that may be caus...
By blocking redox balance, AGEs can cause oxidative stress. This stress could be the source of ferroptosis, which is a novel mechanism of cell death. Unlike apoptosis and necrosis, ferroptosis is triggered by excessive phospholipid hydroperoxide accumulation in an iron-dependent manner (Yan et al.2...
A RAGE is a multiligand cell surface receptor in the immunoglobulin superfamily35. Generally, RAGEs are expressed widely in various cells, such as endothelial cells, macrophages/monocytes, neutrophils, lymphocytes, microglia, astrocytes, and neurons, and organs, such as the brain, heart, lung, kidn...
DJ-1 deficiency has been shown to enhance myocardial infarction and exacerbate left ventricular dysfunction in multiple models including myocardial I/R, permanent myocardial ischemia, and pressure overload-induced heart failure9,10,49,50. Further, delayed treatment with the cleaved form of DJ-1 was...
Advanced glycation end-products (AGEs) are considered potent molecules capable of promoting neuronal cell death and participating in the development of neurodegenerative disorders such as Alzheimer's disease (AD). Previous studies have shown that AGEs exacerbate β-amyloid (Aβ) aggregation and AGE-...
RAGE treatment reduced cytokines of TNF-α and IL-1β induced by LPS via ELISA. Meanwhile, HMGB1 increased MAP-2 expression, which was blocked after anti-RAGE treatment. Hence, HMGB1/RAGE does not exacerbate neuronal inflammation but plays a role in promoting NSCs differentiating into mature ...
nutrients Review Advanced Glycation End Products (AGEs) and Chronic Kidney Disease: Does the Modern Diet AGE the Kidney? Amelia K. Fotheringham 1,2 , Linda A. Gallo 3, Danielle J. Borg 2,4 and Josephine M. Forbes 1,2,* 1 Glycation and Diabetes Complications, Mater Research Institute, ...
Glycation of apoA-I is also a hallmark of diabetic complications to exacerbate neurodegenerative diseases via acceleration of amyloidogenesis. On the other hand, no study has compared the glycation susceptibility of apoA-I and α-syn. The current study showed that α-syn exhibited potent anti-...