BACKGROUND Inflammation, often accompanied by oxidation, caused by advanced glycation end products (AGEs) may be quenched by the soluble receptor for AGEs (sRAGE). The present study aimed to investigate the influence of physical activity on circulating sRAGE, and the association between changes of circulating sRAGE and paraoxonase1 (PON1) activity (as an antioxidative enzyme) in a physical acti...

Advanced glycation endproducts (AGE) are the result of post-translational changes to proteins, which ultimately compromise their structure and/or function. The identification of methods to prevent the formation of these compounds holds great promise in the development of alternative therapies for diseases such as diabetes. Plants used in traditional medicine are often rich sources of anti-glyca...

context advanced glycation end-products (ages) are signaling proteins associated to several vascular and neurological complications in diabetic and non-diabetic patients. ages proved to be a marker of negative outcome in both diabetes management and surgical procedures in these patients. the reported role of ages prompted the development of pharmacological inhibitors of their effects, giving ri...

Type 2 diabetes mellitus represents a major public health challenge, due to the continuously growing prevalence and the complexity of the diabetic complications. Hyperglycemia seems to be the main mechanism for the disease progression. During erythrocyte’s long life span, erythrocyte membranes are affected by the chronic exposure to glucose, which triggers several biochemical modifications that...

The authors of the paper would like to apologize for the following errors contained in the original paper. 1. The exact Figure 1 in the original paper has to be corrected as Figure 1 in this paper. 2. References in the original paper have to be corrected by adding the following:vanced glycation end products cause epithelial-my-ofibroblast transdifferentiation via the receptor for advanced glyca...

The reaction between reducing sugars and protein free amines, known as the Maillar reaction results in the formation of advanced glycation endproducts (AGEs). AGE modification changes the structure of proteins to amyloid cross-beta structure. These protein structures can activate receptors known as RAGE on glial cells (microglia and astrocytes), and induce the expression of inducible nitric oxi...

Nonenzymatic glycation of proteins has been implicated in various diabetic complications and age-related disorders. Proteins undergo glycation at the N-terminus or at the epsilon-amino group of lysine residues. Glycation of proteins proceeds through the stages of Schiff base formation, conversion to ketoamine product and advanced glycation end products. Gramicidin S, which has two ornithine res...