AGEs Produce Harmful Effects via Interaction with RAGE

Advanced glycation end-products (AGEs) are a threefold problem. Firstly, a few species of persistent AGEs can form lasting cross-links between structural molecules of the extracellular matrix that alter its tensile properties, such as a loss of elasticity. Human biochemistry is ill-suited to the task of removing these cross-links, particularly those based on glucosepane. Secondly, AGEs can bind to proteins and modify their function, acting as a form of damage that cells must clear. Thirdly, transient AGEs interact with the receptor for AGEs, RAGE, to produce chronic inflammation and cellular dysfunction. This is characteristic of the abnormal, high-sugar environment of type 2 diabetes, but also an issue to a lesser degree in the broader aged population. Advanced glycation end-products (AGEs; e.g., glyoxal, methylglyoxal, or carboxymethyl-lysine) are heterogenous group of toxic compounds synthesized in the body through both exogenous and endogenous pathways. AGEs are known to covalently modify proteins bringing about loss of functional alteration in the proteins. AGEs also interact with their receptor, receptor for AGE (RAGE) and such interactions influence different biological processes including oxidative stress and apoptosis. Previously, AGE-RAGE axis has long been considered to be the maligning factor for various human diseases including, diabetes, obesity, cardiovascular, aging, etc. Recent developments have revealed the involvement of AGE-RAGE axis in dif...
Source: Fight Aging! - Category: Research Authors: Tags: Daily News Source Type: blogs