RAGE consists of three immunoglobulin-like regions, a transmembrane domain, and a highly charged short cytosolic tail that is essential for intracellular signaling [13] . Th e V domain in the extracellular part of RAGE is essential for binding of its ligands. Because of its ability to recognize three-dimensional structures rather than specifi c amino acid sequences, RAGE can interact with a wide range of ligands. RAGE was fi rst identifi ed as a receptor for advanced glycation endproducts (AGEs), explaining its name. AGEs are products of the nonenzymatic glycation and oxidation of lipids, proteins and other macromolecules that appear, in particular, under conditions of increased availability of reducing sugars and/or enhanced oxidative stress, especially when molecules turn over slowly and aldose levels are elevated. Further investigations showed that RAGE can recognize a diverse array of endogenous molecules that warn the immune system and induce a defensive immune response; the alarmins or DAMPs.