Receptor for Advanced Glycation End Products and Its Involvement in Inflammatory Diseases

Figure 1

Schematic representation of full-length RAGE and its splice variants. RAGE is composed of an intracellular tail, a transmembrane domain, and an extracellular domain consisting of three immunoglobulin-like domains, one V-type followed by two C-type (C1 and C2) domains. The V-type domain is essential for ligand binding, and deletion of this domain results in an N-truncated form. The C-truncated, circulating soluble RAGE corresponds to the extracellular domain of RAGE lacking the intracellular tail and transmembrane domains. It may derive via proteolytic cleavage of full-length RAGE from the cell surface (cRAGE) or via alternative splicing of RAGE mRNA (esRAGE). C: constant; V: variable.