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Multiligand receptor for advanced glycation end products (RAGE) is expressed in a wide variety of tissues, including the liver. Interactions with its ligands lead to cellular activation and thus prolonged inflammation and apoptosis. RAGE also exists in a soluble, truncated isoform called soluble RAGE, which has the same ligand-binding specificity as membrane-RAGE; acting as decoy, it can contribute to the removal/neutralization of circulating ligands and the resultant reduction of signaling pathway activation. Experimental and clinical studies have highlighted the idea that the RAGE-ligand axis is involved in the development of liver fibrosis, inflammation, and regeneration after a massive injury and in the setting of liver transplantation. The involvement of the RAGE-ligand axis in vascular disease, diabetes, cancer, and neurodegeneration is well established, but it still needs to be clarified in the setting of liver diseases. We present a review of the recent literature Receptor for advanced glycation end products (RAGE) is a multiligand-binding member of the immunoglobulin superfamily of cell surface molecules.1 The full-length receptor consists of an extracellular region formed from 1 V-type immunoglobulin domain needed for ligand binding and 2 C-type immunoglobulin domains; these domains are followed by a single, short transmembrane domain and a short cytoplasmic domain that is essential for RAGE-mediated signal transduction.