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. Author manuscript; available in PMC: 2016 Sep 1.
Published in final edited form as: Vascul Pharmacol. 2015 Jun 27;72:1–8. doi: 10.1016/j.vph.2015.06.011

Figure 2. The Multiple Ligands, Domains and Forms of RAGE.

Figure 2

RAGE is an immunoglobulin superfamily receptor that binds multiple families of ligands such as the AGEs, HMGB1, S100/calgranulins, LPA, PS, amyloid-beta peptide and beta-sheet fibrils. The ligands bind at the extracellular domain, largely the V-type domain. The extracellular domain is followed by a single transmembrane spanning domain and a short cytoplasmic domain, which binds to the formin mDia1 to enact cellular signaling. Two forms of soluble RAGE have been identified, soluble or sRAGE is formed by cell surface shedding actions of ADAM10 and MMPs. The second form is an alternatively spliced form called endogenous secretory (esRAGE), also known as RAGEv1. A unique 16 amino acid span in the C2 domain distinguishes esRAGE from sRAGE. Abbreviations: AGEs, advanced glycation endproducts; HMGB1, high mobility group box 1; LPA, lysophosphatidic acid; PS, phosphatidylserine; MMP, matrix metalloproteinase; and ADAM10, A-Distintegrin and Metalloprotease 10.