About sRAGE / Advanced Glycosylation End Product-Specific Receptor:
RAGE stands for Receptor for Advanced Glycation Endproducts. They’re sometimes referred to as AGER. It is a 35 kilodalton transmembrane receptor which belongs to the immunoglobulin super family. This was first mapped by Neeper and colleagues back in 1992. It was given its name because of its ability to bind advanced glycation endproducts, such as glycoproteins; the glycine of these have been modified -- non-enzymatically -- through the Maillard reaction.
sRAGE Function
RAGE is commonly characterized as a pattern recognition reception. This is because it can perform an inflammatory function in innate immunity, and also because of its ability to detect a class of ligands through a common structural motif. Researchers have found that isoforms of the RAGE protein are typically hypothesized to counteract the full-length receptor. There is hope in the medical community that they can be used to develop a cure against RAGE-associated diseases.
Advanced Glycosylation End Product-Specific Receptor Structure
In terms of structure, RAGE exists in two different forms. There’s the membrane-found form, which is referred to as mRAGE, and then there’s the soluble form, which is referred to as sRAGE. While mRAGE has three domains, sRAGE only has one -- the extracellular domain. Researchers have noted that sRAGE will be the product of either alternative splicing or a result of proteolytic cleavage of mRAGE. The full receptor will have the five domains. These are the cytosolic domain, which functions to signal transduction; the transmembrane domain, which helps to anchor the receptor in the cell membrane; the variable domain, which helps to bind the RAGE ligands; and then two constant domains.