AGER Protein, Human (HEK293)

AGER Protein, a cell surface pattern recognition receptor, adeptly senses endogenous stress signals with a wide-ranging ligand repertoire, encompassing advanced glycation end products, S100 proteins, high-mobility group box 1 protein/HMGB1, amyloid beta/APP oligomers, nucleic acids, phospholipids, and glycosaminoglycans. Accumulation of advanced glycosylation end products, especially prevalent in aging and diabetes, triggers inflammatory responses at various disease sites, including diabetes, vascular complications, neurodegenerative disorders, and cancers. RAGE, upon ligand binding, utilizes TIRAP and MYD88 as adapters to transduce signals, ultimately inducing inflammatory cytokines IL6, IL8, and TNFalpha through NF-kappa-B activation. Noteworthy interactions include S100A12-triggered cellular activation, S100B-induced apoptosis post-myocardial infarction, and the facilitation of amyloid-beta peptide translocation in cortical neurons. AGER also plays a role in endothelial albumin transcytosis with HMGB1 through the RAGE/SRC/Caveolin-1 pathway, leading to endothelial hyperpermeability, and mediates the loading of HMGB1 in extracellular vesicles for hepatocyte pyroptosis via the NLRP3 inflammasome. Additionally, it promotes extracellular hypomethylated DNA uptake for the activation of inflammatory responses. The constitutive homodimeric and oligomeric forms, along with interactions with S100 proteins, APP, TIRAP, and HMGB1, highlight the intricate involvement of AGER Protein in various cellular processes and pathological conditions.