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The human granulocyte-specific Ca2+-binding protein S100A12 is particularily over-expressed in autoinflammatory diseases such as juvenile idiopathic arthritis (JIA) as well as other inflammatory conditions (i.e. infections, vasculitides) and has been ascribed to the group of pro-inflammatory damage associated molecular pattern molecules (DAMPs). In order to operate as DAMP, S100A12 requires binding to cellular receptors. Although the protein was originally found to bind the receptor of advanced glycation endproducts (RAGE), we recently demonstrated S100A12 to stimulate proinflammatory cytokine production in monocytes via TLR4 instead of RAGE.

Hexameric S100A12 is required for pro-inflammatory TLR4-signalling