Abstract
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.
Highlights
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 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
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
Summary
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. 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
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