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Induction of Alloantigen-specific Anergy in Human Peripheral Blood Mononuclear Cells by Alloantigen Stimulation with Co-stimulatory Signal Blockade
Published on: March 14, 2011
CD166/ALCAM mediates proinflammatory effects of S100B in delayed type hypersensitivity
Rüdiger von Bauer1, Dimitrios Oikonomou, Alba Sulaj
1Department of Medicine I and Clinical Chemistry, University of Heidelberg, D-69120 Heidelberg, Germany. ruediger.vonbauer@med.uni-heidelberg.de
Journal of Immunology (Baltimore, Md. : 1950)
|June 5, 2013
Summary
Soluble receptor for advanced glycation end products (RAGE) ligands may bind other receptors. CD166/ALCAM acts as a RAGE homolog, mediating S100B-induced inflammation via NF-κB signaling in endothelial cells.
Area of Science:
- Immunology
- Molecular Biology
- Cellular Signaling
Background:
- Pattern recognition receptors, like RAGE, play a role in inflammation.
- Soluble RAGE effectively reduces delayed-type hypersensitivity (DTH), suggesting ligands may interact with other receptors.
Purpose of the Study:
- To identify alternative receptors for RAGE ligands.
- To investigate the role of CD166/ALCAM in S100B-induced inflammation.
Main Methods:
- Utilized wild type (WT), RAGE(-/-), and CD166/ALCAM(-/-) mouse models.
- Employed small interfering RNA (siRNA) to block CD166/ALCAM expression.
- Assessed NF-κB activation in endothelial cells and DTH responses in vivo.
Main Results:
- Identified CD166/ALCAM as a functional homolog of RAGE.
- S100B binding to CD166/ALCAM induced NF-κB activation in WT and RAGE(-/-) cells.
- CD166/ALCAM siRNA attenuated DTH in WT and RAGE(-/-) mice; genetic deletion showed compensatory RAGE upregulation.
Conclusions:
- S100B acts as a proinflammatory cytokine that bridges RAGE and CD166/ALCAM.
- RAGE and CD166/ALCAM exhibit compensatory upregulation upon genetic deletion of the other.
- Both RAGE and CD166/ALCAM are critical in mediating S100B-induced inflammatory responses.
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