Related Experiment Videos
Phagocyte-specific S100 proteins: a novel group of proinflammatory molecules
Johannes Roth1, Thomas Vogl, Clemens Sorg
1Institute of Experimental Dermatology, University of Muenster, Von-Esmarch-Str. 58, D-48149 Muenster, Germany.
Insights
Three S100 calcium-binding proteins act as proinflammatory molecules. Their high expression links to leukocyte recruitment and inflammation, making them targets for new therapies.
Area of Science:
- Biochemistry
- Immunology
- Molecular Biology
Background:
- S100 proteins are calcium-binding molecules.
- Phagocytes release proinflammatory S100 proteins.
- S100A8 and S100A9 are implicated in leukocyte recruitment.
Purpose of the Study:
- To investigate the role of S100 proteins in inflammation.
- To identify novel proinflammatory molecules.
- To explore S100A12 interactions with cellular receptors.
Main Methods:
- Analysis of S100 protein expression in inflammatory conditions.
- In vitro studies on leukocyte recruitment.
- Investigation of S100A12 binding to the receptor for advanced glycation end products (RAGE).
Main Results:
- Three S100 proteins identified as proinflammatory molecules.
- High expression of S100A8 and S100A9 correlates with leukocyte recruitment.
- S100A12 activates endothelial cells, mononuclear phagocytes, and lymphocytes via RAGE.
Conclusions:
- S100A8, S100A9, and S100A12 are key players in inflammatory processes.
- S100A12 acts as a direct activator of immune and endothelial cells.
- These S100 proteins represent promising therapeutic targets for modulating inflammation.
Abstract:
Three members of the S100 family of calcium-binding proteins comprise a new group of proinflammatory molecules released by phagocytes. A novel inflammatory syndrome defined by extraordinarily high expression of S100A8 and S100A9 confirmed recent observations in vitro demonstrating a role of these proteins during recruitment of leukocytes. S100A12 directly activates endothelial cells, mononuclear phagocytes and lymphocytes through interaction with the receptor for advanced glycation end products. Thus, these S100-proteins are attractive targets to modulate inflammation.