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Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
Common interactions between S100A4 and S100A9 defined by a novel chemical probe
Per Björk1, Eva Källberg, Ulf Wellmar
1Active Biotech AB, Lund, Sweden.
Plos One
|May 14, 2013
Summary
Oxyclozanide (OX) inhibits interactions between S100A4, S100A9, RAGE, and TLR4. These proteins, crucial for tumor growth and metastasis, function similarly and dimerize extracellularly, requiring zinc.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- S100A4 and S100A9 proteins are implicated in tumor growth and metastasis.
- The interaction between S100A9 and RAGE is a potential therapeutic target.
Purpose of the Study:
- To investigate the interaction of oxyclozanide (OX) with S100A4 and S100A9.
- To elucidate the roles of S100A4 and S100A9 in interacting with RAGE and TLR4.
- To explore the functional similarities and dimerization of S100A4 and S100A9.
Main Methods:
- Chemical probe screening to identify inhibitors of S100A9-RAGE interaction.
- Biochemical assays to confirm interactions between S100A4, S100A9, RAGE, and TLR4.
- In vitro and in vivo dimerization studies.
- Analysis of protein expression in distinct immune cell subpopulations.
Main Results:
- Oxyclozanide (OX) interacts with both S100A9 and S100A4.
- S100A9 and S100A4 interact with RAGE and TLR4, and these interactions are inhibited by OX.
- S100A4 and S100A9 dimerize in vitro and in vivo, requiring extracellular zinc levels.
- These proteins are expressed by distinct CD11b+ subpopulations in various disease states.
Conclusions:
- S100A4 and S100A9 share functional similarities and interact with RAGE and TLR4, modulated by OX.
- Extracellular dimerization of S100A4 and S100A9 is a key functional aspect.
- These findings suggest potential therapeutic strategies targeting S100A4/S100A9-RAGE/TLR4 interactions in cancer and inflammation.
