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S100 to receptor for advanced glycation end-products binding assay: looking for inhibitors
Laura Padilla1, Sheila Dakhel1, Jose Luis Hernández1
1Biomed Division of LEITAT Technological Center, Barcelona Science Park, 08028 Barcelona, Spain.
Abstract:
Secreted by tumor and stromal cells, S100 proteins exert their biological functions via the interaction with surface receptors. The most described receptor is the receptor for advanced glycation end-products (RAGE), thereby participating in the S100-dependent cell migration, invasion, tumor growth, angiogenesis and metastasis. Several approaches have been described for determining this interaction. Here we describe an easy, specific and highly reproducible ELISA-based method, by optimizing several parameters such as the binding and blocking buffer, interaction time and concentrations, directed to screen chemical and biological inhibitors of this interaction for S100A4, S100A7 and S100P proteins. The efficiency of the protocol was validated by using well described neutralizing agents of the RAGE receptor and of the S100A4 activity. The methodology described here will allow future works with other members of the S100 protein family and their receptors.
Insights
This study presents a new ELISA method to screen inhibitors of S100 protein interactions with the receptor for advanced glycation end-products (RAGE). This assay facilitates the discovery of novel therapeutics targeting cancer progression and metastasis.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- S100 proteins are secreted by tumor and stromal cells, mediating biological functions through receptor interactions.
- The receptor for advanced glycation end-products (RAGE) is a key receptor for S100 proteins, influencing cell migration, invasion, tumor growth, angiogenesis, and metastasis.
Purpose of the Study:
- To develop and validate an easy, specific, and reproducible ELISA-based method for screening inhibitors of S100-RAGE interactions.
- To optimize parameters for an effective assay targeting S100A4, S100A7, and S100P proteins.
Main Methods:
- An optimized ELISA protocol was developed, focusing on binding/blocking buffers, interaction time, and concentrations.
- The assay's efficiency was validated using known neutralizing agents for RAGE and S100A4.
Main Results:
- A highly reproducible ELISA method was established for quantifying S100 protein interactions with RAGE.
- The protocol demonstrated effectiveness in screening potential inhibitors of S100-RAGE axis.
Conclusions:
- The described ELISA method provides a robust platform for identifying inhibitors of S100-RAGE interactions.
- This methodology can be extended to study other S100 protein family members and their receptors for therapeutic development.
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