Title |
S100 to receptor for advanced glycation end-products binding assay: Looking for inhibitors
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Published in |
Biochemical & Biophysical Research Communications, March 2014
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DOI | 10.1016/j.bbrc.2014.02.143 |
Pubmed ID | |
Authors |
Laura Padilla, Sheila Dakhel, Jose Luis Hernández |
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. |
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Geographical breakdown
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Unknown | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 21 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 5 | 24% |
Other | 3 | 14% |
Student > Doctoral Student | 3 | 14% |
Professor | 2 | 10% |
Student > Master | 2 | 10% |
Other | 4 | 19% |
Unknown | 2 | 10% |
Readers by discipline | Count | As % |
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Medicine and Dentistry | 6 | 29% |
Biochemistry, Genetics and Molecular Biology | 4 | 19% |
Agricultural and Biological Sciences | 4 | 19% |
Physics and Astronomy | 2 | 10% |
Pharmacology, Toxicology and Pharmaceutical Science | 1 | 5% |
Other | 1 | 5% |
Unknown | 3 | 14% |