Inhibition of the angiogenesis by the MCP-1 (monocyte chemoattractant protein-1) binding peptide
Autor: | Sunjoo Jeong, Kyung Hee Hong, Ki Hoon Han, Mee Young Kim, Cheol Woo Byeon |
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Rok vydání: | 2004 |
Předmět: |
CCR2
Phage display Angiogenesis Receptors CCR2 Biophysics Neovascularization Physiologic Peptide Angiogenesis Inhibitors Biology Biochemistry Chemokine receptor Structural Biology Peptide Library Genetics Animals Humans CCR10 Peptide library CCL13 Molecular Biology Aorta Chemokine CCL2 chemistry.chemical_classification Chemokine receptor 3 Chemokine receptor 2 Cell Biology Surface Plasmon Resonance Molecular biology Monocyte chemoattractant protein-1 Rats chemistry Chemokine Biological Assay Receptors Chemokine Oligopeptides |
Zdroj: | FEBS letters. 579(7) |
ISSN: | 0014-5793 |
Popis: | The CC chemokine, monocyte chemoattractant protein-1 (MCP-1), plays a crucial role in the initiation of atherosclerosis and has direct effects that promote angiogenesis. To develop a specific inhibitor for MCP-1-induced angiogenesis, we performed in vitro selection employing phage display random peptide libraries. Most of the selected peptides were found to be homologous to the second extracellular loops of CCR2 and CCR3. We synthesized the peptide encoding the homologous sequences of the receptors and tested its effect on the MCP-1 induced angiogenesis. Surface plasmon resonance measurements demonstrated specific binding of the peptide to MCP-1 but not to the other homologous protein, MCP-3. Flow cytometry revealed that the peptide inhibited the MCP-1 binding to THP-1 monocytes. Moreover, CAM and rat aortic ring assays showed that the peptide inhibited MCP-1 induced angiogenesis. Our observations indicate that the MCP-1-binding peptide exerts its anti-angiogenic effect by interfering with the interaction between MCP-1 and its receptor. |
Databáze: | OpenAIRE |
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