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Inhibition of the angiogenesis by the MCP‐1 (monocyte chemoattractant protein‐1) binding peptide
Author(s) -
Kim Mee Young,
Byeon Cheol Woo,
Hong Kyung Hee,
Han Ki Hoon,
Jeong Sunjoo
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.01.070
Subject(s) - angiogenesis , peptide , chemotaxis , ccr2 , monocyte , chemistry , chemokine , chemokine receptor , microbiology and biotechnology , receptor , biology , biochemistry , cancer research , immunology
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.