Journal
NATURE MEDICINE
Volume 18, Issue 1, Pages 172-177Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nm.2590
Keywords
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Funding
- US National Institutes of Health [R01 CA 136553, R01 CA 136829, R01 CA142750, P50 CA93990, U24 CA083099]
- Russian Educational Institutions [11.G34.31.0017]
- Russian Ministry of Education and Science [16.740.11.0367, 16.512.11.2139]
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Studies of ligand-receptor binding and the development of receptor antagonists would benefit greatly from imaging techniques that translate directly from cell-based assays to living animals. We used Gaussia luciferase protein fragment complementation to quantify the binding of chemokine (C-X-C motif) ligand 12 (CXCL12) to chemokine (C-X-C motif) receptor 4 (CXCR4) and CXCR7. Studies established that smallmolecule inhibitors of CXCR4 or CXCR7 specifically blocked CXCL12 binding in cell-based assays and revealed differences in kinetics of inhibiting chemokine binding to each receptor. Bioluminescence imaging showed CXCL12-CXCR7 binding in primary and metastatic tumors in a mouse model of breast cancer. We used this imaging technique to quantify drugmediated inhibition of CXCL12-CXCR4 binding in living mice. We expect this imaging technology to advance research in areas such as ligand-receptor interactions and the development of new therapeutic agents in cell-based assays and small animals.
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