| Autor: |
Luker KE; Center for Molecular Imaging, Department of Radiology, University of Michigan Medical School, Ann Arbor, Michigan, USA., Mihalko LA, Schmidt BT, Lewin SA, Ray P, Shcherbo D, Chudakov DM, Luker GD |
| Jazyk: |
angličtina |
| Zdroj: |
Nature medicine [Nat Med] 2011 Dec 04; Vol. 18 (1), pp. 172-7. Date of Electronic Publication: 2011 Dec 04. |
| DOI: |
10.1038/nm.2590 |
| Abstrakt: |
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 small-molecule 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 drug-mediated 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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