Noninvasive visualization and quantification of tumor αVβ3 integrin expression using a novel positron emission tomography probe, 64Cu-cyclam-RAFT-c(-RGDfK-)4

Nuclear Medicine and Biology

Volumn 38, Issue 4, 2011, Pages 529-540

  Jin, Zhao Hui ^a   Furukawa, Takako ^a,b   Galibert, Mathieu ^c   Boturyn, Didier ^c   Coll, Jean Luc ^d   Fukumura, Toshimitsu ^a   Saga, Tsuneo ^a   Dumy, Pascal ^c   Fujibayashi, Yasuhisa ^a,b  

^a NATIONAL INSTITUTE OF RADIOLOGICAL SCIENCES   (Japan)

^b UNIVERSITY OF FUKUI   (Japan)

^c UNIVERSITÉ JOSEPH FOURIER   (France)

^d INSERM   (France)

Author keywords

Molecular imaging; Multimeric RGD peptide; PET

Indexed keywords

CYCLAM ARGINYLLYSYLASPARAGINE CU 64; TRACER; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 5; VITRONECTIN RECEPTOR;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; AUTORADIOGRAPHY; CANCER CELL CULTURE; CHEMICAL STRUCTURE; CONTROLLED STUDY; DRUG DISTRIBUTION; DRUG DOSE COMPARISON; FEMALE; FLOW CYTOMETRY; GLIOBLASTOMA; HIGH PERFORMANCE THIN LAYER CHROMATOGRAPHY; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; ISOTOPE LABELING; MOLECULAR IMAGING; MOLECULAR PROBE; MOUSE; NON INVASIVE PROCEDURE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; POSITRON EMISSION TOMOGRAPHY; PROTEIN EXPRESSION; QUANTITATIVE ANALYSIS; RECEPTOR BLOCKING; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; TISSUE LEVEL; URINARY EXCRETION;

EID: 79955466439     PISSN: 09698051     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nucmedbio.2010.11.008     Document Type: Article

References (34)

1. Stromblad S., Cheresh D.A. Integrins, angiogenesis and vascular cell survival. Chem Biol 1996, 3:881-885.
2. Jin H., Varner J. Integrins: roles in cancer development and as treatment targets. Br J Cancer 2004, 90:561-565.
3. Desgrosellier J.S., Cheresh D.A. Integrins in cancer: biological implications and therapeutic opportunities. Nat Rev Cancer 2010, 10:9-22.
4. Haubner R., Gratias R., Diefenbach B., Goodman S.L., Jonczyk A., Kessler H. Structural and functional aspects of RGD-containing cyclic pentapeptides as highly potent and selective integrin αVβ3 antagonists. J Am Chem Soc 1996, 118:7461-7472.
5. Schottelius M., Laufer B., Kessler H., Wester H.J. Ligands for mapping αVβ3-integrin expression in vivo. Acc Chem Res 2009, 42:969-980.
6. Gaertner F.C., Schwaiger M., Beer A.J. Molecular imaging of αVβ3 expression in cancer patients. Q J Nucl Med Mol Imaging 2010, 54:309-326.
7. Poethko T., Thumshirn G., Hersel U., Rau F., Haubner R., Schwaiger M., et al. Improved tumor uptake, tumor retention and tumor/background ratios of pegylated RGD-multimers. J Nucl Med 2003, 44(Suppl.):46.
8. Boturyn D., Coll J.L., Garanger E., Favrot M.C., Dumy P. Template assembled cyclopeptides as multimeric system for integrin targeting and endocytosis. J Am Chem Soc 2004, 126:5730-5739.
9. Li Z.B., Cai W., Cao Q., Chen K., Wu Z., He L., et al. 64Cu-labeled tetrameric and octameric RGD peptides for small-animal PET of tumor αVβ3 integrin expression. J Nucl Med 2007, 48:1162-1171.
10. Dijkgraaf I., Kruijtzer J.A., Liu S., Soede A.C., Oyen W.J., Corstens F.H., et al. Improved targeting of the αVβ3 integrin by multimerisation of RGD peptides. Eur J Nucl Med Mol Imaging 2007, 34:267-273.
11. Jin Z.H., Josserand V., Foillard S., Boturyn D., Dumy P., Favrot M.C., et al. In vivo optical imaging of integrin αVβ3 in mice using multivalent or monovalent cRGD targeting vectors. Mol Cancer 2007, 6:41-50.
12. Sancey L., Ardisson V., Riou L.M., Ahmadi M., Marti-Batlle D., Boturyn D., et al. In vivo imaging of tumour angiogenesis in mice with the αVβ3 integrin-targeted tracer 99mTc-RAFT-RGD. Eur J Nucl Med Mol Imaging 2007, 34:2037-2047.
13. Ahmadi M., Sancey L., Briat A., Riou L., Boturyn D., Dumy P., et al. Chemical and biological evaluations of an 111In-labeled RGD-peptide targeting integrin alpha(V) beta(3) in a preclinical tumor model. Cancer Biother Radiopharm 2008, 23:691-700.
14. Sancey L., Garanger E., Foillard S., Schoehn G., Hurbin A., Albiges-Rizo C., et al. Clustering and internalization of integrin αVβ3 with a tetrameric RGD-synthetic peptide. Mol Ther 2009, 17:837-843.
15. Smith S.V. Molecular imaging with copper-64. J Inorg Biochem 2004, 98:1874-1901.
16. Galibert M., Dumy P., Boturyn D. One-pot approach to well-defined biomolecular assemblies via orthogonal chemoselective ligations. Angew Chem Int Ed 2009, 48:2576-2579.
17. Foillard S., Rasmussen M.O., Razkin J., Boturyn D., Dumy P. 1-Ethoxyethylidene, a new group for the stepwise SPPS of aminooxyacetic acid-containing peptides. J Org Chem 2008, 73:983-991.
18. Boturyn D., Dumy P. A convenient access to αVβ3/αVβ5 integrin ligand-conjugates: regioselective solid phase functionalization of a RGD based peptide. Tetrahedron Lett 2001, 42:2787-2790.
19. Galibert M., Jin Z.H., Furukawa T., Fukumura T., Saga T., Fujibayashi Y., et al. RGD-cyclam conjugate: synthesis and potential application for positron emission tomography. Bioorg Med Chem Lett 2010, 20:5422-5425.
20. Zannetti A., Del Vecchio S., Iommelli F., Del Gatto A., De Luca S., Zaccaro L., et al. Imaging of αVβ3 expression by a bifunctional chimeric RGD peptide not cross-reacting with αVβ5. Clin Cancer Res 2009, 15:5224-5233.
21. Jin Z.H., Furukawa T., Waki A., Akaji K., Coll J.L., Saga T., et al. Effect of multimerization of a linear arg-gly-asp peptide on integrin binding affinity and specificity. Biol Pharm Bull 2010, 33:370-378.
22. Garanger E., Boturyn D., Jin Z., Dumy P., Favrot M.C., Coll J.L. New multifunctional molecular conjugate vector for targeting, imaging and therapy of tumors. Mol Ther 2005, 12:1168-1175.
23. Thibault G. Sodium dodecyl sulfate-stable complexes of echistatin and RGD-dependent integrins: a novel approach to study integrins. Mol Pharmacol 2000, 58:1137-1145.
24. Zhang X., Xiong Z., Wu Y., Cai W., Tseng J.R., Gambhir S.S., et al. Quantitative PET imaging of tumor integrin αVβ3 expression with 18F-FRGD2. J Nucl Med 2006, 47:113-121.
25. Wu Y., Zhang X., Xiong Z., Cheng Z., Fisher D.R., Liu S., et al. microPET imaging of glioma integrin αVβ3 expression using 64Cu-labeled tetrameric RGD peptide. J Nucl Med 2005, 46:1707-1718.
26. Chen X., Liu S., Hou Y., Tohme M., Park R., Bading J.R., et al. MicroPET imaging of breast cancer αV-integrin expression with 64Cu-labeled dimeric RGD peptides. Mol Imaging Biol 2004, 6:350-359.
27. Boswell C.A., Sun X., Niu W., Weisman G.R., Wong E.H., Rheingold A.L., et al. Comparative in vivo stability of copper-64-labeled cross-bridged and conventional tetraazamacrocyclic complexes. J Med Chem 2004, 47:1465-1474.
28. Garrison J.C., Rold T.L., Sieckman G.L., Figueroa S.D., Volkert W.A., Jurisson S.S., et al. In vivo evaluation and small-animal PET/CT of a prostate cancer mouse model using 64Cu bombesin analogues: side-by-side comparison of the CB-TE2A and DOTA chelation systems. J Nucl Med 2007, 48:1327-1337.
29. Boswell C.A., Regino C.A., Baidoo K.E., Wong K.J., Bumb A., Xu H., et al. Synthesis of a cross-bridged cyclam derivative for peptide conjugation and 64Cu radiolabeling. Bioconjug Chem 2008, 19:1476-1484.
30. Boswell C.A., Regino C.A., Baidoo K.E., Wong K.J., Milenic D.E., Kelley J.A., et al. A novel side-bridged hybrid phosphonate/acetate pendant cyclam: synthesis, characterization, and 64Cu small animal PET imaging. Bioorg Med Chem 2009, 17:548-552.
31. Kiessling F., Huppert J., Zhang C., Jayapaul J., Zwick S., Woenne E.C., et al. RGD-labeled USPIO inhibits adhesion and endocytotic activity of αVβ3-integrin-expressing glioma cells and only accumulates in the vascular tumor compartment. Radiology 2009, 253:462-469.
32. van Eerd J.E., Vegt E., Wetzels J.F., Russel F.G., Masereeuw R., Corstens F.H. Gelatin-based plasma expander effectively reduces renal uptake of 111In-octreotide in mice and rats. J Nucl Med 2006, 47:528-533.
33. Foillard S., Dumy P., Boturyn D. Highly efficient cell adhesion on beads functionalized with clustered peptide ligands. Org Biomol Chem 2009, 7:4159-4162.
34. Wei L., Ye Y., Wadas T.J., Lewis J.S., Welch M.J., Achilefu S., et al. 64Cu-labeled CB-TE2A and diamsar-conjugated RGD peptide analogs for targeting angiogenesis: comparison of their biological activity. Nucl Med Biol 2009, 36:277-285.