Imaging of alpha(v)beta(3) Expression by a Bifunctional Chimeric RGD Peptide not Cross-Reacting with alpha(v)beta(5) (Articolo in rivista)

Type
Label
  • Imaging of alpha(v)beta(3) Expression by a Bifunctional Chimeric RGD Peptide not Cross-Reacting with alpha(v)beta(5) (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1158/1078-0432.CCR-08-3270 (literal)
Alternative label
  • Zannetti, A; Del Vecchio, S; Iommelli, F; Del Gatto, A; De Luca, S; Zaccaro, L; Papaccioli, A; Sommella, J; Panico, M; Speranza, A; Grieco, P; Novellino, E; Saviano, M; Pedone, C; Salvatore, M (2009)
    Imaging of alpha(v)beta(3) Expression by a Bifunctional Chimeric RGD Peptide not Cross-Reacting with alpha(v)beta(5)
    in Clinical cancer research (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Zannetti, A; Del Vecchio, S; Iommelli, F; Del Gatto, A; De Luca, S; Zaccaro, L; Papaccioli, A; Sommella, J; Panico, M; Speranza, A; Grieco, P; Novellino, E; Saviano, M; Pedone, C; Salvatore, M (literal)
Pagina inizio
  • 5224 (literal)
Pagina fine
  • 5233 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 15 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 16 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biostrutture e Bioimmagini, CNR-Napoli Dipartimento di Scienze Biomorfologiche e Funzionali, Università di Napoli \"Federico II\" Dipartimento di Chimica Farmaceutica e Tossicologia, Università di Napoli \"Federico II\" (literal)
Titolo
  • Imaging of alpha(v)beta(3) Expression by a Bifunctional Chimeric RGD Peptide not Cross-Reacting with alpha(v)beta(5) (literal)
Abstract
  • Purpose: To test whether a novel bifunctional chimeric peptide comprising a cyclic Arg- Gly-Asp pentapeptide covalently bound to an echistatin domain can discriminate alpavbeta3 from alpavbeta5 integrin, thus allowing the in vivo selective visualization of alpavbeta3 expression by single-photon and positron emission tomography (PET) imaging. Experimental Design: The chimeric peptide was preliminarily tested for inhibition of alphavbeta3-dependent cell adhesion and competition of 125I-echistatin binding to membrane of stably transfected K562 cells expressing alpavbeta3 (Kalpavbeta3 ) or alphavbeta5 (Kalpavbeta5) integrin. The chimeric peptide was then conjugated with diethylenetriaminepentaacetic acid and la- beled with 111In for single-photon imaging, whereas a one-step procedure was used for labeling the full-length peptide and a truncated derivative, lacking the last five C-termi- nal amino acids, with 18F for PET imaging. Nude mice bearing tumors from Kalpavbeta3 , Kalpavbeta5, U87MG human glioblastoma, and A431 human epidermoid cells were subjected to single-photon and PET imaging. Results: Adhesion and competitive binding assays showed that the novel chimeric pep- tide selectively binds to alpavbeta3 integrin and does not cross-react with alpavbeta5. In agreement with in vitro findings, single-photon and PET imaging studies showed that the radiola- beled chimeric peptide selectively localizes in tumor xenografts expressing alpavbeta3 and fails to accumulate in those expressing alpavbeta5 integrin. When 18F-labeled truncated derivative was used for PET imaging, alpavbeta3 - and alpavbeta5-expressing tumors were visualized, indicating that the five C-terminal amino acids are required to differentially bind the two integrins. Conclusion: Our findings indicate that the novel chimeric Arg-Gly-Asp peptide, having no cross-reaction with alpavbeta5 integrin, allows highly selective alpavbeta3 expression imaging and monitoring. (Clin Cancer Res 2009;15(16):5224-33) (literal)
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