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Mechanism of Action of the Tumor Vessel Targeting Agent NGR-hTNF: Role of Both NGR Peptide and hTNF in Cell Binding and Signaling.
Valentinis, Barbara; Porcellini, Simona; Asperti, Claudia; Cota, Manuela; Zhou, Dan; Di Matteo, Paola; Garau, Gianpiero; Zucchelli, Chiara; Avanzi, Nilla Roberta; Rizzardi, Gian Paolo; Degano, Massimo; Musco, Giovanna; Traversari, Catia.
Afiliación
  • Valentinis B; MolMed SpA, 20132 Milano, Italy. barbara.valentinis@molmed.com.
  • Porcellini S; MolMed SpA, 20132 Milano, Italy. simona.porcellini@molmed.com.
  • Asperti C; MolMed SpA, 20132 Milano, Italy. claudia.asperti@molmed.com.
  • Cota M; MolMed SpA, 20132 Milano, Italy. manuela.cota@molmed.com.
  • Zhou D; MolMed SpA, 20132 Milano, Italy. dan.zhou@molmed.com.
  • Di Matteo P; MolMed SpA, 20132 Milano, Italy. paola.di_matteo@novartis.com.
  • Garau G; Biocrystallography Unit, Division of Immunology, Transplantation and Infectious Diseases, IRCCS San Raffaele Scientific Institute, 20132 Milano, Italy. Gianpiero.Garau@iit.it.
  • Zucchelli C; Biomolecular NMR Unit, Division of Genetics and Cell Biology, IRCCS San Raffaele Scientific Institute, 20132 Milano, Italy. zucchelli.chiara@hsr.it.
  • Avanzi NR; Biotechnology Department, Nerviano Medical Sciences S.r.l., 20014 Nerviano, Italy. Nilla.Avanzi@nervianoms.com.
  • Rizzardi GP; MolMed SpA, 20132 Milano, Italy. paolo.rizzardi@altheiascience.com.
  • Degano M; Biocrystallography Unit, Division of Immunology, Transplantation and Infectious Diseases, IRCCS San Raffaele Scientific Institute, 20132 Milano, Italy. degano.massimo@hsr.it.
  • Musco G; Biomolecular NMR Unit, Division of Genetics and Cell Biology, IRCCS San Raffaele Scientific Institute, 20132 Milano, Italy. musco.giovanna@hsr.it.
  • Traversari C; MolMed SpA, 20132 Milano, Italy. catia.traversari@molmed.com.
Int J Mol Sci ; 20(18)2019 Sep 12.
Article en En | MEDLINE | ID: mdl-31547231
NGR-hTNF is a therapeutic agent for a solid tumor that specifically targets angiogenic tumor blood vessels, through the NGR motif. Its activity has been assessed in several clinical studies encompassing tumors of different histological types. The drug's activity is based on an improved permeabilization of newly formed tumor vasculature, which favors intratumor penetration of chemotherapeutic agents and leukocyte trafficking. This work investigated the binding and the signaling properties of the NGR-hTNF, to elucidate its mechanism of action. The crystal structure of NGR-hTNF and modeling of its interaction with TNFR suggested that the NGR region is available for binding to a specific receptor. Using 2D TR-NOESY experiments, this study confirmed that the NGR-peptides binds to a specific CD13 isoform, whose expression is restricted to tumor vasculature cells, and to some tumor cell lines. The interaction between hTNF or NGR-hTNF with immobilized TNFRs showed similar kinetic parameters, whereas the competition experiments performed on the cells expressing both TNFR and CD13 showed that NGR-hTNF had a higher binding affinity than hTNF. The analysis of the NGR-hTNF-triggered signal transduction events showed a specific impairment in the activation of pro-survival pathways (Ras, Erk and Akt), compared to hTNF. Since a signaling pattern identical to NGR-hTNF was obtained with hTNF and NGR-sequence given as distinct molecules, the inhibition observed on the survival pathways was presumably due to a direct effect of the NGR-CD13 engagement on the TNFR signaling pathway. The reduced activation of the pro survival pathways induced by NGR-hTNF correlated with the increased caspases activation and reduced cell survival. This study demonstrates that the binding of the NGR-motif to CD13 determines not only the homing of NGR-hTNF to tumor vessels, but also the increase in its antiangiogenic activity.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oligopéptidos / Proteínas Recombinantes de Fusión / Factor de Necrosis Tumoral alfa / Inhibidores de la Angiogénesis / Neoplasias Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2019 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oligopéptidos / Proteínas Recombinantes de Fusión / Factor de Necrosis Tumoral alfa / Inhibidores de la Angiogénesis / Neoplasias Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2019 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza