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Blood, 1 October 2008, Vol. 112, No. 7, pp. 2628-2635. Prepublished online as a Blood First Edition Paper on June 23, 2008; DOI 10.1182/blood-2008-04-150862. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2008-04-150862v1 112/7/2628    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Corti, A. Articles by Pasqualini, R. Search for Related Content PubMed PubMed Citation Articles by Corti, A. Articles by Pasqualini, R. Related Collections Hemostasis, Thrombosis, and Vascular Biology Review Articles Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  REVIEW ARTICLE The neovasculature homing motif NGR: more than meets the eye Angelo Corti1, Flavio Curnis1, Wadih Arap2, and Renata Pasqualini2 1 DIBIT-Department of Oncology and IIT Network Research Unit of Molecular Neuroscience, San Raffaele Scientific Institute, Milan, Italy; and 2 The University of Texas M. D. Anderson Cancer Center, Houston A growing body of evidence suggests that peptides containing the Asn-Gly-Arg (NGR) motif can selectively recognize tumor neovasculature and can be used, therefore, for ligand-directed targeted delivery of various drugs and particles to tumors or to other tissues with an angiogenesis component. The neovasculature binding properties of these peptides rely on the interaction with an endothelium-associated form of aminopeptidase N (CD13), an enzyme that has been implicated in angiogenesis and tumor growth. Recent studies have shown that NGR can rapidly convert to isoaspartate-glycine-arginine (isoDGR) by asparagine deamidation, generating vβ3 ligands capable of affecting endothelial cell functions and tumor growth. This review focuses on structural and functional properties of the NGR motif and its application in drug development for angiogenesis-dependent diseases. Furthermore, we discuss the time-dependent transition of NGR to isoDGR in natural proteins, such as fibronectins, and its potential role of as a "molecular timer" for generating new binding sites for integrins impli-cated in angiogenesis. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: G.-P. Rizzardi and C. Bordignon NGR and isoDGR are separate moieties binding to different receptors Blood, May 21, 2009; 113(21): 5366 - 5366. [Full Text] [PDF] C. Schwoppe, R. Bieker, R. M. Mesters, and W. E. Berdel Response: NGR and isoDGR are separate moieties binding to different receptors Blood, May 21, 2009; 113(21): 5367 - 5367. [Full Text] [PDF] R. Bieker, T. Kessler, C. Schwoppe, T. Padro, T. Persigehl, C. Bremer, J. Dreischaluck, A. Kolkmeyer, W. Heindel, R. M. Mesters, et al. Infarction of tumor vessels by NGR-peptide-directed targeting of tissue factor: experimental results and first-in-man experience Blood, May 14, 2009; 113(20): 5019 - 5027. [Abstract] [Full Text] [PDF] A. M. Gasparri, E. Jachetti, B. Colombo, A. Sacchi, F. Curnis, G.-P. Rizzardi, C. Traversari, M. Bellone, and A. Corti Critical role of indoleamine 2,3-dioxygenase in tumor resistance to repeated treatments with targeted IFN{gamma} Mol. Cancer Ther., December 1, 2008; 7(12): 3859 - 3866. [Abstract] [Full Text] [PDF]

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