Efficient delivery of angiostatin K1-5 into tumors following insertion of an NGR peptide into adenovirus capsid

Jullienne, Betsy; Vigant, Frédéric; Muth, Erika; Chaligné, Ronan; Bouquet, Céline; Giraudier, Stéphane; Perricaudet, Michel; Benihoud, Karim

doi:10.1038/gt.2009.97

Cited by 19 publications

(17 citation statements)

References 40 publications

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“…For example, 41-, 47-and 91-integrins, can recognize the sequence LDV in fibronectin and SVVYGLR in osteopontin, whereas 11-, 21-, 101-and 111-integrins recognize the GFOGER sequence in collagen (Humphries et al, 2006). Besides these well-characterized binding motifs, it has been proposed that the NGR and DGR sequences also have a role in integrin recognition, although controversial data have been reported with regard to the integrinbinding properties of these motifs Hautanen et al, 1989;Jullienne et al, 2009;Koivunen et al, 1999;Liu et al, 1997;Rusnati et al, 1997;Soncin, 1992;Yamada and Kennedy, 1987). Interestingly, these motifs and many other integrin recognition sequences (reviewed by Ruoslahti, 1996) contain aspartate (Asp) or asparagine (Asn), i.e.…”

Section: Introductionmentioning

confidence: 99%

Isoaspartate-dependent molecular switches for integrin–ligand recognition

Corti¹,

Curnis²

2011

Journal of Cell Science

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Formation of isoAsp in ECM proteins and its functional effects Formation of isoAsp and ECM protein damageThe formation of isoAsp residues at Asn or Asp residues in proteins is generally considered a degradation reaction as a consequence of protein aging. IsoAsp formation has been shown to occur in ECM proteins, including collagen types I and III, in fibronectin, in -crystallin and in the ECM of the mammalian brain (Lanthier and Desrosiers, 2004;Lindner and Helliger, 2001; Reissner and Aswad, SummaryIntegrins are cell-adhesion receptors that mediate cell-extracellular-matrix (ECM) and cell-cell interactions by recognizing specific ligands. Recent studies have shown that the formation of isoaspartyl residues (isoAsp) in integrin ligands by asparagine deamidation or aspartate isomerization could represent a mechanism for the regulation of integrin-ligand recognition. This spontaneous posttranslational modification, which might occur in aged proteins of the ECM, changes the length of the peptide bond and, in the case of asparagine, also of the charge. Although these changes typically have negative effects on protein function, recent studies suggested that isoAsp formation at certain Asn-Gly-Arg (NGR) sites in ECM proteins have a gain-of-function effect, because the resulting isoAsp-Gly-Arg (isoDGR) sequence can mimic Arg-Gly-Asp (RGD), a well-known integrin-binding motif. Substantial experimental evidence suggests that the NGR-to-isoDGR transition can occur in vitro in natural proteins and in drugs containing this motif, thereby promoting integrin recognition and cell adhesion. In this Commentary, we review these studies and discuss the potential effects that isoAsp formation at NGR, DGR and RGD sites might have in the recognition of integrins by natural ligands and by drugs that contain these motifs, as well as their potential biological and pharmacological implications.

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Section: Introductionmentioning

confidence: 99%

Isoaspartate-dependent molecular switches for integrin–ligand recognition

Corti¹,

Curnis²

2011

Journal of Cell Science

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“…Lewis lung carcinoma (LLC) implantation mouse has been recognized as a standard experimental model for study cancer growth and metastasis. Recent reports suggested that [23][24][25]. Thus, LLC implantation mouse model was used to evaluate the eYcacy of CIP-13F targeting APN/CD13.…”

Section: Discussionmentioning

confidence: 99%

CIP-13F, a novel aminopeptidase N (APN/CD13) inhibitor, inhibits Lewis lung carcinoma growth and metastasis in mice

Pei

Yuan

Qin

et al. 2011

Cancer Chemother Pharmacol

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“…For instance, the tumor homing ability of a CNGRC-phage and of a CNGRC-TNF conjugate was inhibited by coadministration with an anti-CD13 antibody in different murine models [6,31]. Furthermore, other investigators provided evidence for the requirement of CD13 for NGR-peptide binding to cells in several in vitro and in vivo experimental models [17,19,21,23,29,[32][33][34][35][36][37][38].…”

Section: The Molecular Basis Of the Neovascula-ture Homing Propertiesmentioning

confidence: 96%

“…Adenovirus with the NGR sequence inserted into either fiber or hexon capsid proteins can efficiently deliver angiostatin K1-5 cDNA into endothelial cells, thus leading to a dramatic inhibition of cell proliferation, increased cell death, and tumor growth inhibition in animal models [34]. NGR has been incorporated also into Moloney murine leukaemia virus envelope escort proteins improving retrovirus binding and transduction of endothelial cells [22].…”

Section: Ngr-peptides and Viral Particles/nucleic Acid Deliverymentioning

confidence: 99%

Tumor Vasculature Targeting Through NGR Peptide-Based Drug Delivery Systems

Corti

Curnis

2011

CPB

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Various peptide sequences have been discovered by selecting peptide-phage display libraries in vitro against specific receptors or in vivo in tumor-bearing animals. One class of these peptides is characterized by the presence of Asn-Gly-Asp (NGR), a structural motif that can recognize the endothelium and other cells of neoangiogenic vessels. Because of this property these peptides have been used by several investigators to deliver a variety of drugs, cytokines, nanoparticles, viruses and imaging agents to tumor blood vessels. Here we review the reports on these conjugates and discuss the structural, functional and stability properties of NGR embedded into different molecular scaffolds.

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Efficient delivery of angiostatin K1-5 into tumors following insertion of an NGR peptide into adenovirus capsid

Cited by 19 publications

References 40 publications

Isoaspartate-dependent molecular switches for integrin–ligand recognition

Isoaspartate-dependent molecular switches for integrin–ligand recognition

CIP-13F, a novel aminopeptidase N (APN/CD13) inhibitor, inhibits Lewis lung carcinoma growth and metastasis in mice

Tumor Vasculature Targeting Through NGR Peptide-Based Drug Delivery Systems

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