Corpus ID: 13556380

Placental Growth Factor ( PlGF ) – Specific Uptake in Tumor Microenvironment of 89 Zr-Labeled PlGF Antibody RO 5323441

@inproceedings{Munnink2013PlacentalGF,
  title={Placental Growth Factor ( PlGF ) – Specific Uptake in Tumor Microenvironment of 89 Zr-Labeled PlGF Antibody RO 5323441},
  author={Thijs H. Oude Munnink and Karin Rita Tamas and Marjolijn N. Lub-de Hooge and Silke R. Vedelaar and Hetty Timmer-Bosscha and Annemiek M E Walenkamp and K. Michael Weidner and Frank Herting and Jean Tessier and Elisabeth G. E. de Vries},
  year={2013}
}
1Department of Medical Oncology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands; 2Department of Hospital and Clinical Pharmacy, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands; 3Department of Nuclear Medicine and Molecular Imaging; University of Groningen, University Medical Center Groningen, Groningen, The Netherlands; 4Pharma Research and Early Development, DTA Oncology, Roche Diagnostics GmbH, Penzberg… Expand

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Preclinical data concerning the function and inhibition of PlGF and the importance of its role in primary tumor growth are reviewed and early-phase clinical trials of TB-403, a monoclonal antibody inhibiting PlGF, are discussed. Expand
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With the tumor cell lines and mouse models used, antiangiogenic therapies that target both PlGF and VEGF may elicit a host response rather than, or in addition to, a malignant cell response that contribute to therapeutic resistance and tumor escape as suggested by others. Expand
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It is reported that embryonic angiogenesis in mice was not affected by deficiency of PlGF, andTransplantation of wild-type bone marrow rescued the impairedAngiogenesis and collateral growth in Pgf−/− mice, indicating that PlGF might have contributed to vessel growth in the adult by mobilizing bone-marrow–derived cells. Expand
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It is concluded that neuropilin-1 is a receptor for PlGF-2, and the presence of sulfate moieties on the glucosamine-o-6 and on the iduronic acid-O-2 groups of heparin was required for the potentiation of125I-Pl GF-2 binding to two endothelial cell surface receptors. Expand
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Although anti-PlGF treatment inhibited wound healing, extravasation of B16F10 cells, and growth of a tumor engineered to overexpress the PlGF receptor (VEGFR-1), neutralization of PlGF using four novel blocking antibodies had no significant effect on tumor angiogenesis in 15 models. Expand
Anti-PlGF Inhibits Growth of VEGF(R)-Inhibitor-Resistant Tumors without Affecting Healthy Vessels
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The efficacy and safety ofalphaPlGF, its pleiotropic and complementary mechanism to VEGF(R)Is, and the negligible induction of an angiogenic rescue program suggest that alphaPlGF may constitute a novel approach for cancer treatment. Expand
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