Angiogenesis in cancer, vascular, rheumatoid and other disease

Folkman, Judah

doi:10.1038/nm0195-27

Cited by 7,110 publications

(4,934 citation statements)

References 47 publications

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“…26,27 In the case of cancer, it is thought that these strategies can potentially overcome acquired Gene Therapy drug resistance since the cellular targets of such therapies are normal, genetically stable microvascular endothelial cells. 15 However, because such approaches target specific signaling pathways, resistance to anti-angiogenic therapy may arise if tumor cells secrete multiple survival factors to maintain their own capillary network.…”

Section: Discussionmentioning

confidence: 99%

Ablation of microvessels in vivo upon dimerization of iCaspase-9

Nör

Song

et al. 2002

Gene Ther

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Section: Discussionmentioning

confidence: 99%

Ablation of microvessels in vivo upon dimerization of iCaspase-9

Nör

Song

et al. 2002

Gene Ther

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“…Several members of the ®broblast growth factor family of which FGF-1 (aFGF) and FGF-2 (bFGF) are the best characterized bind to the FGFR-1 with high a nity. In vivo, FGF-1 and FGF-2 act as angiogenic factors (Folkman, 1995) and as potent inducers of DNA synthesis. In vitro, FGF-1 stimulates endothelial cell migration and proliferation (reviewed by Burgess and Maciag, 1989).…”

Section: Introductionmentioning

confidence: 99%

Fibroblast growth factor receptor-1 mediates chemotaxis independently of direct SH2-domain protein binding

et al. 1998

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Endothelial cells expressing ®broblast growth factor receptor-1 (FGFR-1) migrate and proliferate in response to treatment with FGF. We analysed ligand-induced migration and proliferation of porcine aortic endothelial cells expressing wild-type FGFR-1, point-mutated Y766F FGFR-1, unable to activate phospholipase C-g1 (PLCg1), or carboxyl-terminally truncated FGFR-1, lacking either 48 (from amino acid 774 in the FGFR-1 sequence) or 63 (from amino acid 759) amino acid residues of the C-terminal tail. The truncated CT63 FGFR-1 mutant failed to mediate chemotaxis, but was in response to ligand stimulation capable of mediating proliferation of the cells, stimulation of MAP kinase activity and tyrosine phosphorylation of FRS2, an FGFR-1 speci®c signaling molecule. The defect in migration-capacity of CT63 was not due to loss of Y766, and thereby PLC-g1 activation, since cells expressing the mutant Y766F FGFR-1 migrated as e ciently as the wild-type receptor cells. Induction of phospholipase A 2 (PLA 2 ) activity by the activated FGFR-1 was dependent on the presence of Y766, and was therefore also not critical for the chemotactic response. Although the FGFR-1 only very ine ciently mediates activation of phosphatidylinositol 3' kinase (PI 3-kinase), the PI 3-kinase inhibitor wortmannin suppressed wild-type FGFR-1 mediated migration. We conclude that the signal transduction pathway for FGFR-1 mediated migration is independent of phosphotyrosine residues in the receptor and requires activation of a wortmannin-sensitive enzyme.

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“…Angiogenesis, the growth of new capillaries, is a critical process in tumour growth and metastasis (Folkman, 1995). Numerous angiogenic factors have been identified to date, the most potent of these being vascular endothelial growth factor (VEGF), otherwise known as vascular permeability factor (VPF).…”

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confidence: 99%

A peptide corresponding to the neuropilin-1-binding site on VEGF165 induces apoptosis of neuropilin-1-expressing breast tumour cells

et al. 2005

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There is increasing evidence that vascular endothelial growth factor (VEGF) has autocrine as well as paracrine functions in tumour biology. Vascular endothelial growth factor-mediated cell survival signalling occurs via the classical tyrosine kinase receptors Flt-1, KDR/Flk-1 and the more novel neuropilin (NP) receptors, NP-1 and NP-2. A 24-mer peptide, which binds to neuropilin-1, induced apoptosis of murine and human breast carcinoma cells, whereas a peptide directed against KDR had no effect. Both anti-NP1 and anti-KDR peptides induced endothelial cell apoptosis. Confocal microscopy using 5-(6)-carboxyfluorescein-labelled peptides showed that anti-NP1 bound to both tumour and endothelial cells, whereas anti-KDR bound endothelial cells only. This study demonstrates that NP-1 plays an essential role in autocrine antiapoptotic signalling by VEGF in tumour cells and that NP1-blockade induces tumour cell and endothelial cell apoptosis. Specific peptides can therefore be used to target both autocrine (tumour cells) and paracrine (endothelial cells) signalling by VEGF.

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Angiogenesis in cancer, vascular, rheumatoid and other disease

Cited by 7,110 publications

References 47 publications

Ablation of microvessels in vivo upon dimerization of iCaspase-9

Ablation of microvessels in vivo upon dimerization of iCaspase-9

Fibroblast growth factor receptor-1 mediates chemotaxis independently of direct SH2-domain protein binding

A peptide corresponding to the neuropilin-1-binding site on VEGF165 induces apoptosis of neuropilin-1-expressing breast tumour cells

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