Mitogenic properties of a new endothelial cell growth factor related to pleiotrophin

Courty, José; Dauchel, Marie Claude; Caruelle, Daniéle; Perderiset, Mylène; Barritault, Denis

doi:10.1016/s0006-291x(05)81267-7

Cited by 126 publications

(99 citation statements)

References 13 publications

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“…Concomitantly, pleiotrophin is a proto-oncogene that functions as a mitogenic, anti-apoptotic, and tumor-transforming factor (4,(12)(13)(14)(15)(16)(17)(18). Furthermore, pleiotrophin stimulates epithelial-to-mesenchymal transition (EMT) (19), extensive remodeling of the malignant cell microenvironment (20), tumor angiogenesis (21,22), and metastasis (7).…”

Section: Pleiotrophin (Ptn)mentioning

confidence: 99%

Loss of Receptor Protein Tyrosine Phosphatase β/ζ (RPTPβ/ζ) Promotes Prostate Cancer Metastasis

Diamantopoulou

Kitsou

Ménashi

et al. 2012

Journal of Biological Chemistry

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Background:The role of pleiotrophin and its receptors RPTP␤/ and Syndecan-3 during tumor metastasis remains unknown. Results: RPTP␤/ knockdown initiates EMT, promotes pleiotrophin-mediated migration and attachment through Syndecan-3 and induces in vivo metastasis. Conclusion: RPTP␤/ plays a suppressor-like role in prostate cancer metastasis. Significance: Boosting RPTP␤/ or attenuating Syndecan-3 signaling pathways may lead to more effective therapeutic strategies in treating prostate cancer metastasis.

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Section: Pleiotrophin (Ptn)mentioning

confidence: 99%

Loss of Receptor Protein Tyrosine Phosphatase β/ζ (RPTPβ/ζ) Promotes Prostate Cancer Metastasis

Diamantopoulou

Kitsou

Ménashi

et al. 2012

Journal of Biological Chemistry

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“…Pleiotrophin is a polypeptide growth factor that has been shown to induce proliferation in a wide range of cells including epithelial, endothelial and mesenchymal cell lineages (Chauhan et al, 1993;Courty et al, 1991; Figure 2 Amino acid sequence alignments of NPM ± ALK, hLTK, dALK, hIGF-1R and c-ROS. The tyrosine kinase catalytic domain of NPM ± ALK is shown from aa 178 to 440. hLTK: Human leukocyte tyrosine kinase; dALK: Drosophila homologue of anaplastic lymphoma kinase; hIGF-1R: Human insulin-like growth factor 1 receptor; c-ROS: proto-oncogene c-ROS, a receptor tyrosine kinase related to the viral oncoprotein v-Ros (Neckameyer et al, 1986).~: ATP-binding site; &: Active site; *: NPM ± ALK tyrosine residues Y338, Y342 and Y343 Fang et al, 1992;Li et al, 1990;Wellstein et al, 1992).…”

Section: A Putative Alk Ligand Pleiotrophinmentioning

confidence: 99%

“…The overlapping expression patterns of ALK and pleiotrophin in the nervous system, including the thalamus and midbrain in the adult and developing brain, suggest that the molecules indeed could represent a growth factor/receptor pair (Schulte and Wellstein, 1997). However, pleiotrophin e ects have been demonstrated also in endothelial cells and ®broblasts (Chauhan et al, 1993;Courty et al, 1991;Fang et al, 1992;Li et al, 1990;Wellstein et al, 1992). Elevated pleiotrophin levels in the serum of patients su ering from a variety of solid tumors have been demonstrated Souttou et al, 1998) and animal studies have suggested that pleiotrophin may contribute to tumor growth, invasion and metastasis (Chauhan et al, 1993;Choudhuri et al, 1997;Czubayko et al, 1994Czubayko et al, , 1996Schulte et al, 1996).…”

Section: A Putative Alk Ligand Pleiotrophinmentioning

confidence: 99%

Translocations involving anaplastic lymphoma kinase (ALK)

2001

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Anaplastic large-cell lymphoma (ALCL) comprises a group of non-Hodgkin's lymphomas (NHLs) that were ®rst described in 1985 by Stein and co-workers and are characterized by the expression of the CD30/Ki-1 antigen (Stein et al., 1985). Approximately half of these lymphomas are associated with a typical chromosomal translocation, t(2;5)(p23;q35). Much confusion about the exact classi®cation and clinicopathological features of this subgroup of NHL was clari®ed with the identi®ca-tion of NPM ± ALK (nucleophosmin-anaplastic lymphoma kinase) as the oncogene created by the t(2;5) (Morris et al., 1994). With the discovery of NPM ± ALK as the speci®c lymphoma gene mutation, this NHL subtype could be rede®ned on the molecular level. This achievement was enhanced by the availability of speci®c antibodies that recognize ALK fusion proteins in para n-embedded lymphoma tissues. Several excellent recent reviews have summarized the histopathological and molecular ®ndings of ALCL and their use in the classi®cation of this lymphoma entity (Anagnostopoulos and Stein, 2000;Benharroch et al., 1998;Drexler et al., 2000;Foss et al., 2000;Gogusev and Nezelof, 1998;Kadin and Morris, 1998;Ladanyi, 1997;Morris et al., 2001;Shiota and Mori, 1996;Skinnider et al., 1999;Stein et al., 2000). This review will focus on the molecular function and signal transduction pathways activated by ALK fusion oncogenes, with recent advances and possible clinical implications to be discussed. Oncogene (2001) 20, 5623 ± 5637.

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“…In the last decade, we and others have shown that heparin affin regulatory peptide (HARP) (Rauvala, 1989), a neurite outgrowth promoting molecule, induces the proliferation of various cell types including fibroblasts, epithelial cells, and endothelial cells (Courty et al, 1991;Fang et al, 1992;Papadimitriou et al, 2000). Compelling evidence that HARP contributes to the regulation of angiogenesis has been reported (Laaroubi et al, 1994;Choudhuri et al, 1997;Delbe et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Heparin affin regulatory peptide binds to vascular endothelial growth factor (VEGF) and inhibits VEGF-induced angiogenesis

et al. 2004

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Heparin affin regulatory peptide (HARP) is an heparinbinding molecule involved in the regulation of cell proliferation and differentiation. Here, we report that HARP inhibited the biological activity induced by the 165-amino-acid form of vascular endothelial growth factor (VEGF 165 ) on human umbilical vein endothelial cells. Endothelial-cell proliferation induced by VEGF 165 showed about 50% inhibition in the presence of HARP in a concentration of 3 nM. In similar range of concentrations, HARP blocked tube formation induced by VEGF 165 in three-dimensional angiogenesis assay. In vivo studies showed that HARP inhibited the VEGF 165 -induced Matrigelt infiltration of endothelial cells. We then investigated the mechanisms of this inhibition and shown that HARP inhibited the binding of 125 I-VEGF 165 to the VEGF receptors of endothelial cells. Additional studies using VEGF soluble receptors indicated that binding of 125 I-VEGF 165 to kinase insert domain-containing receptor and neuropilin receptor was inhibited by HARP, but conversely the binding of 125 I-VEGF 165 to fms-like tyrosine kinase I receptor was unaffected. A competitive affinity-binding assay demonstrated that HARP interacted directly with VEGF 165 with a dissociation coefficient of 1.38 nM. Binding assay using deletion mutants of HARP revealed that the thrombospondin type-1 repeats domains were involved in this interaction. These data demonstrate for the first time that the angiogenic factor HARP can also negatively regulates the angiogenic activity of VEGF 165 .

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Mitogenic properties of a new endothelial cell growth factor related to pleiotrophin

Cited by 126 publications

References 13 publications

Loss of Receptor Protein Tyrosine Phosphatase β/ζ (RPTPβ/ζ) Promotes Prostate Cancer Metastasis

Loss of Receptor Protein Tyrosine Phosphatase β/ζ (RPTPβ/ζ) Promotes Prostate Cancer Metastasis

Translocations involving anaplastic lymphoma kinase (ALK)

Heparin affin regulatory peptide binds to vascular endothelial growth factor (VEGF) and inhibits VEGF-induced angiogenesis

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