Co-Expression of VEGF-C and Its Receptors, VEGFR-2 and VEGFR-3, in Endothelial Cells of Lymphangioma. Implication in Autocrine or Paracrine Regulation of Lymphangioma

Huang, Hsin–Yi; Ho, Chao‐Chi; Huang, Pei‐Hsin; Hsu, Su-Ming

doi:10.1038/labinvest.3780386

Cited by 66 publications

(52 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In addition, B-TEC expressed vascular endothelial-cadherin (Fig. 1J) and the VEGFR-3, the lymphatic-associated VEGF receptor, which is also expressed by renal TEC (17) and by vascular tumors (24,25) (Fig. 1H).…”

Section: Resultsmentioning

confidence: 99%

Isolation and characterization of human breast tumor-derived endothelial cells

et al. 2006

View full text Add to dashboard Cite

Abstract. Increasing evidence indicates that tumor-derived endothelial cells (TEC) possess a distinct and unique phenotype in respect to normal endothelial cells and may be able to acquire resistance to drugs. However, few functional studies are available on cultured TEC. In the present study, we obtained TEC from human breast carcinomas and, to dispel the possibility of contaminating tumor cells, we established six different clones that we characterized at a functional level. Breast TEC cell lines and clones did not undergo normal cell senescence in culture and showed constant expression of markers of endothelial activation and angiogenesis. These cells showed increased apoptosis resistance to vincristine and doxorubicin and increased random cell motility, as compared to normal micro-endothelial cells. In addition, breast TEC, at variance to normal endothelial cells, were able to grow and to organize in the absence of serum in capillary-like structures on Matrigel that persisted up to one week. These functional characteristics of breast TEC may be relevant for tumor angiogenesis and may indicate an increased pro-angiogenic activity of endothelial cells within the tumor. Moreover, our data suggest that TEC might be more appropriate for screening antiangiogenic drugs than normal endothelial cells.

show abstract

Section: Resultsmentioning

confidence: 99%

Isolation and characterization of human breast tumor-derived endothelial cells

et al. 2006

View full text Add to dashboard Cite

show abstract

“…VEGF-C was originally described as a specific growth factor for lymphatic vessels (2,3,22), but later was also found to induce angiogenesis of blood vessels (3,(23)(24)(25)(26)(27)(28), raising questions about the mechanism(s) that determine the distinct effects of VEGF-C in vivo. In addition, VEGF-C overexpression was linked to various cancers and metastasizing tumors in which VEGF-C was shown to mediate vascular and lymphatic vessel formation (3,23,29).…”

Section: Figurementioning

confidence: 99%

The secretory proprotein convertases furin, PC5, and PC7 activate VEGF-C to induce tumorigenesis

Siegfried¹,

Basak²,

Cromlish³

et al. 2003

J. Clin. Invest.

View full text Add to dashboard Cite

“…14,37,38 However, it has been demonstrated that VEGFR-3 activity requires heterodimerization with VEGFR-2, which is also expressed on lymphatic vessels. [39][40][41] In this study, we have investigated the ability of NRP2 to interact with VEGFR-2 and VEGFR-3 and analyzed the consequences of such interactions on human endothelial cell survival and migration.…”

Section: Introductionmentioning

confidence: 99%

Neuropilin-2 interacts with VEGFR-2 and VEGFR-3 and promotes human endothelial cell survival and migration

Favier

Alam

Barron

et al. 2006

Blood

262

249

View full text Add to dashboard Cite

Neuropilin 2 (NRP2) is a receptor for the vascular endothelial growth factor (VEGF) and the semaphorin (SEMA) families, 2 unrelated ligand families involved in angiogenesis and neuronal guidance. NRP2 specifically binds VEGF-A and VEGF-C, although the biological relevance of these interactions in human endothelial cells is poorly understood. In this study, we show that both VEGF-A and VEGF-C induce the interaction of NRP2 with VEGFR-2. This interaction correlated with an enhancement of the VEGFR-2 phosphorylation threshold. Overexpression of NRP2 in primary human endothelial cells promoted cell survival induced by VEGF-A and VEGF-C. In contrast, SEMA3F, another ligand for NRP2, was able to inhibit human endothelial cell survival and migration induced by VEGF-A and VEGF-C. Moreover, a siRNA targeting specifically NRP2 was a potent inhibitor of human endothelial cell migration induced by VEGF-A and VEGF-C. Thus, our data indicate that NRP2 acts as a coreceptor that enhances human endothelial cell biological responses induced by VEGF-A and VEGF-C.

show abstract

Co-Expression of VEGF-C and Its Receptors, VEGFR-2 and VEGFR-3, in Endothelial Cells of Lymphangioma. Implication in Autocrine or Paracrine Regulation of Lymphangioma

Cited by 66 publications

References 16 publications

Isolation and characterization of human breast tumor-derived endothelial cells

Isolation and characterization of human breast tumor-derived endothelial cells

The secretory proprotein convertases furin, PC5, and PC7 activate VEGF-C to induce tumorigenesis

Neuropilin-2 interacts with VEGFR-2 and VEGFR-3 and promotes human endothelial cell survival and migration

Contact Info

Product

Resources

About