Abstract
Introduction: The angiogenic mediator, vascular endothelial growth factor, VEGF is strongly associated with tumor metastases. We postulated that VEGF-induced trans-endothelial migration of neoplastic thyroid cells is mediated by VEGF receptor 2, (KDR/Flk-1) and phosphorylation of the adherens junction protein, vascular endothelial cadherin (VE cadherin). Methods: Transmigration of two labeled thyroid cancer cell lines, DRO’90 and NPA-’87 across human umbilical vein (HUVEC) monolayers was examined in the presence or absence of an antibody (2C3, 10 μg/ml) which prevents binding of VEGF to KDR/Flk-1, or an isotype-matched control antibody, C44 (10 μg/ml). VEGF-induced tyrosine phosphorylation of, VE cadherin was also examined in the presence of these antibodies. Data were analyzed by ANOVA. Results: Compared to vehicle controls and C44, 2C3 significantly blocked the transmigration of both thyroid cancer cell lines across intact HUVEC monolayers, (see figure below) p < 0.05. Additionally, 2C3 markedly reduced VEGF-induced tyrosine phosphorylation of VE cadherin. Conclusions: KDR/Flk-1 signaling regulates the migration of neoplastic thyroid cells across endothelial monolayers. This pathway is associated with tyrosine phosphorylation of vascular endothelial cadherin.
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