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  • 1
    Keywords: RECEPTOR ; ANGIOGENESIS ; CELLS ; ENDOTHELIAL-CELLS ; EXPRESSION ; GROWTH ; GROWTH-FACTOR ; tumor ; CELL ; Germany ; IN-VIVO ; VIVO ; DISEASE ; DISTINCT ; DIFFERENTIATION ; ACTIVATION ; LIGAND ; MECHANISM ; MARKER ; CONTRAST ; mechanisms ; culture ; MUSCLE ; SMOOTH-MUSCLE CELLS ; T-LYMPHOCYTES ; BODY ; REGULATOR ; VEGF ; CELL-DIFFERENTIATION ; JUNCTIONS ; RE ; endothelial cells ; cell differentiation ; neovascularization ; in vivo ; ENDOTHELIAL-CELL ; regulatory mechanism ; VASCULAR MORPHOGENESIS ; JUNCTION ; CONTACT ; ARTERIAL-VENOUS DIFFERENTIATION ; CARDIOVASCULAR DEVELOPMENT ; EPH ; SMOOTH-MUSCLE-CELLS ; EphB4 ; ephrinB2 ; smooth muscle cells
    Abstract: Objective-The EphB ligand ephrinB2 has been identified as a critical determinant of arterial endothelial differentiation and as a positive regulator of invading endothelial cells during angiogenesis. This study was aimed at identifying determinants of endothelial cell ephrinB2 expression. Methods and Results-Arteriovenous asymmetrical endothelial cell ephrinB2 expression in vivo is lost on transfer into culture with aortic endothelial cells becoming partially ephrinB2-negative and saphenous vein endothelial cells becoming partially ephrinB2-positive. Contact with smooth muscle cells and angiogenic stimulation by vascular endothelial growth factor lead to an increased endothelial cell ephrinB2 expression. Quiescent, smooth muscle-contacting endothelial cells express ephrinB2 uniformly on their luminal surface. In contrast, monolayer endothelial cells translocate ephrinB2 to interendothelial cell junctions, which is strongly enhanced by EphB4-Fc-mediated receptor body activationed. Junctional ephrinB2 colocalizes and coimmunoprecipitates with CD31. Conclusions-This study identifies distinct regulatory mechanisms of endothelial ephrinB2 expression and cellular distribution in quiescent and activated endothelial cells. The data demonstrate that endothelial cell ephrinB2 expression is controlled by microenvironmental determinants rather than being an intrinsic endothelial cell differentiation marker
    Type of Publication: Journal article published
    PubMed ID: 16357318
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  • 2
    Keywords: ANGIOGENESIS ; CELLS ; EXPRESSION ; GROWTH ; carcinoma ; IN-VIVO ; INHIBITION ; MIGRATION ; ADHESION MOLECULE ; MORPHOGENESIS ; RECEPTOR-TYROSINE KINASE ; BREAST-CANCER METASTASIS ; LUNG METASTASIS
    Abstract: The tyrosine kinase receptor EphB4 interacts with its ephrinB2 ligand to act as a bidirectional signaling system that mediates adhesion, migration, and guidance by controlling attractive and repulsive activities. Recent findings have shown that hematopoietic cells expressing EphB4 exert adhesive functions towards endothelial cells expressing ephrinB2. We therefore hypothesized that EphB4/ephrinB2 interactions may be involved in the preferential adhesion of EphB4-expressing tumor cells to ephrinB2-expressing endothelial cells. Screening of a panel of human tumor cell lines identified EphB4 expression in nearly all analyzed tumor cell lines. Human A375 melanoma cells engineered to express either full-length EphB4 or truncated EphB4 variants which lack the cytoplasmic catalytic domain (Delta C-EphB4) adhered preferentially to ephrinB2-expressing endothelial cells. Force spectroscopy by atomic force microscopy confirmed, on the single cell level, the rapid and direct adhesive interaction between EphB4 and ephrinB2. Tumor cell trafficking experiments in vivo using sensitive luciferase detection techniques revealed significantly more EphB4-expressing A375 cells but not Delta C-EphB4-expressing or mock-transduced control cells in the lungs, the liver, and the kidneys. Correspondingly, ephrinB2 expression was detected in the microvessels of these organs. The specificity of the EphB4-mediated tumor homing phenotype was validated by blocking the EphB4/ephrinB2 interaction with soluble EphB4-Fc. Taken together, these experiments identify adhesive EphB4/ephrinB2 interactions between tumor cells and endothelial cells as a mechanism for the site-specific metastatic dissemination of tumor cells.
    Type of Publication: Journal article published
    PubMed ID: 21047731
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  • 3
    Keywords: RECEPTOR ; ANGIOGENESIS ; CELLS ; ENDOTHELIAL-CELLS ; GROWTH ; GROWTH-FACTOR ; BLOOD ; CELL ; Germany ; IN-VIVO ; KINASE ; THERAPY ; TYROSINE KINASE ; SYSTEM ; SYSTEMS ; PROTEIN ; MOLECULES ; LIGAND ; FAMILY ; BLOOD-FLOW ; DENDRITIC CELLS ; blood flow ; FLOW ; DOWN-REGULATION ; FIELD ; MOLECULE ; METASTASIS ; TRAFFICKING ; ADHESION ; RECEPTORS ; ESTABLISHMENT ; VESSELS ; REGULATOR ; PERMEABILITY ; VEGF ; signaling ; RE ; FAMILIES ; GUIDANCE ; assembly ; TYROSINE KINASES ; ROLES ; function ; ENDOTHELIAL-CELL ; endothelium ; receptor tyrosine kinase ; TIE2 ; VASCULAR MORPHOGENESIS ; CARDIOVASCULAR DEVELOPMENT ; EPH RECEPTOR ; RECEPTOR TYROSINE KINASES ; VASCULAR-PERMEABILITY ; LIGAND ANGIOPOIETIN-2 ; NEURAL DEVELOPMENT ; TUMOR ENDOTHELIUM
    Abstract: Vascular receptor tyrosine kinases (RTK) have been identified as critical regulatory signaling molecules of developmental and adult vascular morphogenic processes [vascular endothelial growth factor (VEGF) receptors=sprouting; EphB receptors=assembly; Tie2 receptor=maturation and quiescence]. It is intriguing that the same molecules that control the growth of blood and lymphatic vessels play critical roles in the adult to regulate maintenance functions related to vascular homeostasis. VEGF is among the most potent inducers of vascular permeability. The second vascular RTK system, the interaction of paracrine-acting Angiopoietin-1 with its cognate receptor Tie2, acts as an endothelial maintenance and survival-mediating molecular system, which stabilizes the vessel wall and controls endothelial cell quiescence. The third vascular RTK system, the interaction of Eph receptors with their Eph family receptor-interacting protein (ephrin) ligands, transduces positional guidance cues on outgrowing vascular sprouts, which are critical for proper arteriovenous assembly and establishment of blood flow. As such, Eph-ephrin interactions act as an important regulator of cell-cell interactions, exerting propulsive and repulsive functions on neighboring cells and mediating adhesive functions. This review summarizes recent findings related to the roles of the Angiopoietin-Tie and the Eph-ephrin systems as regulators of cell trafficking in the vascular system. The recognition of vascular homeostatic functions of vascular RTKs marks an important change of paradigm in the field of angiogenesis research as it relates angiogenesis-inducing molecules to vascular maintenance functions in the adult. This may also broaden the scope of vascular RTK-targeted therapies. J. Leukoc. Biol. 80: 719-726;2006
    Type of Publication: Journal article published
    PubMed ID: 16864601
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