VE-Cadherin Mediates Endothelial Cell Capillary Tube Formation in Fibrin and Collagen Gels1

Bach, Tami L.; Barsigian, Carl; Chalupowicz, Diana G.; Busler, Dennis E.; Yaen, Christopher H.; Grant, Derrick S.; Martinez, Josè

doi:10.1006/excr.1997.3844

Cited by 206 publications

(174 citation statements)

References 48 publications

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“…In VE-cadherin-deficient embryos and yolk sacs, the vascularization vitro Matsumura et al 1997Bach et al 1998 process was arrested at a very primitive stage, with no sign of angiogenic sprouting ( ). For example, the yolk sac Gory-Faur et al 1999 é blood islands formed normally but did not undergo vascular branching until fetal death at midgestation, indicating that VE-cadherin is required for developmental angiogenesis.…”

Section: Ve-cadherin Requirement and Function In Angiogenesismentioning

confidence: 99%

Angiogenesis: The VE-Cadherin Switch

Wallez

Vilgrain

Huber

2006

Trends in Cardiovascular Medicine

119

101

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Section: Ve-cadherin Requirement and Function In Angiogenesismentioning

confidence: 99%

Angiogenesis: The VE-Cadherin Switch

Wallez

Vilgrain

Huber

2006

Trends in Cardiovascular Medicine

119

101

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“…14,[26][27][28] Control experiments indicated that Fg added to breast cancer or endothelial cells was not processed further by protease degradation or crosslinking to higher ordered structures (data not shown). Synthetic peptides corresponding to the Fg b-chain primary structure were custom synthesized as previously described, 11 and include b , b [15][16][17][18][19][20][21][22][23][24][25][26][27] , b 18-31 and b [24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42] (Table I). Fibrinopeptide A (Bachem) was used as a nonspecific peptide for permeability studies.…”

Section: Fibrinogen Purification and Synthetic Peptidesmentioning

confidence: 99%

“…Because b [15][16][17] residues are critical for the binding specificity of b to VE-cadherin, 17 synthetic peptides containing or missing residues of the b 15-42 primary structure were used in the permeability assay (Fig. 2c).…”

Section: Fg-induced Ec Permeability Involves Fg-b 15-42 Sequences Andmentioning

confidence: 99%

“…The negative control peptide corresponding to fibrinopeptide A induced minimal %FITC-Dextran Flux compared with Fg or peptide b 15-42 (#p < 0.0001); however, the 13% relative fluorescence was significant (-p 5 0.001) compared with basal levels that were 1% of intact Fg-induced permeability. Peptides missing b 15-17 residues (b [18][19][20][21][22][23][24][25][26][27][28][29][30][31] or b [24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42] ) or truncated at the C-terminus (b [15][16][17][18][19][20][21][22][23][24][25][26][27] (Fig. 2c).…”

Section: Fg-induced Ec Permeability Involves Fg-b 15-42 Sequences Andmentioning

confidence: 99%

“…Breakdown of VE-cadherin-mediated endothelial barrier function leads to altered vascular permeability and remodeling, which are associated with a number of disease processes including ischemia-reperfusion injury, inflammation, angiogenesis, and cancer growth and metastasis. VE-cadherin also supports EC capillary tube formation in fibrin gels, 15 which requires exposure of the fibrin b 15-42 neo-aminoterminus 16 ; portions of the third and fourth extracellular domains of VE-cadherin constitute a fibrin b 15-42 receptor. 17,18 Using the fibrin-specific monoclonal antibody (MoAb) T2G1, we showed that binding of fibrin monomer to the surface of EC is b 15-42 -dependent, which leads to reduced accessibility of b 15-21 to T2G1.…”

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confidence: 99%

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The VE‐cadherin binding domain of fibrinogen induces endothelial barrier permeability and enhances transendothelial migration of malignant breast epithelial cells

Sahni

Arévalo

Sahni

et al. 2009

Intl Journal of Cancer

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Fibrin deposition and exudation of plasma fibrinogen (Fg) have long been recognized as hallmarks of inflammation, cardiovascular disease and neoplasia. The Fg-b 15-42 domain binds to the endothelial cell adhesion molecule, VE-cadherin, promoting endothelial cell proliferation, angiogenesis and leukocyte diapedesis. Furthermore, spontaneous blood-borne and lymphatic metastasis of some types of tumor emboli requires plasma fibrin(ogen); however, the molecular mechanisms by which this occurs are poorly understood. We sought to determine whether Fg-b 15-42 and VEcadherin binding interactions promote endothelial barrier permeability and breast cancer cell transendothelial migration (TEM) using transwell insert culture systems. Synthetic peptides containing/missing residues b 15-17 critical for In 1865, Armand Trousseau reported the observation that patients with an increased incidence of coagulopathies would later manifest visceral malignancies, which became known as Trousseau's syndrome. Ironically, Trousseau diagnosed himself with his own syndrome in 1866 and died of gastric cancer the following year. Causal factors linked to the prothrombotic state of Trousseau's syndrome also facilitate cancer metastasis, including thrombin, tissue factor, selectins, platelets, endothelial cells (EC) and fibrin. 1 Deposition of fibrinogen (Fg) 5 and fibrin commonly occurs within the stroma of most solid tumors, 2 and elevated levels of plasma Fg and fibrin degradation products (FDPs) correlate positively with lymph node involvement and metastasis of colon, ovarian, lung and breast cancers. 1 Studies by Degen and co-workers 3-5 have firmly established that plasma fibrin(ogen) and platelets play critical roles in spontaneous cancer metastasis through both the circulation and lymphatic systems, in part by protecting tumor cells from natural killer cell-mediated lysis.Expression of interleukin (IL)-6 during systemic inflammation upregulates expression of specific plasma proteins in the liver, including Fg. 6 Excessive fibrin deposition is accompanied by local expression of proinflammatory mediators, vascular leakage, and inflammatory cell recruitment and activation leading to amplification of the inflammatory response. 2,7,8 Residues 15-42 on the b chain of Fg have been implicated in functional attributes ascribed to fibrin(ogen). Although the primary structure of fibrinopeptide B (FPB) is poorly conserved across species, the fibrin b 15-42 domain is highly conserved, implying evolutionary conservation of function. 9 The b 15-42 region constitutes a cryptic domain in soluble Fg that is exposed in fibrin after thrombin cleavage. 10 Newly exposed residues, b15-GHRP-18, promote lateral aggregation of fibrin monomers during polymerization and insoluble clot formation in secondary hemostasis. 10 Furthermore, exposure of the b 15-42 domain mediates fibrin binding to EC surfaces, 11 promotes EC adhesion and spreading, 12 and stimulates proliferation of EC, fibroblasts and cancer cells. 13,14 Cadherins mediate homophilic cell-cell adhesion...

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Molecular mechanisms that control endothelial cell contacts

Vestweber

2000

J. Pathol.

114

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Endothelial cell contacts control the permeability of the blood vessel wall. This allows the endothelium to form a barrier for solutes, macromolecules, and leukocytes between the vessel lumen and the interstitial space. Loss of this barrier function in pathophysiological situations can lead to extracellular oedema. The ability of leukocytes to enter tissue at sites of inflammation is dependent on molecular mechanisms that allow leukocytes to adhere to the endothelium and to migrate through the endothelial cell layer and the underlying basal lamina. It is a commonly accepted working hypothesis that inter‐endothelial cell contacts are actively opened and closed during this process. Angiogenesis is another important process that requires well‐controlled regulation of inter‐endothelial cell contacts. The formation of new blood vessels by sprouting from pre‐existing vessels depends on the loosening of established endothelial cell contacts and the migration of endothelial cells that form the outgrowing sprouts. This review focuses on the molecular composition of endothelial cell surface proteins and proteins of the cytoskeletal undercoat of the plasma membrane at sites of inter‐endothelial cell contacts and discusses the current knowledge about the potential role of such molecules in the regulation of endothelial cell contacts. Copyright © 2000 John Wiley & Sons, Ltd.

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VE-Cadherin Mediates Endothelial Cell Capillary Tube Formation in Fibrin and Collagen Gels1

Cited by 206 publications

References 48 publications

Angiogenesis: The VE-Cadherin Switch

Angiogenesis: The VE-Cadherin Switch

The VE‐cadherin binding domain of fibrinogen induces endothelial barrier permeability and enhances transendothelial migration of malignant breast epithelial cells

Molecular mechanisms that control endothelial cell contacts

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