Cultured Endothelial Cells Regulate Platelet Adhesion to their Extracellular Matrix by Regulating its von Willebrand Factor Content

Yp, Wu; Jj, Sixma; Groot, de

doi:10.1055/s-0038-1653846

Cited by 14 publications

(13 citation statements)

References 30 publications

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“…Addition of antibiotics to the culture medium of HUVE cells decreases the amount of von Willebrand factor deposited in the cellular matrix (28). Among the 14 antibiotics examined, only amphotericin, penicillin, streptomycin, and rifamycin had no significant influence on the composition and reactivity of the endothelial cell matrix.…”

Section: Discussionmentioning

confidence: 92%

Neomycin inhibits angiogenin-induced angiogenesis

1998

Proc. Natl. Acad. Sci. U.S.A.

107

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A class of angiogenesis inhibitor has emerged from our mechanistic study of the action of angiogenin, a potent angiogenic factor. Neomycin, an aminoglycoside antibiotic, inhibits nuclear translocation of human angiogenin in human endothelial cells, an essential step for angiogenin-induced angiogenesis. The phospholipase Cinhibiting activity of neomycin appears to be involved, because U-73122, another phospholipase C inhibitor, has a similar effect. In contrast, genistein, oxophenylarsine, and staurosporine, inhibitors of tyrosine kinase, phosphotyrosine phosphatase, and protein kinase C, respectively, do not inhibit nuclear translocation of angiogenin. Neomycin inhibits angiogenin-induced proliferation of human endothelial cells in a dose-dependent manner. At 50 M, neomycin abolishes angiogenin-induced proliferation but does not affect the basal level of proliferation and cell viability. Other aminoglycoside antibiotics, including gentamicin, streptomycin, kanamycin, amikacin, and paromomycin, have no effect on angiogenininduced cell proliferation. Most importantly, neomycin completely inhibits angiogenin-induced angiogenesis in the chicken chorioallantoic membrane at a dose as low as 20 ng per egg. These results suggest that neomycin and its analogs are a class of agents that may be developed for anti-angiogenin therapy.

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Section: Discussionmentioning

confidence: 92%

Neomycin inhibits angiogenin-induced angiogenesis

1998

Proc. Natl. Acad. Sci. U.S.A.

107

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“…Cells were removed with 0.1 mol/L NH 4 OH for 15 minutes at room temperature, and subsequently the matrices were washed 3 times with PBS (10 mmol/L phosphate buffer [pH 7.4] and 0.15 mol/L NaCl). The isolation procedure of the ECM did not influence the amount of fibronectin in the ECM, 34 and the matrix is free of cell membrane fragments. 35 …”

Section: Extracellular Matrixmentioning

confidence: 89%

Fibronectin in an Extracellular Matrix of Cultured Endothelial Cells Supports Platelet Adhesion via Its Ninth Type III Repeat

Beumer¹,

Heijnen-Snyder²,

IJsseldijk³

et al. 2000

ATVB

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Abstract-We investigated the involvement of different domains of fibronectin in mediating platelet adhesion to fibronectin in the extracellular matrix (ECM) of cultured endothelial cells under flow conditions. Polyclonal anti-fibronectin antibodies were absorbed with Sepharose to which no protein, intact fibronectin, or different fibronectin fragments had been coupled to obtain supernatants (Sups) (Sup 0 , Sup FN , and Sup name of the fragment , respectively) from which a specific part of the antibodies had been removed. Treatment of the ECM before perfusion with Sup 0 resulted in a 36% decrease in platelet coverage, whereas treatment with Sup FN resulted in maximal adhesion. Treatment of the ECM with supernatants from which antibodies directed against the gelatin-or heparin-binding domain had been removed showed the same inhibition as treatment with Sup 0 . Removal of antibodies directed to the 120-kDa cell-binding domain resulted in a level of adhesion equal to the level found when the ECM was treated with Sup FN . Further analysis of this central region showed that only treatment with supernatants from which antibodies directed to the ninth type III repeat (III-9) of fibronectin had been removed resulted in a significantly higher adhesion than treatment with Sup 0 . Studies of adhesion to the fragments themselves showed that only fragments containing III-10 were able to support adhesion. Mutation of the Arg-Gly-Asp (RGD) sequence into Arg-Gly-Glu (RGE) in one of those fragments resulted in a complete loss of adhesive capacity. These data suggest that platelet adhesion to fibronectin in the ECM depends on III-9, whereas III-10 does not seem to be required. For platelet adhesion to isolated fibronectin, an intact RGD sequence seems to be crucial. Key Words: platelet adhesion Ⅲ fibronectin Ⅲ endothelial cell matrix T he extracellular matrix (ECM) protein fibronectin is involved in a variety of biological processes by mediating cell adhesion and migration. 1 As a constituent of the subendothelium of the vessel wall, it is recognized by blood platelets. In this way, fibronectin contributes to the process of hemostasis, which follows after the vessel has been damaged and the integrity of the endothelial cell layer has been lost.Fibronectin is composed of 3 types of homologous repeats, designated as types I, II, and III. 2 Proteolysis yields proteaseresistant functional domains that interact with heparin, collagen, fibrin, and cells. The cell-binding domain, which occupies the central region in the molecule, consists of type III repeats, each Ϸ90 amino acids in length. 3 The first sequence in fibronectin found to possess celladhesive properties was the arginine-glycine-aspartic acid (RGD) sequence, which is located in the 10th type III repeat (III-10) of the cell-binding domain. 4 On platelets, this sequence in fibronectin is recognized by 2 receptors, glycoprotein (GP) IIb/IIIa 5,6 and very late antigen 5 (VLA-5), 7 corresponding to GP Ic/IIa on the platelet. 8 -10 Both receptors are members of the superfamily o...

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“…Triton treatment removes cells effectively by solubilizing lipid membranes, but leaves ECM matrix components such as fibronectin, laminin, von Willebrand factor and collagens intact so that they are able to bind to adhesive receptors which are expressed on cells. [46][47][48] Triplicates of 10 5 cells/well were adhered to rinsed ECM under static conditions in the presence of adhesion blocking or control antibodies (10 g/ml) for 1 h at 37°C. Non-adherent cells were removed and viable adherent cells were quantified using the MTT assay.…”

Section: Adhesion To Ecmmentioning

confidence: 99%

“…The procedure employed to obtain ECM removes adherent cells and leaves matrix components such as fibronectin, laminin, von Willebrand factor and collagens intact for binding to adhesive receptors expressed on cells. [46][47][48] Although we cannot formally exclude the possibility that Triton X-100 treatment removes potential ligand(s) for CD44v6 and CD44v9 from the matrix selectively and completely, these data collectively suggest that both CD44v6 and CD44v9 are involved in cell-cell interaction, rather than binding to matrix components.…”

Section: Figurementioning

confidence: 99%

CD44 variant isoforms are involved in plasma cell adhesion to bone marrow stromal cells

Driel

Günthert²,

Kessel³

et al. 2002

Leukemia

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Expression of CD44v9-containing isoforms (CD44v9) on myeloma plasma cells correlates with unfavorable prognosis, suggesting that CD44 variant molecules are involved in the disease process. In this study, the presence of CD44v on B cell lines from different stages of development was analyzed by flow cytometry and a role in adhesion to stromal cells from different tissues was evaluated in in vitro binding assays. CD44v3, v6 and v9 isoforms were exclusively expressed on plasma cell lines and CD44v9 expression correlated with IL-6-dependent plasma cell growth. Binding studies using CD44 isoformspecific reagents showed that CD44v6 and CD44v9 were involved in binding to bone marrow stromal cells, but not to in vitro synthesized ECM or hyaluronic acid. CD44v9-mediated plasma cell binding resulted in a significant induction of IL-6 secretion by bone marrow stromal cells. Large differences in quantitative plasma cell binding to stromal cells from different tissues were observed. These, however, could not be related to a differential use of CD44v in these binding processes. The role of CD44v9 in adhesion induced IL-6 secretion and its preferential expression on IL-6-dependent plasma cell lines may explain the previously observed correlation between CD44v9 expression and adverse prognosis in multiple myeloma.

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Cultured Endothelial Cells Regulate Platelet Adhesion to their Extracellular Matrix by Regulating its von Willebrand Factor Content

Cited by 14 publications

References 30 publications

Neomycin inhibits angiogenin-induced angiogenesis

Neomycin inhibits angiogenin-induced angiogenesis

Fibronectin in an Extracellular Matrix of Cultured Endothelial Cells Supports Platelet Adhesion via Its Ninth Type III Repeat

CD44 variant isoforms are involved in plasma cell adhesion to bone marrow stromal cells

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