Ets-1 Upregulates Matrix Metalloproteinase-1 Expression through Extracellular Matrix Adhesion in Vascular Endothelial Cells

2002 ◽  
Vol 291 (1) ◽  
pp. 130-138 ◽  
Author(s):  
Shinji Naito ◽  
Shunichi Shimizu ◽  
Mutsumi Matsuu ◽  
Masahiro Nakashima ◽  
Toshiyuki Nakayama ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Matrix Metalloproteinase ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Matrix Adhesion ◽  
Matrix Metalloproteinase 1

Matrix Metalloproteinase-1 Expression by Interaction between Monocytes and Vascular Endothelial Cells

2000 ◽  
Vol 32 (8) ◽  
pp. 1459-1468 ◽  
Author(s):  
Yukihiro Hojo ◽  
Uichi Ikeda ◽  
Masafumi Takahashi ◽  
Yoichi Sakata ◽  
Toshihiro Takizawa ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Matrix Metalloproteinase ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Matrix Metalloproteinase 1

scholarly journals Fluvastatin Inhibits Matrix Metalloproteinase-1 Expression in Human Vascular Endothelial Cells

Hypertension ◽  
2000 ◽  
Vol 36 (3) ◽  
pp. 325-329 ◽  
Author(s):  
Uichi Ikeda ◽  
Masahisa Shimpo ◽  
Ruri Ohki ◽  
Hideko Inaba ◽  
Masafumi Takahashi ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Matrix Metalloproteinase ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Matrix Metalloproteinase 1

Interaction between vascular endothelial cells and vascular intimal spindle-shaped cells in vitro

1983 ◽  
Vol 60 (1) ◽  
pp. 89-102
Author(s):  
D de Bono ◽  
C. Green
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Vascular Endothelial Cells ◽  
Three Dimensional ◽  
Vascular Endothelial ◽  
Pure Cultures ◽  
Species Specific ◽  
Endothelial Growth Factor

The interactions between human or bovine vascular endothelial cells and fibroblast-like vascular intimal spindle-shaped cells have been studied in vitro, using species-specific antibodies to identify the different components in mixed cultures. Pure cultures of endothelial cells grow as uniform, nonoverlapping monolayers, but this growth pattern is lost after the addition of spindle cells, probably because the extracellular matrix secreted by the latter causes the endothelial cells to modify the way they are attached to the substrate. The result is a network of tubular aggregates of endothelial cells in a three-dimensional ‘polylayer’ of spindle-shaped cells. On the other hand, endothelial cells added to growth-inhibited cultures of spindle-shaped cells will grow in sheets over the surface of the culture. Human endothelial cells grown in contact with spindle-shaped cells have a reduced requirement for a brain-derived endothelial growth factor. The interactions of endothelial cells and other connective tissue cells in vitro may be relevant to the mechanisms of endothelial growth and blood vessel formation in vivo, and emphasize the potential importance of extracellular matrix in controlling endothelial cell behaviour.

scholarly journals High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells--implications for the modulation of FGF-2.

1995 ◽  
Vol 128 (6) ◽  
pp. 1221-1228 ◽  
Author(s):  
A Hanneken ◽  
P A Maher ◽  
A Baird
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Protein Interactions ◽  
Binding Proteins ◽  
Vascular Endothelial Cells ◽  
Extracellular Domain ◽  
Cytoplasmic Domain ◽  
Basement Membranes ◽  
Vascular Endothelial ◽  
High Affinity

We recently characterized three FGF-binding proteins (FGF-BPs) which are soluble forms of the extracellular domains of the high affinity FGF receptors (Hanneken, A. M., W. Ying, N. Ling, and A. Baird. Proc. Natl. Acad. Sci. USA. 1994. 91:9170-9174). These proteins circulate in blood and have been proposed to modulate the biological activity of the FGF family of proteins. Immunohistochemical studies now demonstrate that these soluble, truncated FGF receptors are also present in the basement membranes of retinal vascular endothelial cells. These immunoreactive proteins can be detected with antibodies raised to the extracellular domain of FGFR-1 but not with antibodies raised to either the juxtamembrane domain or the cytoplasmic domain of FGFR-1. Western blotting of human retinal extracts with the antibody raised to the extracellular domain of FGFR-1 detects specific, low molecular mass proteins at 85 kD and 55 kD, corresponding in size to the FGF-BPs, which are not detected with antibodies against the cytoplasmic domain of the receptor. The interaction of this receptor with the extracellular matrix is not dependent on the presence of FGF-2. Immunoreactive receptors are still detected in vascular basement membranes after the removal of FGF-2 with heparitinase. In addition, the recombinant extracellular domain of FGFR-1 continues to bind to corneal endothelial cell matrix after endogenous FGF-2 has been removed with 2 M NaCl. Acid treatment, which has been shown to disrupt protein interactions with the extracellular matrix, leads to a significant reduction in the presence of the matrix form of the FGF receptor. This loss can be restored with exogenous incubations of the recombinant extracellular domain of FGFR-1. This report is the first demonstration that a truncated form of a high affinity growth factor receptor can be localized to the extracellular matrix. These findings add to the list of binding proteins associated with the extracellular matrix (IGFBP-5) and suggest a potentially new regulatory mechanism for controlling the biological availability of FGF, and other peptide growth factors, in the extracellular matrix.

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