Endothelial cell-derived basic fibroblast growth factor: synthesis and deposition into subendothelial extracellular matrix.

Abstract

Bovine aortic and corneal endothelial cells synthesize a growth factor that remains mostly cell-associated but can also be extracted from the subendothelial extracellular matrix (ECM) deposited by these cells. The endothelial cellderived growth factors extracted from cell lysates and from the extracellular matrix appear to be structurally related to basic fibroblast growth factor by the criteria that they (i) bind to heparin-Sepharose and are eluted at 1.4-1.6 M NaCl, (ii) have a molecular weight of about 18,400, (iii) cross-react with anti-basic fibroblast growth factor antibodies when analyzed by electrophoretic blotting and immunoprecipitation, and (iv) are potent mitogens for bovine aortic and capillary endothelial cells. It is suggested that endothelium can store growth factors capable of autocrine growth promotion in two ways: by sequestering growth factor within the cell and by incorporating it into the underlying extracellular matrix.

Antibodies against basic fibroblast growth factor inhibit the autocrine growth of pulmonary artery endothelial cells

“…To confirm that the BAE cells used in this study produced bFGF as reported for other endothelial cells [6,7], a BAE cell-free extract was examined for its proliferative activity on BCE cells. As Fraction number Fig.4.…”

“…Vascular and capillary endothelial cells produce bFGF [6,7] and specific receptors are expressed on the cell surface [8][9][10][11]. These observations suggest that bFGF might be an autocrine growth factor of endothelial cells.…”

Human CYR61-mediated enhancement of bFGF-induced DNA synthesis in human umbilical vein endothelial cells

“…Plates coated with cell-free subendothelial extracellular matrix was prepared as described (Vlodavsky et al, 1987). Brie¯y, HUVECs were grown in 6-well plates (Falcon) as described above, culture media was changed every 3 days.…”

“…bFGF was iodinated essentially as described (Vlodavsky et al, 1987). Brie¯y, bFGF in 0.2 M sodium-phosphate bu er, pH 7.2 was labeled with 125 I (Na 125 I, 333 mCi/ml, NEN) in the presence of Iodo-Beads (Pierce) (5 min, room temperature).…”

“…Binding to ECM-coated plates and subsequent release of iodinated bFGF were performed as described (Vlodavsky et al, 1987). ECM-coated plates prepared as described above were preheated (1 h, 808C) to inactivate possible proteolytic activity residing in the ECM.…”