Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate

1993 ◽  
Vol 124 (2) ◽  
pp. 121-129 ◽  
Author(s):  
Angelo G. Gambarini ◽  
Catarina A. Miyamoto ◽  
Geovani A. Lima ◽  
Helena B. Nader ◽  
Carl P. Dietrich
Keyword(s):  
Growth Factor ◽  
Heparan Sulfate ◽  
Fibroblast Growth Factor ◽  
Mitogenic Activity ◽  
Fibroblast Growth ◽  
Acidic Fibroblast Growth Factor ◽  
Sulfated Oligosaccharides

scholarly journals Interaction of Heparan Sulfate from Mammary Cells with Acidic Fibroblast Growth Factor (FGF) and Basic FGF

1998 ◽  
Vol 273 (13) ◽  
pp. 7303-7310 ◽  
Author(s):  
Hassan Rahmoune ◽  
Hai-Lan Chen ◽  
John T. Gallagher ◽  
Philip S. Rudland ◽  
David G. Fernig
Keyword(s):  
Growth Factor ◽  
Heparan Sulfate ◽  
Fibroblast Growth Factor ◽  
Mammary Cells ◽  
Fibroblast Growth ◽  
Acidic Fibroblast Growth Factor ◽  
Basic Fgf

Strategy for fluorescent labeling of human acidic fibroblast growth factor without impairment of mitogenic activity: A bona fide tracer

2011 ◽  
Vol 411 (1) ◽  
pp. 1-9 ◽  
Author(s):  
M. José Feito ◽  
Mercedes Jiménez ◽  
Concha Fernández-Cabrera ◽  
Germán Rivas ◽  
Guillermo Giménez-Gallego ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fluorescent Labeling ◽  
Mitogenic Activity ◽  
Fibroblast Growth ◽  
Acidic Fibroblast Growth Factor ◽  
Bona Fide

Extracellular matrix heparan sulfate proteoglycans modulate the mitogenic capacity of acidic fibroblast growth factor

1989 ◽  
Vol 140 (3) ◽  
pp. 584-592 ◽  
Author(s):  
Portia B. Gordon ◽  
Haing U. Choi ◽  
Greg Conn ◽  
Asra Ahmed ◽  
Bettina Ehrmann ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Growth Factor ◽  
Heparan Sulfate ◽  
Fibroblast Growth Factor ◽  
Heparan Sulfate Proteoglycans ◽  
Fibroblast Growth ◽  
Acidic Fibroblast Growth Factor

scholarly journals Thrombin-induced release of active basic fibroblast growth factor- heparan sulfate complexes from subendothelial extracellular matrix

Blood ◽  
1993 ◽  
Vol 81 (12) ◽  
pp. 3324-3331 ◽  
Author(s):  
M Benezra ◽  
I Vlodavsky ◽  
R Ishai-Michaeli ◽  
G Neufeld ◽  
R Bar-Shavit
Keyword(s):  
Extracellular Matrix ◽  
Growth Factor ◽  
Heparan Sulfate ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Mitogenic Activity ◽  
Angiogenic Factor ◽  
Fibroblast Growth ◽  
Tgf Beta ◽  
Large Reservoir

Abstract The angiogenic factor, basic fibroblast growth factor (bFGF), is sequestered and protected by binding to heparan sulfate proteoglycans (HSPG) in the subendothelial extracellular matrix (ECM). Release of ECM- bound bFGF provides a novel mechanism for regulation of cell proliferation and neovascularization in normal and pathologic situations. Exposure of ECM to thrombin, the final activation product of the clotting cascade, resulted in release of high molecular weight HSPG-bFGF complex, as indicated by its immunoprecipitation with anti- bFGF antibodies, susceptibility to degradation by bacterial heparinase, and inhibition of its mitogenic activity in the presence of neutralizing anti-bFGF antibodies. The ECM-resident bFGF-HSPG complex was not released by thrombin in the presence of hirudin or antithrombin III, or by catalytically blocked thrombin preparations. A threefold to fivefold higher mitogenic activity was released by thrombin from ECM that was preheated (1 hour, 80 degrees C), as compared with native ECM. This difference is attributed to heat stable bFGF-HSPG complexes that are more readily released after heat treatment of the ECM and to activation and release of ECM-resident transforming growth factor-beta (TGF-beta) activity. Our results indicate that the large reservoir of proteolytic activity present in plasma in the form of prothrombin may participate in release from the subendothelial ECM of biologically active bFGF and TGF-beta, depending on the accessibility of thrombin. Thrombin may gain access to the subendothelium on clot formation after tissue injury and as a result of the conversion of prothrombin to thrombin induced by the ECM itself.

scholarly journals Heparan Sulfate Oligosaccharides Require 6-O-Sulfation for Promotion of Basic Fibroblast Growth Factor Mitogenic Activity

1998 ◽  
Vol 273 (36) ◽  
pp. 22936-22942 ◽  
Author(s):  
David A. Pye ◽  
Romain R. Vives ◽  
Jeremy E. Turnbull ◽  
Patricia Hyde ◽  
John T. Gallagher
Keyword(s):  
Growth Factor ◽  
Heparan Sulfate ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Mitogenic Activity ◽  
Fibroblast Growth ◽  
Heparan Sulfate Oligosaccharides

Retina Protective Effect of Acidic Fibroblast Growth Factor after Canceling Its Mitogenic Activity

2008 ◽  
Vol 24 (5) ◽  
pp. 445-452 ◽  
Author(s):  
Hua Xu ◽  
Jin-Nan Yang ◽  
Xiao-Kun Li ◽  
Qing Zheng ◽  
Wen Zhao ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protective Effect ◽  
Fibroblast Growth Factor ◽  
Mitogenic Activity ◽  
Fibroblast Growth ◽  
Acidic Fibroblast Growth Factor

scholarly journals Thrombin-induced release of active basic fibroblast growth factor- heparan sulfate complexes from subendothelial extracellular matrix

Blood ◽  
1993 ◽  
Vol 81 (12) ◽  
pp. 3324-3331 ◽  
Author(s):  
M Benezra ◽  
I Vlodavsky ◽  
R Ishai-Michaeli ◽  
G Neufeld ◽  
R Bar-Shavit
Keyword(s):  
Extracellular Matrix ◽  
Growth Factor ◽  
Heparan Sulfate ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Mitogenic Activity ◽  
Angiogenic Factor ◽  
Fibroblast Growth ◽  
Tgf Beta ◽  
Large Reservoir

The angiogenic factor, basic fibroblast growth factor (bFGF), is sequestered and protected by binding to heparan sulfate proteoglycans (HSPG) in the subendothelial extracellular matrix (ECM). Release of ECM- bound bFGF provides a novel mechanism for regulation of cell proliferation and neovascularization in normal and pathologic situations. Exposure of ECM to thrombin, the final activation product of the clotting cascade, resulted in release of high molecular weight HSPG-bFGF complex, as indicated by its immunoprecipitation with anti- bFGF antibodies, susceptibility to degradation by bacterial heparinase, and inhibition of its mitogenic activity in the presence of neutralizing anti-bFGF antibodies. The ECM-resident bFGF-HSPG complex was not released by thrombin in the presence of hirudin or antithrombin III, or by catalytically blocked thrombin preparations. A threefold to fivefold higher mitogenic activity was released by thrombin from ECM that was preheated (1 hour, 80 degrees C), as compared with native ECM. This difference is attributed to heat stable bFGF-HSPG complexes that are more readily released after heat treatment of the ECM and to activation and release of ECM-resident transforming growth factor-beta (TGF-beta) activity. Our results indicate that the large reservoir of proteolytic activity present in plasma in the form of prothrombin may participate in release from the subendothelial ECM of biologically active bFGF and TGF-beta, depending on the accessibility of thrombin. Thrombin may gain access to the subendothelium on clot formation after tissue injury and as a result of the conversion of prothrombin to thrombin induced by the ECM itself.

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