Expression of basic fibroblast growth factor (bFGF), FGF receptor 1 and FGF receptor 2 in uterine leiomyomas and myometrium during the menstrual cycle, after menopause and GnRHa treatment*

2001 ◽  
Vol 80 (6) ◽  
pp. 497-504 ◽  
Author(s):  
Xuxia Wu ◽  
Agneta Blanck ◽  
Matts Olovsson ◽  
Björn Möller ◽  
Bo Lindblom
Keyword(s):  
Growth Factor ◽  
Menstrual Cycle ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Uterine Leiomyomas ◽  
Fibroblast Growth ◽  
Fgf Receptor

scholarly journals Oligomeric self-association of basic fibroblast growth factor in the absence of heparin-like glycosaminoglycans

1999 ◽  
Vol 341 (3) ◽  
pp. 613-620 ◽  
Author(s):  
Joseph C. DAVIS ◽  
Ganesh VENKATARAMAN ◽  
Zachary SHRIVER ◽  
P. Antony RAJ ◽  
Ram SASISEKHARAN
Keyword(s):  
Biological Activity ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Fibroblast Growth ◽  
Heparin Binding ◽  
Fgf Receptor ◽  
Natural Tendency ◽  
Heparin Binding Growth Factors ◽  
Self Association

Basic fibroblast growth factor (FGF-2) represents a class of heparin-binding growth factors that are stored in the extracellular matrix attached to heparin-like glycosaminoglycans (HLGAGs). It has been proposed that cell surface HLGAGs have a central role in the biological activity of FGF-2, presumably by inducing dimers or oligomers of FGF-2 and leading to the dimerization or oligomerization of FGF receptor and hence signal transduction. We have previously proposed that FGF-2 possesses a natural tendency to self-associate to form FGF-2 dimers and oligomers; HLGAGs would enhance FGF-2 self-association. Here, through a combination of spectroscopic, chemical cross-linking and spectrometric techniques, we provide direct evidence for the self-association of FGF-2 in the absence of HLGAGs, defying the notion that HLGAGs induce FGF-2 oligomerization. Further, the addition of HLGAGs seems to enhance significantly the FGF-2 oligomerization process without affecting the relative percentages of FGF-2 dimers, trimers or oligomers. FGF-2 self-association is consistent with FGF-2's possessing biological activity both in the presence and in the absence of HLGAGs; this leads us to propose that FGF-2 self-association enables FGF-2 to signal both in the presence and in the absence of HLGAGs.

Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells

1992 ◽  
Vol 12 (1) ◽  
pp. 240-247
Author(s):  
D M Ornitz ◽  
A Yayon ◽  
J G Flanagan ◽  
C M Svahn ◽  
E Levi ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Receptor Binding ◽  
Receptor Activation ◽  
Soluble Form ◽  
Placental Alkaline Phosphatase ◽  
Fibroblast Growth ◽  
Fgf Receptor

Heparin is required for the binding of basic fibroblast growth factor (bFGF) to high-affinity receptors on cells deficient in cell surface heparan sulfate proteoglycan. So that this heparin requirement could be evaluated in the absence of other cell surface molecules, we designed a simple assay based on a genetically engineered soluble form of murine FGF receptor 1 (mFR1) tagged with placental alkaline phosphatase. Using this assay, we showed that FGF-receptor binding has an absolute requirement for heparin. By using a cytokine-dependent lymphoid cell line engineered to express mFR1, we also showed that FGF-induced mitogenic activity is heparin dependent. Furthermore, we tested a series of small heparin oligosaccharides of defined lengths for their abilities to support bFGF-receptor binding and biologic activity. We found that a heparin oligosaccharide with as few as eight sugar residues is sufficient to support these activities. We also demonstrated that heparin facilitates FGF dimerization, a property that may be important for receptor activation.

scholarly journals Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells.

1992 ◽  
Vol 12 (1) ◽  
pp. 240-247 ◽  
Author(s):  
D M Ornitz ◽  
A Yayon ◽  
J G Flanagan ◽  
C M Svahn ◽  
E Levi ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Receptor Binding ◽  
Receptor Activation ◽  
Soluble Form ◽  
Placental Alkaline Phosphatase ◽  
Fibroblast Growth ◽  
Fgf Receptor

Heparin is required for the binding of basic fibroblast growth factor (bFGF) to high-affinity receptors on cells deficient in cell surface heparan sulfate proteoglycan. So that this heparin requirement could be evaluated in the absence of other cell surface molecules, we designed a simple assay based on a genetically engineered soluble form of murine FGF receptor 1 (mFR1) tagged with placental alkaline phosphatase. Using this assay, we showed that FGF-receptor binding has an absolute requirement for heparin. By using a cytokine-dependent lymphoid cell line engineered to express mFR1, we also showed that FGF-induced mitogenic activity is heparin dependent. Furthermore, we tested a series of small heparin oligosaccharides of defined lengths for their abilities to support bFGF-receptor binding and biologic activity. We found that a heparin oligosaccharide with as few as eight sugar residues is sufficient to support these activities. We also demonstrated that heparin facilitates FGF dimerization, a property that may be important for receptor activation.

Sign in / Sign up

Export Citation Format

Share Document