Mutations in the heparin-binding domains of human basic fibroblast growth factor alter its biological activity

Biochemistry ◽  
1991 ◽  
Vol 30 (22) ◽  
pp. 5608-5615 ◽  
Author(s):  
William F. Heath ◽  
Amanda S. Cantrell ◽  
Nancy G. Mayne ◽  
S. Richard Jaskunas
Keyword(s):  
Biological Activity ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Fibroblast Growth ◽  
Heparin Binding ◽  
Binding Domains

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.

In Vitro Assessment of the Biological Activity of Basic Fibroblast Growth Factor Released from Various Polymers and Biomatrices

1997 ◽  
Vol 12 (1) ◽  
pp. 31-56 ◽  
Author(s):  
Marilyn J. Davies ◽  
Christopher A. Mitchell ◽  
Moira A. L. Maley ◽  
Miranda D. Grounds ◽  
Alan R. Harvey ◽  
...  
Keyword(s):  
Biological Activity ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Fibroblast Growth ◽  
In Vitro Assessment
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