A possible role for multidrug resistance-associated protein in the secretion of basic fibroblast growth factor by osteogenic sarcoma cell line (MG-63).

1998 ◽  
Author(s):  
S Aggarwal ◽  
S Gupta
Keyword(s):  
Multidrug Resistance ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Cell Line ◽  
Basic Fibroblast Growth Factor ◽  
Osteogenic Sarcoma ◽  
Fibroblast Growth ◽  
Sarcoma Cell ◽  
Sarcoma Cell Line

Characterization of the basic fibroblast growth factor-evoked proliferation of the human Müller cell line, MIO-M1

2004 ◽  
Vol 242 (5) ◽  
pp. 414-422 ◽  
Author(s):  
Margrit Hollborn ◽  
Karsten Jahn ◽  
G. Astrid Limb ◽  
Leon Kohen ◽  
Peter Wiedemann ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Cell Line ◽  
Basic Fibroblast Growth Factor ◽  
Müller Cell ◽  
Fibroblast Growth ◽  
Muller Cell

Characterisation of a laminarin sulphate which inhibits basic fibroblast growth factor binding and endothelial cell proliferation

1995 ◽  
Vol 108 (11) ◽  
pp. 3591-3598 ◽  
Author(s):  
R. Hoffman ◽  
D.H. Paper ◽  
J. Donaldson ◽  
S. Alban ◽  
G. Franz
Keyword(s):  
Cell Proliferation ◽  
Endothelial Cell ◽  
Growth Factor ◽  
Dna Synthesis ◽  
Fibroblast Growth Factor ◽  
Cell Line ◽  
Basic Fibroblast Growth Factor ◽  
Fibroblast Growth ◽  
Endothelial Cell Line ◽  
High Affinity

We have evaluated a series of laminarin sulphates with different degrees of sulphation (0.3-2.3) as antagonists of basic fibroblast growth factor (bFGF) and as inhibitors of the bFGF-dependent endothelial cell line FBHE. Inhibition of binding of bFGF by the laminarin sulphates increased with increasing degree of sulphation. Binding of bFGF to low affinity sites on BHK cells was inhibited more strongly than binding to high affinity sites. IC50 values for inhibition of binding to low and high affinity sites by the most highly sulphated laminarin sulphate (LAM S5; degree of sulphation 2.31) were 12 +/- 8 micrograms/ml and 69 +/- 66 micrograms/ml, respectively. LAM S5 dissociated bFGF from low affinity sites on BHK cells but not from high affinity sites. LAM S5 increased the electrophoretic mobility of bFGF indicating that LAM S5 binds directly to bFGF. LAM S5 reduced uptake of bFGF by FBHE cells by 67%. Increasing the degree of sulphation of laminarin sulphates increased the inhibition of bFGF-stimulated DNA synthesis of the endothelial cell line FBHE (IC50 for LAM S5 approx. 1 microgram/ml). There was no inhibition of DNA synthesis of FBHE cells by LAM S5 in the presence of 1 microgram/ml bFGF indicating that bFGF antagonism is involved in the anti-proliferative activity of this compound. LAM S5 may be of value against diseases associated with bFGF-dependent cell proliferation.

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