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J Biol Chem, Vol. 273, Issue 13, 7303-7310, March 27, 1998

Interaction of Heparan Sulfate from Mammary Cells with Acidic Fibroblast Growth Factor (FGF) and Basic FGF
REGULATION OF THE ACTIVITY OF BASIC FGF BY HIGH AND LOW AFFINITY BINDING SITES IN HEPARAN SULFATE

Hassan Rahmoune, Hai-Lan Chen, John T. Gallagher^§, Philip S. Rudland, and David G. Fernig

From the  School of Biological Sciences, Life Sciences Building, University of Liverpool, Crown Street, Liverpool L69 7ZB and the ^§ Cancer Research Campaign Department of Medical Oncology, Christie Hospital, Wilmslow Road, Manchester M20 9BX, United Kingdom

We have determined the relationship between the binding sites for acidic fibroblast growth factor (aFGF) and basic FGF (bFGF) in heparan sulfate (HS) prepared from a panel of mammary cell lines and the ability of the HS to activate aFGF and bFGF in DNA synthesis assays. The k_a of the HS for aFGF fell into three groups, whereas the k_d (0.0015-0.016 s¹) and the K_d (0.4-8.6 µM) formed a continuum. bFGF possessed a high affinity binding site (K_d 22-30 nM) with a fast k_a (320,000-550,000 M¹ s¹), termed "fast/high," and a lower affinity site (K_d 47-320 nM) with a slower k_a (35,000-150,000 M¹ s¹), termed "slow/low." Most of the species of HS possessed the latter binding site, which was able to activate bFGF in HS-deficient fibroblasts. However, the HS from the culture medium of the mammary fibroblasts and the myoepithelial-like cells possessed both a fast/high and a slow/low binding site and could not activate bFGF, although it could potentiate the growth-stimulatory activity of aFGF. Treatment of the HS possessing two binding sites for bFGF with heparitinase 1 released oligosaccharides that were able to restore the activity of bFGF in HS-deficient fibroblasts.

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