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dc.contributor.authorRahmoune, H
dc.contributor.authorChen, H L
dc.contributor.authorGallagher, John T
dc.contributor.authorRudland, P S
dc.contributor.authorFernig, D G
dc.date.accessioned2010-02-23T13:00:15Z
dc.date.available2010-02-23T13:00:15Z
dc.date.issued1998-03-27
dc.identifier.citationInteraction 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. 1998, 273 (13):7303-10 J. Biol. Chem.en
dc.identifier.issn0021-9258
dc.identifier.pmid9516424
dc.identifier.urihttp://hdl.handle.net/10541/92753
dc.description.abstractWe 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 ka of the HS for aFGF fell into three groups, whereas the kd (0.0015-0.016 s-1) and the Kd (0.4-8.6 microM) formed a continuum. bFGF possessed a high affinity binding site (Kd 22-30 nM) with a fast ka (320,000-550,000 M-1 s-1), termed "fast/high," and a lower affinity site (Kd 47-320 nM) with a slower ka (35,000-150,000 M-1 s-1), 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.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshBinding Sites
dc.subject.meshBreast
dc.subject.meshCells, Cultured
dc.subject.meshEpithelial Cells
dc.subject.meshFemale
dc.subject.meshFibroblast Growth Factor 1
dc.subject.meshFibroblast Growth Factor 2
dc.subject.meshHeparitin Sulfate
dc.subject.meshHumans
dc.subject.meshKinetics
dc.subject.meshMammary Glands, Animal
dc.subject.meshMolecular Weight
dc.subject.meshProtein Binding
dc.subject.meshRats
dc.subject.meshRecombinant Proteins
dc.titleInteraction 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.en
dc.typeArticleen
dc.contributor.departmentSchool of Biological Sciences, Life Sciences Building, University of Liverpool, Crown Street, Liverpool L69 7ZB, United Kingdom.en
dc.identifier.journalThe Journal of Biological Chemistryen
html.description.abstractWe 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 ka of the HS for aFGF fell into three groups, whereas the kd (0.0015-0.016 s-1) and the Kd (0.4-8.6 microM) formed a continuum. bFGF possessed a high affinity binding site (Kd 22-30 nM) with a fast ka (320,000-550,000 M-1 s-1), termed "fast/high," and a lower affinity site (Kd 47-320 nM) with a slower ka (35,000-150,000 M-1 s-1), 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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