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dc.contributor.authorBrickman, Y G
dc.contributor.authorFord, M D
dc.contributor.authorGallagher, John T
dc.contributor.authorNurcombe, V
dc.contributor.authorBartlett, P F
dc.contributor.authorTurnbull, Jeremy E
dc.date.accessioned2010-02-25T11:47:15Z
dc.date.available2010-02-25T11:47:15Z
dc.date.issued1998-02-20
dc.identifier.citationStructural modification of fibroblast growth factor-binding heparan sulfate at a determinative stage of neural development. 1998, 273 (8):4350-9 J. Biol. Chem.en
dc.identifier.issn0021-9258
dc.identifier.pmid9468484
dc.identifier.urihttp://hdl.handle.net/10541/93027
dc.description.abstractHeparan sulfate (HS) glycosaminoglycans are essential modulators of fibroblast growth factor (FGF) activity and appear to act by coupling particular forms of FGF to appropriate FGF receptors. During neural development, one particular HS proteoglycan is able to rapidly switch its potentiating activity from FGF-2, as neural precursor cell proliferation occurs, to FGF-1, as neuronal differentiation occurs. Using various analytical techniques, including chemical and enzymatic cleavage, low pressure chromatography, and strong anion-exchange high performance liquid chromatography, we have analyzed the different HSs expressed during these crucial developmental stages. There are distinct alterations in patterns of 6-O-sulfation, total chain length, and the number of sulfated domains of the HS from the more mature embryonic brain. These changes correlate with a switch in the ability of the HS to potentiate the actions of FGF-1 in triggering cell differentiation. It thus appears that each HS pool is designed to function in the modulation of an intricate interaction with a specific growth factor and its cognate receptor, and suggests tightly regulated expression of specific, bioactive disaccharide sequences. The data can be used to construct a simple model of controlled variations in HS chain structure which have functional consequences at a crucial stage of neuronal maturation.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCells, Cultured
dc.subject.meshChromatography, Gel
dc.subject.meshChromatography, High Pressure Liquid
dc.subject.meshFibroblast Growth Factors
dc.subject.meshHeparitin Sulfate
dc.subject.meshHydrogen-Ion Concentration
dc.subject.meshMice
dc.subject.meshModels, Chemical
dc.subject.meshMolecular Structure
dc.subject.meshNitrous Acid
dc.subject.meshOligosaccharides
dc.titleStructural modification of fibroblast growth factor-binding heparan sulfate at a determinative stage of neural development.en
dc.typeArticleen
dc.contributor.departmentDepartment of Anatomy and Cell Biology, University of Melbourne, Victoria, Australia 3052.en
dc.identifier.journalThe Journal of Biological Chemistryen
html.description.abstractHeparan sulfate (HS) glycosaminoglycans are essential modulators of fibroblast growth factor (FGF) activity and appear to act by coupling particular forms of FGF to appropriate FGF receptors. During neural development, one particular HS proteoglycan is able to rapidly switch its potentiating activity from FGF-2, as neural precursor cell proliferation occurs, to FGF-1, as neuronal differentiation occurs. Using various analytical techniques, including chemical and enzymatic cleavage, low pressure chromatography, and strong anion-exchange high performance liquid chromatography, we have analyzed the different HSs expressed during these crucial developmental stages. There are distinct alterations in patterns of 6-O-sulfation, total chain length, and the number of sulfated domains of the HS from the more mature embryonic brain. These changes correlate with a switch in the ability of the HS to potentiate the actions of FGF-1 in triggering cell differentiation. It thus appears that each HS pool is designed to function in the modulation of an intricate interaction with a specific growth factor and its cognate receptor, and suggests tightly regulated expression of specific, bioactive disaccharide sequences. The data can be used to construct a simple model of controlled variations in HS chain structure which have functional consequences at a crucial stage of neuronal maturation.


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