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J Biol Chem, Vol. 273, Issue 8, 4350-4359, February 20, 1998
From the Department of Anatomy and Cell Biology, University of
Melbourne, Victoria, Australia 3052, the ¶ Walter and Eliza Hall
Institute of Medical Research, Royal Melbourne Hospital, Victoria,
Australia 3050, and the § CRC Medical Oncology Department,
University of Manchester, Christie CRC Research Centre,
Manchester, M20 4BX United Kingdom
Heparan 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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