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Related Experiment Videos

Structural features in heparin which modulate specific biological activities mediated by basic fibroblast growth

M Ishihara1, P N Shaklee, Z Yang

  • 1Glycomed Inc., Alameda, CA 94501.

Glycobiology
|August 1, 1994
PubMed
Summary

Heparin oligosaccharides

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Glycoscience

Background:

  • Basic fibroblast growth factor (bFGF) activity is modulated by heparin and heparan sulfate (HS) binding.
  • Heparin-derived oligosaccharides are crucial for understanding bFGF interactions and biological responses.
  • Previous studies showed varying effects of oligosaccharide size on bFGF binding and cell proliferation.

Purpose of the Study:

  • To investigate the structural requirements of heparin oligosaccharides for bFGF interaction and biological activity modulation.
  • To assess the role of specific sulfate groups and uronic acid carboxylates in bFGF binding.
  • To explore alternative functional groups that can substitute for uronic acid charges in modulating bFGF activity.

Main Methods:

  • Preparation and fractionation of size- and structure-defined oligosaccharides from modified heparins (e.g., 2-O-desulphated, 6-O-desulphated, carboxy-reduced, carboxy-amidomethylsulphonated).

Related Experiment Videos

  • Utilized bFGF-affinity chromatography to isolate relevant oligosaccharide fractions.
  • Assessed the inhibitory or enhancing effects of these oligosaccharides on specific bFGF-mediated biological activities.

    • Main Results:

    • Both 2-O-sulphate groups and the negative charge of uronic acid carboxylates (L-iduronic acid residues) are essential for specific heparin-bFGF interactions.
    • These structural features are critical for modulating bFGF's mitogenic activity.
    • The negative charge of uronic acid carboxylates can be functionally replaced by other negatively charged moieties, such as the amidomethyl sulphonate group.

    Conclusions:

    • Specific structural elements of heparin, particularly 2-O-sulphate and uronic acid charges, dictate its interaction with bFGF.
    • These interactions are key to modulating bFGF's biological functions, including cell proliferation.
    • The findings provide insights into the design of heparin mimetics for therapeutic applications involving bFGF.