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ATP-dependent stabilization and protection of fibroblast growth factor 2

Karsten Rose1, Ronald E Gast, Anna Seeger

  • 1Institut für Pharmazeutische und Medizinische Chemie, Westfälische Wilhelms-Universität Münster, Germany. rosek@uni-muenster.de

Journal of Biotechnology
|October 20, 2009
PubMed

Insights

Adenosine triphosphate (ATP) and similar compounds stabilize fibroblast growth factor 2 (FGF2), protecting it from degradation. This stabilization enhances FGF2's effectiveness in cell culture, suggesting potential medical applications.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Regenerative Medicine

Background:

  • Fibroblast growth factor 2 (FGF2) is crucial for cell proliferation, angiogenesis, and neuroprotection.
  • Clinical trials utilize FGF2 for bone regeneration, wound healing, and cardioprotection.
  • Inadequate stability of FGF2 post-application is a significant challenge.

Purpose of the Study:

  • To investigate the protective effects of adenosine triphosphate (ATP) and other nucleoside triphosphates on FGF2 stability.
  • To determine the mechanism and efficacy of ATP-mediated FGF2 stabilization.

Main Methods:

  • In vitro protease digestion assays using trypsin, plasmin, and neutrophile elastase.
  • Assessment of ATP binding capacity using a mutant FGF2.
  • Cell culture experiments evaluating FGF2-dependent proliferation of human umbilical vein endothelial cells.

Main Results:

  • ATP, other nucleoside triphosphates, and sodium triphosphate protected FGF2 from protease digestion.
  • A 2:1 molar ratio of ligand to FGF2 was sufficient for protection.
  • The protective effect was dependent on the number of phosphate residues (ATP > ADP > AMP).
  • Alkaline phosphatase abolished ATP's protective effect.
  • A mutant FGF2 with reduced ATP-binding capacity showed no protease resistance with ATP.
  • ATP-bound FGF2 enhanced endothelial cell proliferation after protease or heat treatment.

Conclusions:

  • Nucleoside triphosphates, particularly ATP, effectively stabilize FGF2 against protease degradation.
  • ATP binding is critical for this protective effect.
  • Stabilized FGF2 demonstrates enhanced biological activity in cell culture.
  • Nucleoside triphosphate stabilization offers promising avenues for FGF2's medical applications.

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