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FGF3 from Xenopus laevis

P Kiefer1, M Mathieu, M J Close

  • 1Imperial Cancer Research Fund, London, UK.

The EMBO Journal
|November 1, 1993
PubMed
Summary

Fibroblast growth factor 3 (FGF3) in Xenopus laevis (XFGF3) is secreted and binds to cell surfaces. It transforms cell morphology and stimulates DNA synthesis, with variations based on FGF receptor interactions.

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Area of Science:

  • Developmental Biology
  • Molecular Biology
  • Cell Biology

Background:

  • Fibroblast growth factor 3 (FGF3) initially identified as a mouse mammary tumor virus oncogene product.
  • Normal FGF3 function is primarily observed during embryonic development.

Purpose of the Study:

  • Investigate the function of FGF3 in Xenopus laevis by isolating and characterizing its homologue, XFGF3.
  • Understand the biochemical properties and biological activities of XFGF3.

Main Methods:

  • Isolation and expression of XFGF3 cDNA in COS-1 cells.
  • Characterization of XFGF3 protein products (p31 and p27) including secretion, cell surface association, and glycosylation.
  • Analysis of XFGF3 binding to heparin-Sepharose and displacement by soluble heparin.
  • Assessment of XFGF3's ability to induce morphological transformation and DNA synthesis in various cell lines expressing FGF receptors.
  • Construction and analysis of XFGF3-mouse FGF3 chimeras.

Main Results:

  • XFGF3 cDNA expression yields a secreted, cell surface-associated 31 kDa protein (p31) and a truncated 27 kDa form (p27), both glycosylated.
  • Both XFGF3 forms bind heparin and can be displaced by soluble heparin.
  • Conditioned medium with XFGF3 induces morphological transformation in NIH3T3 cells and stimulates DNA synthesis in quiescent C57MG and BALB/MK cells.
  • Chimeric FGF3 proteins showed altered host range dependent on the proportion of mouse FGF3 sequences.

Conclusions:

  • XFGF3 exhibits distinct biochemical and functional properties compared to its mouse counterpart.
  • XFGF3 plays a role in cell signaling, influencing cell morphology and proliferation through interactions with FGF receptors.
  • Structural modifications, particularly involving the N-terminus, influence the specificity of FGF3 activity.

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