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Related Experiment Videos

Endogenous basic fibroblast growth factor isoforms involved in different intracellular protein complexes

V Patry1, B Bugler, A Maret

  • 1INSERM U397, Institut Louis Bugnard, CHU Rangueil, Toulouse, France.

The Biochemical Journal
|August 15, 1997
PubMed
Summary

Different forms of basic fibroblast growth factor (bFGF) exhibit distinct cellular roles. These bFGF isoforms associate with different protein complexes in the nucleus and cytoplasm, indicating varied functional activities.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Basic fibroblast growth factor (bFGF), also known as FGF-2, exists in multiple isoforms.
  • These isoforms arise from alternative translation initiation sites (AUG and CUG codons).
  • Different bFGF forms possess distinct intracellular biological activities.

Purpose of the Study:

  • To identify the intracellular targets of different bFGF isoforms.
  • To investigate the subcellular localization and complex formation of bFGF variants.
  • To elucidate the functional implications of isoform-specific interactions.

Main Methods:

  • Transfection of bFGF isoforms (155- and 210-amino acid) into CHO cells.
  • Verification of subcellular localization (cytoplasmic vs. nuclear).

Related Experiment Videos

  • Radiation fragmentation assay to determine complex sizes.
  • Co-immunoprecipitation assays with chimeric proteins.

    • Main Results:

    • The 155-amino acid bFGF localized to the cytoplasm, while the 210-amino acid form localized to the nucleus.
    • The 155- and 210-amino acid bFGF isoforms were found in protein complexes of approximately 130 kDa and 320 kDa, respectively.
    • Different cellular proteins associate with distinct regions of the bFGF molecule, confirmed in both transfected CHO and native SK-Hep1 cells.

    Conclusions:

    • bFGF isoforms form distinct molecular complexes within the cytosol and nucleus.
    • These isoform-specific complexes suggest divergent functional roles for different bFGF variants.
    • Understanding these complexes is crucial for deciphering the multifaceted functions of bFGF.