Characterization of a Mr 25,000 basic fibroblast growth factor form in adult, regenerating, and fetal rat liver

Biochem Biophys Res Commun. 1989 Nov 15;164(3):1182-9. doi: 10.1016/0006-291x(89)91794-4.


A heparin-binding Mr 25,000 immunoreactive bFGF-like protein (ir-bFGF) is recognized in adult rat liver extract by affinity-purified polyclonal anti-human placental bFGF antibodies. Hepatic levels of this protein increase 4-fold in regenerating rat liver during the first 48 h after partial hepatectomy. Also, they appear to be higher in embryonic than in newborn or in adult rat liver. Mr 25,000 ir-bFGF from regenerating rat liver, partially purified by heparin-affinity chromatography, induces plasminogen activator activity and cell proliferation in transformed fetal bovine aortic endothelial GM 7373 cells and competes with Mr 18,000 [125I]bFGF for the binding to high affinity bFGF receptors. The data indicate the presence in rat liver of a high molecular weight form of bFGF whose expression is modulated during embryonic development and liver regeneration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aging
  • Animals
  • Cattle
  • Cell Line
  • Chromatography, Affinity
  • Endothelium, Vascular / drug effects
  • Endothelium, Vascular / metabolism
  • Fetus
  • Fibroblast Growth Factors / isolation & purification*
  • Fibroblast Growth Factors / metabolism
  • Fibroblast Growth Factors / pharmacology
  • Immune Sera
  • Kinetics
  • Liver / embryology
  • Liver / growth & development
  • Liver / metabolism*
  • Liver Regeneration*
  • Male
  • Molecular Weight
  • Plasminogen Activators / biosynthesis
  • Rats
  • Rats, Inbred Strains
  • Receptors, Cell Surface / metabolism
  • Receptors, Fibroblast Growth Factor
  • Recombinant Proteins / metabolism
  • Reference Values


  • Immune Sera
  • Receptors, Cell Surface
  • Receptors, Fibroblast Growth Factor
  • Recombinant Proteins
  • Fibroblast Growth Factors
  • Plasminogen Activators