Fibrinogen and fibrin protect fibroblast growth factor-2 from proteolytic degradation

Abha Sahni, Christopher A. Baker, Lee Ann Sporn, Charles W. Francis

Research output: Contribution to journalArticlepeer-review

56 Scopus citations


We have recently reported that fibrinogen and fibrin bind to fibroblast growth factor-2 (FGF-2) and potentiate its ability to stimulate proliferation of endothelial cells. In the present report, we have investigated the potential of fibrinogen and fibrin to protect FGF-2 from proteolytic degradation. FGF-2 was incubated with trypsin or chymotrypsin in the presence or absence of fibrinogen or fibrin and proteolysis of FGF-2 was assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. In the absence of fibrinogen there was progressive tryptic degradation of FGF-2, but in the presence of fibrinogen, FGF-2 was completely protected from trypsin with no evidence of degradation. The degree of protection was maximum at a molar ratio of FGF-2 to fibrinogen 1:2. Fibrinogen afforded similar protection from degradation by chymotrypsin. Polymerized fibrin provided partial protection of FGF-2 from tryptic degradation, with intact FGF-2 present for up to 360 min. Fibrin provided nearly complete protection from chymotrypsin. These observations indicate that binding of FGF-2 to fibrinogen or fibrin provides protection from proteolytic degradation, and this may modulate its cell proliferative activity.

Original languageEnglish (US)
Pages (from-to)736-741
Number of pages6
JournalThrombosis and Haemostasis
Issue number5
StatePublished - 2000
Externally publishedYes


  • FGF-2
  • Fibrinogen
  • Proteolysis
  • Trypsin

ASJC Scopus subject areas

  • Hematology


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