Thromb Haemost 2000; 83(05): 736-741
DOI: 10.1055/s-0037-1613902
Review Article
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Fibrinogen and Fibrin Protect Fibroblast Growth Factor-2 from Proteolytic Degradation

Abha Sahni
1   From the Vascular Medicine Unit, Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY, USA
,
Christopher A. Baker
1   From the Vascular Medicine Unit, Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY, USA
,
Lee Ann Sporn
1   From the Vascular Medicine Unit, Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY, USA
,
Charles W. Francis
1   From the Vascular Medicine Unit, Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY, USA
› Institutsangaben

This work was supported in part by Grant No. HL-30616 and HL-07152 from the National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland.
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Publikationsverlauf

Received 15. Oktober 1999

Accepted after resubmission 11. Januar 2000

Publikationsdatum:
08. Dezember 2017 (online)

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Summary

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.