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Thromb Haemost 2000; 83(05): 736-741
DOI: 10.1055/s-0037-1613902
Review Article
Schattauer GmbH

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
› Author AffiliationsThis 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.
Further Information

Publication History

Received 15 October 1999

Accepted after resubmission 11 January 2000

Publication Date:
08 December 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.

Key words

Fibrinogen - FGF-2 - trypsin - proteolysis
 

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