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Cell proliferation on fibrin: modulation by fibrinopeptide cleavage
LA Sporn, LA Bunce and CW Francis
Department of Medicine, University of Rochester School of Medicine &
Dentistry, NY 14642, USA.
Fibrin forms the cohesive network of hemostatic plugs and thrombi, and it
also provides the temporary matrix for initial support of healing and
revascularization. Because cell proliferation is needed for
revascularization after vessel injury, we have characterized structural
requirements of fibrin needed to support cell proliferation on fibrin in
vitro. Proliferation of cultured human endothelial cells and fibroblasts
was measured by 3H-thymidine incorporation on fibrin surfaces varying in
structure. Fibrin prepared with thrombin and lacking both fibrinopeptides A
and B (desAB fibrin) supported proliferation of both endothelial cells and
fibroblasts. In contrast, fibrin prepared with reptilase, which cleaves
only fibrinopeptide A, supported significantly less proliferation. Also,
fibrin prepared by thrombin treatment of fibrinogen lacking residues beta
1-42 supported only a low level of proliferation. Therefore, fibrinopeptide
B cleavage and exposure of beta 15-42 enhanced proliferation of cells on
fibrin. Specific proteolytic inhibitors were used to eliminate the
potential mitogenic effects of residual fibrin-bound thrombin. Additional
controls showed that neither catalytically inactive thrombin nor addition
of the thrombin receptor-activating peptide (SFLLRNPNDKYEPF [SFLL])
stimulated proliferation on desA fibrin. The results indicate that cell
proliferation on fibrin is enhanced by fibrinopeptide B cleavage and
exposure of the amino terminus of the fibrin beta chain. They also show
that specific structural features of the temporary fibrin matrix formed at
sites of injury may modulate the proliferative response of vascular cells.
Volume 86,
Issue 5,
pp. 1802-1810,
09/01/1995
Copyright © 1995 by The American Society of Hematology
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