Abstract

Fibrinogen (FBG) has long been regarded as serving essentially a hemostatic role by its conversion from a soluble, plasma protein to an insoluble fibrin gel. However, several extrahepatic sites of FBG biosynthesis have been identified. Indeed, we have demonstrated that both lung epithelial cell derived and plasma FBG assemble into the extracellular matrix (ECM) of epithelial cells and fibroblasts. In this report, we determined that FBG assembly into the ECM is a cell dependent step that occurs in the absence of de novo protein synthesis. Using an in vitro model of wound repair, we examined the role of FBG in modulating gene expression. Data collected from cDNA array analysis indicated that FBG downregulates steady state levels of fibronectin mRNA, whereas cyclin D1 mRNA levels were upregulated in fibroblasts. Taken together, these data suggest that FBG may function independently of hemostasis in cellular adhesive interactions to modulate cellular signaling processes during wound repair.