Evolution of vertebrate fibrin formation and the process of its dissolution

The thrombin-catalysed conversion of fibrinogen into a fibrin gel is common to all extant vertebrates. Because fibrin formation is both temporary and risky, an effective scheme for fibrinolysis evolved concomitantly. In this regard, the fibrinogen molecule is well adapted both for network polymerization and for subsequent dismantling. The question is, has it always been so? It has long been known that the three non-identical chains that compose vertebrate fibrinogen are descended from a common ancestor, and the original molecule must have been either a homotrimer or a dimer thereof. Three-dimensional studies on core fragments of fibrinogen are revealing new insights about both fibrin formation and its destruction. These studies are also showing exactly what structural changes have accompanied changes in function for the various domains. Chief among these is the reversal of direction for the alpha chain after replacement of its C-terminal domain.