Fetal fibrinogen and fibrinogen Paris I: Comparative fibrin monomers aggregation studies

Abstract

Comparative studies have demonstrated that in human cord the conversion of fibrinogen to fibrin by thrombin led to the appearance of fibrin monomers that had an aggregation profile that differed from the adult. The aggregation rate and the final recorded absorbance were respectively slower and lower for the cord fibrin monomers. The action of thrombin on fibrinogen derived from bovine fetus led to the appearance of fibrin monomers that had the same characteristics described for human cord monomers. In addition two different features were observed: the monomers had an inhibitory effect on the aggregation of cow monomers and a second population “soluble fibrin monomers” was observed. Whether these differences were related to species specificity or to the degree of gestation is not known. The study of the congenital and inherited fibrinogen Paris I showed that the aggregation step of the fibrinogen to fibrin conversion was abnormal. In addition the fibrin monomers had an inhibitory effect on the aggregation of normal fibrin monomers and, a second population “soluble fibrin monomers” was observed. The fact that the same observations were made while studying the aggregation of bovine fetus fibrin monomers and the abnormal fibrinogen Paris I may be fortuitous. It may also allow to raise the question whether or not some cases of abnormal fibrinogen are related to the persistance of fetal fibrinogen. Biochemical data would still be necessary to sustain such a hypothesis.