The fibrinogen molecule plays a crucial role in blood coagulation. It is composed of 3 distinct chains named Aα, Bβ, and γ, coded respectively by FGA, FGB, and FGG genes. Any mutation occurring in one of these genes can lead to a fibrinogen disorder. However, their phenotypic impact is often difficult to assess. Here, we present 3 different approaches to study these mutations using the zebrafish as a functional model. We focused on well-documented mutations in human dysfibrinogenemia: γR301C and γR301H. The first approach consists of performing a knockdown of the fgg gene via a morpholino combined with a transgenic cDNA expression. The second is to create a new zebrafish line with a large deletion of the fgg and perform cDNA transgenic expression. The third is to create fish with the corresponding γR301C and γR301H mutations using CRISPR-Cas9. Our first results confirm that these mutations significantly increase the time to occlusion (TTO) in zebrafish. Further studies are needed to validate the effectiveness of all approaches.