The assembly and structure of the fibrin clot.
This review summarizes our current understanding of the structure of the fibrinogen molecule, its conversion to fibrin, and the main features of fibrin clot assembly and crosslinking. Several major aspects of fibrin matrix assembly and crosslinking are newly discovered, and differ significantly from more traditional views of fibrin structure. The new information that I have summarized will be of importance for correctly understanding the role that fibrin plays in the hemostatic process, and for learning how the structure of the fibrin clot network contributes to its strength, elasticity, interactions with cells, tissue matrix, and its susceptibility to fibrinolysis.
Mosesson
M W
MW
University of Wisconsin Medical School, Sinai Samaritan Medical Center, Milwaukee 53201.
D000595:Amino Acid Sequence; D001777:Blood Coagulation; D005337:Fibrin / Q000096:biosynthesis / Q000648:ultrastructure*; D005340:Fibrinogen / Q000378:metabolism / Q000648:ultrastructure*; D005342:Fibrinolysis; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011108:Polymers; D011487:Protein Conformation
D011108:Polymers; D005337:Fibrin; D005340:Fibrinogen