[Molecular mechanisms of the polymerization of fibrin and the formation of its three-dimensional network].
The results of biochemical, immunochemical, and X-ray studies of the structures of fibrinogen and fibrin molecules were analyzed. The mechanisms of the successive formation of the fibrin three-dimensional network were described: the polymerization of monomeric molecules with the formation of bifilar protofibrils, the lateral association of protofibrils, and the embranchment of the forming fibrils. Data on the electron and confocal microscopy of the polymeric fibrin were considered. The role of the known polymerization centers of fibrin which participated in the formation of protofibrils and their lateral association was discussed. Data on the existence of the previously unknown polymerization centers were given. In particular, the experimental results demonstrated that one of such centers which participated in the formation of protofibrils was located in the Bbeta12-46 fragment, and did not require the cleavage of fibrinopeptide B for its functioning. The results of the computer modeling of the spatial structure of the fibrin(ogen) molecule and the intermolecular interactions in the course of the fibrin polymerization were presented. The location of the alphaC domains in the fibrin(ogen) molecule and their role in the polymerization process were discussed. Information on the structure of the calcium-binding sites of fibrin(ogen) and the functional role of Ca2+ in fibrin polymerization was published. The structure of factor XIII(a) and the mechanisms of fibrin stabilization by this factor were briefly described.
Lugovskoĭ
E V
EV
Gritsenko
P G
PG
Komisarenko
S V
SV
D000595:Amino Acid Sequence; D000818:Animals; D001704:Biopolymers / Q000737:chemistry; D005337:Fibrin / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary
D001704:Biopolymers; D005337:Fibrin