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Special Issue "Fibrinogen/Fibrin, Factor XIII and Fibrinolysis in Diseases"
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".
Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 44873
Special Issue Editors
Special Issue Information
In the final phase of coagulation cascade thrombin, a proteolytic enzyme of restricted substrate specificity is produced, which converts the soluble plasma protein fibrinogen into insoluble fibrin. Fibrinogen has a symmetrical hetero-trimeric structure, consisting of pairs of Aa, Bb and g chains. Thrombin cleaves short fibrinopeptides from the N-terminus of fibrinogen Aa chain and the Bb chain. The remaining a2b2g2 structure spontaneously polymerizes forming a fibrin clot. Such polymerized fibrin is still not stable enough to resist the shear stress of circulating blood and the proteolytic breakdown by the powerful fibrinolytic enzyme, plasmin. Stabilization of the fibrin clot is conferred by the activation of another coagulation factor, factor XIII (FXIII). FXIII is a hetero-tetramer of two potentially active A subunits (FXIII-A) and two inhibitory/protective B subunits (FXIII-B). It is activated by the concerted action of thrombin and Ca2+. Thrombin cleaves the activation peptide from FXIII-A and in the presence of Ca2+ the two subunits spontaneously dissociate allowing FXIII-A to assume an enzymatically active configuration. The active enzyme is a transglutaminase (FXIIIa) that crosslinks fibrin a and g chains and a2-plasmin inhibitor (a2-PI) to fibrin through e(g-glutamyl)lysyl bonds. This way FXIIIa mechanically strengthens fibrin and prevents its prompt fibrinolytic degradation.
The proper function of the terminal phase of coagulation cascade is essential for maintaining hemostasis. Inherited and acquired deficiencies of the three key components, fibrinogen, FXIII and a2-PI result in bleeding diathesis, while elevated plasma levels and certain polymorphisms can predispose to thromboembolic events. Many details concerning the involvement of these key proteins in the pathomechanism of different diseases remain unexplored. The aim of this special issue is to attract scientists working in this field, encourage them to publish their original results and share their views with the scientific community. It is our hope that the special issue will contribute to a better understanding of 1/ the biochemistry of the terminal phase of coagulation cascade, 2/ pathological events directly or indirectly involving the key components, 3/ their influence on the outcome of certain therapeutic interventions.
Prof. László Muszbek
Dr. Nicola J. Mutch
Manuscript Submission Information
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