Fibrin - wikipedia Fibrin Micrograph showing fibrin ( dark pink amorphous material ) in a blocked vein surrounded by extravasated red blood cells ( right of image ). An artery ( left of image ) and the amnion ( far left of image ) is also seen. Placenta in a case of fetal thrombotic vasculopathy. H&E stain. Fibrin ( also called Factor Ia ) is a fibrous, non-globular protein involved in the clotting of blood. It is formed by the action of the protease thrombin on fibrinogen which causes it to polymerize. The polymerized fibrin together with platelets forms a hemostatic plug or clot over a wound site. When the lining of a blood vessel is broken, platelets are attracted forming a platelet plug. These platelets have thrombin receptors on their surfaces that bind serum thrombin molecules which in turn convert soluble fibrinogen in the serum into fibrin at the wound site. Fibrin forms long strands of tough insoluble protein that are bound to the platelets. Factor XIII completes the cross-linking of fibrin so that it hardens and contracts. The cross-linked fibrin forms a mesh atop the platelet plug that completes the clot. Contents 1 Role in disease 2 Physiology 3 Structure 4 See also 5 References 6 External links Role in disease From Fibrinogen to Fibrin with the help of Thrombin and Factor VIII. Excessive generation of fibrin due to activation of the coagulation cascade leads to thrombosis, the blockage of a vessel by an agglutination of red blood cells, platelets, polymerized fibrin and other components. Ineffective generation or premature lysis of fibrin increases the likelihood of a hemorrhage. Dysfunction or disease of the liver can lead to a decrease in the production of fibrin 's inactive precursor, fibrinogen, or to the production of abnormal fibrinogen molecules with reduced activity ( dysfibrinogenaemia ). Hereditary abnormalities of fibrinogen ( the gene is carried on chromosome 4 ) are both quantitative and qualitative in nature and include afibrinogenaemia, hypofibrinogenaemia, dysfibrinogenaemia, and hypodysfibrinogenaemia. Reduced, absent, or dysfunctional fibrin is likely to render patients as hemophiliacs. Physiology Cross-linking by thrombin and stabilization by activated factor XIII Fibrin from different animal sources is generally glycosylated with complex type biantennary asparagine linked glycans. Variety is found in the degree of core fucosylation and in the type of sialic acid and galactose linkage. Structure Crystal structure of the double - d fragment from human fibrin The image at the left is a crystal structure of the double - d fragment from human fibrin with two bound ligands. The experimental method used to obtain the image was X-ray diffraction, and it has a resolution of 2.30 Å. The structure is mainly made up of single alpha helices shown in red and beta sheets shown in yellow. The two blue structures are the bound ligands. The chemical structures of the ligands are Ca ion, alpha - D - mannose ( C H O ), and D - glucosamine ( C H NO ). See also D - dimer Fibrin glue Fibrin scaffold Fibrinolysis References Jump up ^ Kehrel BE ( 2003 ). `` ( Blood platelets : biochemistry and physiology ) ''. Hamostaseologie ( in German ). 23 ( 4 ) : 149 -- 58. doi : 10.1267 / Hamo03040149. PMID 14603379. Jump up ^ Pabst M, Bondili JS, Stadlmann J, Mach L, Altmann F ( July 2007 ). `` Mass + retention time = structure : a strategy for the analysis of N - glycans by carbon LC - ESI - MS and its application to fibrin N - glycans ''. Anal. Chem. 79 ( 13 ) : 5051 -- 7. doi : 10.1021 / ac070363i. PMID 17539604. External links TGW1916.net, Defibrinated blood harvested from sheep ( video ) Fibrin : Molecule of the Month, by David Goodsell, RCSB Protein Data Bank Proteins involved in coagulation Coagulation factors Primary hemostasis vWF platelet membrane glycoproteins : Ib ( A IX ) IIb / IIIa ( IIb IIIa ) VI Intrinsic pathway HMWK / Bradykinin Prekallikrein / Kallikrein XII `` Hageman '' XI IX VIII Extrinsic pathway III `` Tissue factor '' VII Common pathway X V II `` ( Pro ) thrombin '' I `` Fibrin '' Fibrinogen ( FGA, FGG ) XIII Coagulation inhibitors Antithrombin ( inhibits II, IX, X, XI, XII ) Protein C ( inhibits V, VIII ) / Protein S ( cofactor for protein C ) Protein Z ( inhibits X ) ZPI ( inhibits X, XI ) TFPI ( inhibits III ) Thrombolysis / fibrinolysis Plasmin tPA / urokinase PAI - 1 / 2 α2 - AP α2 - macroglobulin TAFI Acute - phase proteins Amyloid SAP SAA Other positive Alpha 1 - antichymotrypsin Alpha 1 - antitrypsin Alpha 2 - macroglobulin C - reactive protein Ceruloplasmin C3 Ferritin Fibrin Haptoglobin Hemopexin Orosomucoid Negative Serum albumin Transferrin NDL : 00570673 Retrieved from `` https://en.wikipedia.org/w/index.php?title=Fibrin&oldid=801882650 '' Categories : Coagulation system Blood proteins Acute phase proteins Hidden categories : CS1 German - language sources ( de ) Talk Contents About Wikipedia Български Català Čeština Dansk Deutsch Español Euskara فارسی Français Galego Հայերեն Ido Bahasa Indonesia Italiano עברית Қазақша Lietuvių Magyar മലയാളം Nederlands 日本 語 Oromoo Plattdüütsch Polski Português Русский Slovenščina کوردی Basa Sunda Suomi Svenska Українська 中文 25 more Edit links This page was last edited on 22 September 2017, at 14 : 31. 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Question: the factor that is responsible for stabilizing a soluble firbrin monomer into an insoluble clot is
Answer: Factor XIII