
n.
An elastic, insoluble, whitish protein produced by the action of thrombin on fibrinogen and forming an interlacing fibrous network in the coagulation of blood.
fibrinous fi'brin·ous adj.
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American Heritage Dictionary:
fi·brin |

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Oxford Food & Nutrition Dictionary:
fibrin |
The blood protein formed from fibrinogen which is responsible for the clotting of blood.
Oxford Food & Fitness Dictionary:
fibrin |
A fibrous, insoluble protein formed during blood clotting. Molecules of fibrin form a network trapping cells and debris that seal off a damaged vessel. Unwanted fibrin formation can occur inside undamaged vessels, causing thromboses. One theory (the fibrin deposit theory) suggests that regular aerobic exercise reduces fibrin deposits in the blood, lowering the risk of thromboses and some other cardiovascular disorders.
A fibrous, insoluble protein formed during blood clotting. Molecules of fibrin form a network, trapping cells and debris, and sealing off damaged blood vessels.
Oxford Dictionary of Biochemistry:
fibrin |
| fibrillin, fibrillarin, fibril | |
| fibrin stabilizing factor, fibrinase, fibrinogen |
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Wikipedia on Answers.com:
Fibrin |
Fibrin (also called Factor Ia) is a fibrous, non-globular protein involved in the clotting of blood. It is a fibrillar protein that is polymerised to form a "mesh" that forms a hemostatic plug or clot (in conjunction with platelets) over a wound site.
Fibrin is involved in signal transduction, blood coagulation, platelet activation, and protein polymerization.
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Excessive generation of fibrin due to activation of the coagulation cascade leads to thrombosis, the block of a vessel by an agglutination of red blood cells, platelets, polymerized fibrin and other components. Ineffective generation or premature lysis of fibrin predisposes to 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 of both quantitative and qualitative in nature and include afibrinogenaemia, hypofibrinogenaemia, dysfibrinogenaemia, and hypodysfibrinogenaemia.
Consequences of reduced, absent, or dysfunctional fibrin is likely to render patients as hemophiliacs.
Fibrin from different animal sources is generally glycosylated with complex type diantennary asparagine linked glycans. Variety is just found in the degree of core fucosylation and in the type of sialic acid and galactose linkage.[1]
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+2 ion, alpha-D-mannose (C6H12O6), and D-glucosamine (C8H15NO6).
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