フィブリン
WordNet
- a white insoluble fibrous protein formed by the action of thrombin on fibrinogen when blood clots; it forms a network that traps red cells and platelets
- in the clotting of blood thrombin catalyzes factor XIII into its active form (fibrinase) which causes fibrin to form a stable clot (同)factor_XIII
- a rare congenital disorder of blood coagulation in which no fibrinogen is found in the blood plasma
- remove fibrin from (blood)
PrepTutorEJDIC
- (凝固血液中の)線維素,フィブリン
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/03/08 11:36:55」(JST)
[Wiki en表示]
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[1] 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
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.[2]
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+2 ion, alpha-D-mannose (C6H12O6), and D-glucosamine (C8H15NO6).
See also
- D-dimer
- Fibrin glue
- Fibrin scaffold
References
- ^ Kehrel BE (2003). "[Blood platelets: biochemistry and physiology]". Hamostaseologie (in German) 23 (4): 149–58. doi:10.1267/Hamo03040149. PMID 14603379.
- ^ 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
- B
- IX)
- IIb/IIIa (IIb
- IIIa)
- VI
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|
Intrinsic pathway |
- HMWK/Bradykinin
- Prekallikrein/Kallikrein
- XII "Hageman"
- XI
- IX
- VIII
|
|
Extrinsic pathway |
|
|
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 |
|
|
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
|
|
UpToDate Contents
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English Journal
- Differential regulation of macrophage inflammatory activation by fibrin and fibrinogen.
- Hsieh JY1, Smith TD1, Meli VS1, Tran TN1, Botvinick EL1, Liu WF2.
- Acta biomaterialia.Acta Biomater.2017 Jan 1;47:14-24. doi: 10.1016/j.actbio.2016.09.024. Epub 2016 Sep 20.
- Fibrin is a major component of the provisional extracellular matrix formed during tissue repair following injury, and enables cell infiltration and anchoring at the wound site. Macrophages are dynamic regulators of this process, advancing and resolving inflammation in response to cues in their micro
- PMID 27662809
- Fibrin structural and diffusional analysis suggests that fibers are permeable to solute transport.
- Leonidakis KA1, Bhattacharya P2, Patterson J3, Vos BE4, Koenderink GH4, Vermant J5, Lambrechts D6, Roeffaers M7, Van Oosterwyck H8.
- Acta biomaterialia.Acta Biomater.2017 Jan 1;47:25-39. doi: 10.1016/j.actbio.2016.09.044. Epub 2016 Oct 4.
- Fibrin hydrogels are promising carrier materials in tissue engineering. They are biocompatible and easy to prepare, they can bind growth factors and they can be prepared from a patient's own blood. While fibrin structure and mechanics have been extensively studied, not much is known about the relati
- PMID 27717911
- Click chemistry improved wet adhesion strength of mussel-inspired citrate-based antimicrobial bioadhesives.
- Guo J1, Kim GB1, Shan D1, Kim JP1, Hu J2, Wang W3, Hamad FG4, Qian G3, Rizk EB5, Yang J6.
- Biomaterials.Biomaterials.2017 Jan;112:275-286. doi: 10.1016/j.biomaterials.2016.10.010. Epub 2016 Oct 12.
- For the first time, a convenient copper-catalyzed azide-alkyne cycloaddition (CuAAC, click chemistry) was successfully introduced into injectable citrate-based mussel-inspired bioadhesives (iCMBAs, iCs) to improve both cohesive and wet adhesive strengths and elongate the degradation time, providing
- PMID 27770631
- Computational model of mesenchymal migration in 3D under chemotaxis.
- Ribeiro FO1,2, Gómez-Benito MJ2, Folgado J1, Fernandes PR1, García-Aznar JM2.
- Computer methods in biomechanics and biomedical engineering.Comput Methods Biomech Biomed Engin.2017 Jan;20(1):59-74. Epub 2016 Jun 23.
- Cell chemotaxis is an important characteristic of cellular migration, which takes part in crucial aspects of life and development. In this work, we propose a novel in silico model of mesenchymal 3D migration with competing protrusions under a chemotactic gradient. Based on recent experimental observ
- PMID 27336322
Japanese Journal
- 症例報告 有瘻性膿胸に対してEWSを用いた気管支充填術と瘻孔内フィブリン糊注入の併用が有効であった1例
- D-dimerと可溶性フィブリンモノマー複合体の組合せによる腰椎疾患の周術期における静脈血栓塞栓症の検索方法 (日本脊椎・脊髄神経手術手技学会特集号)
- Journal of spine research : official journal of the Japanese Society for Spine Surgery and Related Research 7(7), 1145-1149, 2016-07
- NAID 40020922950
- 術後髄液漏を防ぐための筋膜・皮下組織縫合の工夫 : フィブリン糊製剤を使用しないで (日本脊椎・脊髄神経手術手技学会特集号)
- Journal of spine research : official journal of the Japanese Society for Spine Surgery and Related Research 7(7), 1105-1109, 2016-07
- NAID 40020922821
- 臨床経験 肺血栓塞栓症・深部静脈血栓症急性期におけるフィブリン関連マーカー
Related Links
- 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 the later to polymerize. The polymerized fibrin together with platelets ...
- In a few places only was the peritoneal surface coated with fibrin, and the intestines were mostly free from adhesions. ... (fī'brĭn) A fibrous protein produced by the action of thrombin on fibrinogen and essential to the coagulation of ...
- fibrin [fi´brin] an insoluble protein that is essential to clotting of blood, formed from fibrinogen by action of thrombin. fi·brin (fī'brin), An elastic filamentous protein derived from fibrinogen by the action of thrombin, which releases ...
Related Pictures
★リンクテーブル★
[★]
- 英
- fibrin, Fbn
- 同
- 線維素
- 関
- フィブリノゲン、血液凝固因子
- トロンビンの作用によりフィブリノゲンより生成したフィブリンモノマーは、重合してフィブリンポリマーとなる (SP.507)
- フィブリンポリマーは第XIIIa因子(第XIII因子の活性型)の作用により架橋結合を生じて安定なフィブリンを生じる (SP.507)
[★]
- 英
- fibrillin ← フィブリン fibrin と勘違いするな
- 関
- ミクロフィブリル 細線維、弾性線維
臨床関連
-fibrillin
[★]
[★]
異常フィブリノゲン血症