FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2078132464> ?p ?o ?g. }

• W2078132464 endingPage "1904" @default.
• W2078132464 startingPage "1894" @default.
• W2078132464 abstract "SummaryFibrinogen molecules are comprised of two sets of disulfide‐bridged Aα‐, Bβ‐, and γ‐chains. Each molecule contains two outer D domains connected to a central E domain by a coiled‐coil segment. Fibrin is formed after thrombin cleavage of fibrinopeptide A (FPA) from fibrinogen Aα‐chains, thus initiating fibrin polymerization. Double‐stranded fibrils form through end‐to‐middle domain (D:E) associations, and concomitant lateral fibril associations and branching create a clot network. Fibrin assembly facilitates intermolecular antiparallel C‐terminal alignment of γ‐chain pairs, which are then covalently ‘cross‐linked’ by factor XIII (‘plasma protransglutaminase’) or XIIIa to form ‘γ‐dimers’. In addition to its primary role of providing scaffolding for the intravascular thrombus and also accounting for important clot viscoelastic properties, fibrin(ogen) participates in other biologic functions involving unique binding sites, some of which become exposed as a consequence of fibrin formation. This review provides details about fibrinogen and fibrin structure, and correlates this information with biological functions that include: (i) suppression of plasma factor XIII‐mediated cross‐linking activity in blood by binding the factor XIII A2B2 complex. (ii) Non‐substrate thrombin binding to fibrin, termed antithrombin I (AT‐I), which down‐regulates thrombin generation in clotting blood. (iii) Tissue‐type plasminogen activator (tPA)‐stimulated plasminogen activation by fibrin that results from formation of a ternary tPA‐plasminogen‐fibrin complex. Binding of inhibitors such as α2‐antiplasmin, plasminogen activator inhibitor‐2, lipoprotein(a), or histidine‐rich glycoprotein, impairs plasminogen activation. (iv) Enhanced interactions with the extracellular matrix by binding of fibronectin to fibrin(ogen). (v) Molecular and cellular interactions of fibrin β15–42. This sequence binds to heparin and mediates platelet and endothelial cell spreading, fibroblast proliferation, and capillary tube formation. Interactions between β15–42 and vascular endothelial (VE)‐cadherin, an endothelial cell receptor, also promote capillary tube formation and angiogenesis. These activities are enhanced by binding of growth factors like fibroblast growth factor‐2 (FGF‐2) and vascular endothelial growth factor (VEGF), and cytokines like interleukin (IL)‐1. (vi) Fibrinogen binding to the platelet αIIbβ3 receptor, which is important for incorporating platelets into a developing thrombus. (vii) Leukocyte binding to fibrin(ogen) via integrin αMβ2 (Mac‐1), which is a high affinity receptor on stimulated monocytes and neutrophils. Fibrinogen molecules are comprised of two sets of disulfide‐bridged Aα‐, Bβ‐, and γ‐chains. Each molecule contains two outer D domains connected to a central E domain by a coiled‐coil segment. Fibrin is formed after thrombin cleavage of fibrinopeptide A (FPA) from fibrinogen Aα‐chains, thus initiating fibrin polymerization. Double‐stranded fibrils form through end‐to‐middle domain (D:E) associations, and concomitant lateral fibril associations and branching create a clot network. Fibrin assembly facilitates intermolecular antiparallel C‐terminal alignment of γ‐chain pairs, which are then covalently ‘cross‐linked’ by factor XIII (‘plasma protransglutaminase’) or XIIIa to form ‘γ‐dimers’. In addition to its primary role of providing scaffolding for the intravascular thrombus and also accounting for important clot viscoelastic properties, fibrin(ogen) participates in other biologic functions involving unique binding sites, some of which become exposed as a consequence of fibrin formation. This review provides details about fibrinogen and fibrin structure, and correlates this information with biological functions that include: (i) suppression of plasma factor XIII‐mediated cross‐linking activity in blood by binding the factor XIII A2B2 complex. (ii) Non‐substrate thrombin binding to fibrin, termed antithrombin I (AT‐I), which down‐regulates thrombin generation in clotting blood. (iii) Tissue‐type plasminogen activator (tPA)‐stimulated plasminogen activation by fibrin that results from formation of a ternary tPA‐plasminogen‐fibrin complex. Binding of inhibitors such as α2‐antiplasmin, plasminogen activator inhibitor‐2, lipoprotein(a), or histidine‐rich glycoprotein, impairs plasminogen activation. (iv) Enhanced interactions with the extracellular matrix by binding of fibronectin to fibrin(ogen). (v) Molecular and cellular interactions of fibrin β15–42. This sequence binds to heparin and mediates platelet and endothelial cell spreading, fibroblast proliferation, and capillary tube formation. Interactions between β15–42 and vascular endothelial (VE)‐cadherin, an endothelial cell receptor, also promote capillary tube formation and angiogenesis. These activities are enhanced by binding of growth factors like fibroblast growth factor‐2 (FGF‐2) and vascular endothelial growth factor (VEGF), and cytokines like interleukin (IL)‐1. (vi) Fibrinogen binding to the platelet αIIbβ3 receptor, which is important for incorporating platelets into a developing thrombus. (vii) Leukocyte binding to fibrin(ogen) via integrin αMβ2 (Mac‐1), which is a high affinity receptor on stimulated monocytes and neutrophils." @default.
• W2078132464 created "2016-06-24" @default.
• W2078132464 creator A5073314507 @default.
• W2078132464 date "2005-08-01" @default.
• W2078132464 modified "2023-10-11" @default.
• W2078132464 title "Fibrinogen and fibrin structure and functions" @default.
• W2078132464 cites W1067939983 @default.
• W2078132464 cites W126825949 @default.
• W2078132464 cites W1483922672 @default.
• W2078132464 cites W1488989676 @default.
• W2078132464 cites W1499054077 @default.
• W2078132464 cites W1505283703 @default.
• W2078132464 cites W1507013396 @default.
• W2078132464 cites W1520458024 @default.
• W2078132464 cites W1529957677 @default.
• W2078132464 cites W1536945368 @default.
• W2078132464 cites W1546967816 @default.
• W2078132464 cites W1552506639 @default.
• W2078132464 cites W1556587647 @default.
• W2078132464 cites W1570621415 @default.
• W2078132464 cites W1580322940 @default.
• W2078132464 cites W1586370846 @default.
• W2078132464 cites W1586686759 @default.
• W2078132464 cites W1596065641 @default.
• W2078132464 cites W1603365810 @default.
• W2078132464 cites W1609872692 @default.
• W2078132464 cites W1617551935 @default.
• W2078132464 cites W1649140242 @default.
• W2078132464 cites W1853030675 @default.
• W2078132464 cites W1856146912 @default.
• W2078132464 cites W1861164204 @default.
• W2078132464 cites W1867300921 @default.
• W2078132464 cites W1907444416 @default.
• W2078132464 cites W1961340888 @default.
• W2078132464 cites W1965500868 @default.
• W2078132464 cites W1965888938 @default.
• W2078132464 cites W1966890284 @default.
• W2078132464 cites W1968056160 @default.
• W2078132464 cites W1968386409 @default.
• W2078132464 cites W1969632860 @default.
• W2078132464 cites W1971299102 @default.
• W2078132464 cites W1972282939 @default.
• W2078132464 cites W1974656135 @default.
• W2078132464 cites W1976385916 @default.
• W2078132464 cites W1977941390 @default.
• W2078132464 cites W1979335925 @default.
• W2078132464 cites W1980063169 @default.
• W2078132464 cites W1980364322 @default.
• W2078132464 cites W1981438065 @default.
• W2078132464 cites W1983821197 @default.
• W2078132464 cites W1984050935 @default.
• W2078132464 cites W1984237607 @default.
• W2078132464 cites W1987969307 @default.
• W2078132464 cites W1988873606 @default.
• W2078132464 cites W1989144240 @default.
• W2078132464 cites W1990922681 @default.
• W2078132464 cites W1991243300 @default.
• W2078132464 cites W1995054061 @default.
• W2078132464 cites W1996930129 @default.
• W2078132464 cites W1998939630 @default.
• W2078132464 cites W2003843472 @default.
• W2078132464 cites W2010459407 @default.
• W2078132464 cites W2011068964 @default.
• W2078132464 cites W2012569445 @default.
• W2078132464 cites W2014816029 @default.
• W2078132464 cites W2015332717 @default.
• W2078132464 cites W2015577105 @default.
• W2078132464 cites W2015863714 @default.
• W2078132464 cites W2016139654 @default.
• W2078132464 cites W2017990024 @default.
• W2078132464 cites W2018612827 @default.
• W2078132464 cites W2019014231 @default.
• W2078132464 cites W2019667037 @default.
• W2078132464 cites W2020450503 @default.
• W2078132464 cites W2021526142 @default.
• W2078132464 cites W2022315251 @default.
• W2078132464 cites W2022372977 @default.
• W2078132464 cites W2022405658 @default.
• W2078132464 cites W2022760394 @default.
• W2078132464 cites W2023580043 @default.
• W2078132464 cites W2025358191 @default.
• W2078132464 cites W2026348204 @default.
• W2078132464 cites W2026724199 @default.
• W2078132464 cites W2026974631 @default.
• W2078132464 cites W2027141031 @default.
• W2078132464 cites W2028047806 @default.
• W2078132464 cites W2028684039 @default.
• W2078132464 cites W2029380703 @default.
• W2078132464 cites W2029677015 @default.
• W2078132464 cites W2029682227 @default.
• W2078132464 cites W2029786429 @default.
• W2078132464 cites W2030377408 @default.
• W2078132464 cites W2031408965 @default.
• W2078132464 cites W2034811729 @default.
• W2078132464 cites W2037160988 @default.
• W2078132464 cites W2037383079 @default.
• W2078132464 cites W2037483881 @default.
• W2078132464 cites W2038850324 @default.

• next