Fibrinogen and fibrin structure and functions

MOSESSON, M.W.

doi:10.1111/j.1538-7836.2005.01365.x

Cited by 1,695Blood properties and coagulationBlood Coagulation and Thrombosis MechanismsTrauma, Hemostasis, Coagulopathy, Resuscitation

Fibrinogen and fibrin structure and functions

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MOSESSON, M.W.·2005·Journal of Thrombosis and Haemostasis

DOI 10.1111/j.1538-7836.2005.01365.x

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Abstract

Fibrinogen molecules are comprised of two sets of disulfide-bridged Aalpha-, Bbeta-, and gamma-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 Aalpha-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 gamma-chain pairs, which are then covalently 'cross-linked' by factor XIII ('plasma protransglutaminase') or XIIIa to form 'gamma-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 alpha2-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 beta15-42. This sequence binds to heparin and mediates platelet and endothelial cell spreading, fibroblast proliferation, and capillary tube formation. Interactions between beta15-42 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 alpha(IIb)beta3 receptor, which is important for incorporating platelets into a developing thrombus. (vii) Leukocyte binding to fibrin(ogen) via integrin alpha(M)beta2 (Mac-1), which is a high affinity receptor on stimulated monocytes and neutrophils.

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E-M19 harbors acute phase reactants (A2M, CP), immunoglobulins (IGHG1, IGHA1), and blood fibrinogens involved in coagulation.
“Another protein-based module that shows weak overlap in the RNA networks in brain is E-M19, which harbors several acute phase reactants (e.g. A2M and CP), immunoglobulins (IGHG1 and IGHA1) as well as blood fibrinogens involved in coagulation (Mosesson, 2005).”
From A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer’s Disease (2017) · cites this paper as Mosesson, 2005

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Characterization of fibrinogen New York 1. A dysfunctional fibrinogen with a deletion of B beta(9-72) corresponding exactly to exon 2 of the gene.
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Evidence That Both Exosites on Thrombin Participate in Its High Affinity Interaction with Fibrin
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Monocyte Plasminogen Activator Inhibitor 2 (PAI-2) Inhibits u-PA-mediated Fibrin Clot Lysis and Is Cross-linked to Fibrin
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FIBRINOPEPTIDE B IN FIBRIN ASSEMBLY AND METABOLISM: PHYSIOLOGIC SIGNIFICANCE IN DELAYED RELEASE OF THE PEPTIDE*
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Thrombin cleavage enhances exposure of a heparin binding domain in the N-terminus of the fibrin beta chain
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The Covalent Structure of Factor XIIIa Crosslinked Fibrinogen Fibrils
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Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction
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Interaction of Fibrin(ogen) with the Endothelial Cell Receptor VE-Cadherin: Mapping of the Receptor-Binding Site in the NH2-Terminal Portions of the Fibrin β Chains
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Cross-linking of Plasminogen Activator Inhibitor 2 and α2-Antiplasmin to Fibrin(ogen)
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Interaction of Fibrin with VE‐Cadherin
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Studies on the ultrastructure of fibrin lacking fibrinopeptide B (beta- fibrin)
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The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (gamma 275 Arg-->Cys).
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Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by factor XIIIa and tissue transglutaminase. Identification of a rapid mode of hybrid alpha-/gamma-chain cross-linking that is promoted by the gamma-chain cross-linking.
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The sequence A alpha-(148-160) in fibrin, but not in fibrinogen, is accessible to monoclonal antibodies.
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Sequence γ377−395(P2), but Not γ190−202(P1), Is the Binding Site for the αMI-Domain of Integrin αMβ2 in the γC-Domain of Fibrinogen
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Interleukin-1β but not IL-1α binds to fibrinogen and fibrin and has enhanced activity in the bound form
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Human Thrombi Contain an Abundance of Active Thrombin
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BIOCHEMICAL AND CHROMATOGRAPHIC STUDIES OF CERTAIN ACTIVITIES ASSOCIATED WITH HUMAN FIBRINOGEN PREPARATIONS*
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Multiple Binding with Identical Linkage: A Mechanism That Explains the Effect of Lipoprotein(a) on Fibrinolysis
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The sequence gamma-(312-324) is a fibrin-specific epitope
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Cleavage of fibrin-derived D-dimer into monomers by endopeptidase from puff adder venom (Bitis arietans) acting at cross-linked sites of the .gamma.-chain. Sequence of carboxy-terminal cyanogen bromide .gamma.-chain fragments
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Multiple Protein Interactions as Exhibited by the Blood-clotting Mechanism.
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Multiple Pulmonary Emboli in a Patient with Afibrinogenaemia
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Factor XIIIa Cross-links Lipoprotein(a) With Fibrinogen and Is Present in Human Atherosclerotic Lesions
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Spreading of platelets on fibrin is mediated by the amino terminus of the beta chain including peptide beta 15-42
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Structure and Rheology of Fibrin Networks
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Fibroblasts Spread on Immobilized Fibrin Monomer by Mobilizing a β1-class Integrin, Together with a Vitronectin Receptor αvβ3 on Their Surface
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The fibrin cross‐linking debate: cross‐linked γ‐chains in fibrin fibrils bridge ‘transversely’ between strands: yes
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FIBRINOGEN HETEROGENEITY*
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Evaluation of the Factors Contributing to Fibrin–dependent Plasminogen Activation
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Biological and synthetic polymer networks
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Evidence for Intramolecular Cross-Linked Aα·γ Chain Heterodimers in Plasma Fibrinogen
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Binding of tissue‐type plasminogen activator to fibrinogen fragments
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Fibrinogen Naples I (Bβ A68T) Nonsubstrate Thrombin-Binding Capacities
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Congenital afibrinogenemia. Vascular changes and multiple thromboses induced by fibrinogen infusions and contraceptive medication.
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Cross‐linked γ‐chains in fibrin fibrils bridge transversely between strands: no
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A synthetic analog of fibrinogen alpha 27-50 is an inhibitor of thrombin.
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Contact with the N Termini in the Central E Domain Enhances the Reactivities of the Distal D Domains of Fibrin to Factor XIIIa
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A Synthetic Analog of Fibrinogen α27–50 Is an Inhibitor of Thrombin
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Hypofibrinogenaemia and Massive Thrombosis
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Cross‐linked γ‐chains in a fibrin fibril are situated transversely between its strands
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Authors: MOSESSON, M. W.
Corresponding author: MOSESSON, M.W.
Venue: Journal of Thrombosis and Haemostasis
Publisher: Elsevier BV
Published: 2005-08
Volume: 3
Issue: 8
Pages: 1894-1904
ISSN: 1538-7836 (ISSN-L)
DOI: 10.1111/j.1538-7836.2005.01365.x
OpenAlex: W2078132464
Cited by: 1,695
References: 187
Citations by year: 2026: 58 · 2025: 64 · 2024: 96 · 2023: 92 · 2022: 97 · 2021: 131 · 2020: 113 · 2019: 105 · 2018: 86 · 2017: 89 · 2016: 96 · 2015: 105 · 2014: 96 · 2013: 72 · 2012: 74
FWCI: 7.87
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6342 d)
Locations: Journal of Thrombosis and Haemostasis (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Heart, Lung, and Blood Institute (R01HL070627, R01-HL70627)
Topics: Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Blood properties and coagulation
Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
Health Sciences › Medicine › Critical Care and Intensive Care Medicine › Trauma, Hemostasis, Coagulopathy, Resuscitation
Keywords: fibrinogen, fibrin structure, fibrin polymerization, plasminogen activation, tissue plasminogen activator, heparin binding, fibronectin binding, angiogenesis, endothelial cell spreading
MeSH terms: Amino Acid Sequence, Animals, Cross-Linking Reagents, Factor XIII, Fibrin, Fibrinogen, Fibrinolysis, Growth Substances, Humans, Leukocytes, Models, Biological, Models, Molecular, Molecular Sequence Data, Protein Conformation, Time Factors, Cytokines, Endothelial Cells

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Fibrinogen and fibrin structure and functions

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