Comprehensive Physiology Wiley Online Library

Blood Coagulation and Fibrinolysis

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Congenital Deficiencies in Initiation of Blood Coagulation
1.1 Factor XII
1.2 Plasma Prekallikrein
1.3 Plasma Kininogens
1.4 Interaction of Contact‐System Proteins
1.5 Factor XI
1.6 Factor IX
1.7 Factor VIII
2 Relationship of Intrinsic and Extrinsic Blood Coagulation
2.1 Factor X
2.2 Factor VII
2.3 Thromboplastin
3 Regulation of Prothrombin Activation
3.1 Prothrombin
3.2 Factor V
3.3 Coagulant Phospholipid Surfaces
3.4 Calcium Ions
3.5 Thrombin Formation
3.6 Thrombin Specificity
3.7 Regulation of Thrombin Activity
3.8 Heparin and Antithrombin III
3.9 Interaction of Thrombin With Fibrin
3.10 Nonmammalian Inhibitors of Thrombin
3.11 Thrombinlike Enzymes in Snake Venoms
4 Electron Microscopy of Fibrinogen
5 Fibrinogen Structure
5.1 Model of Fibrinogen Molecule
5.2 Conversion of Fibrinogen to Fibrin Clot
5.3 Polymerization Sites
5.4 Cross‐Linking of Fibrin
6 Interaction of Fibrinogen with Plasma Proteins
7 Interaction of Fibrinogen with Cells
8 Degradation by Proteases other than Plasmin
9 Degradation of Fibrinogen and Fibrin by Plasmin
9.1 Role of Fibrin in Clot Formation and Lysis
10 Plasminogen and Plasmin
10.1 Plasminogen Activators
10.2 Inhibitors of Plasminogen and Plasmin
10.3 Physiological Fibrinolysis
Figure 1. Figure 1.

Stick models of zymogens involved in coagulation, kinin formation, and fibrinolysis. Dark bars, polypeptide chain containing the active‐site serine. Dotted lines, 1 or more disulfide bridges. Numbers, zymogen domains, in most cases defined by sites of proteolytic cleavage. Bar size is roughly proportional to molecular weight. Dark triangles, location of active serine residue. Domain 1 of prothrombin, factor VII, IX, and X contains the Gla residues responsible for Ca2+ binding and thus phospholipid attachment. Domain 1 in factor XI, XII, and prekallikrein represents the heavy chain, probably the site of attachment to negatively charged surfaces. Domain 1 in plasminogen represents the peptide cleaved by plasmin to convert Glu‐plasminogen to Lys‐plasminogen. Domain 3 of prothrombin is the factor V‐binding site and is cleaved from domain 2 by thrombin. In factors IX and X, bonds between domain 2 and 3 are cleaved during zymogen activation. In prothrombin, cleavage between dark and light halves of the molecule by factor Xa is not sufficient to form thrombin but does remove prothrombin from its phospholipid attachment. Cleavage between domain 4 and 5 to form 2‐chain thrombin forms the active enzyme. In all other cases zymogen conversion to enzyme occurs by cleavage between dark and light portions to form 2 polypeptide chains connected by disulfide bridges. Only factor XI exists as a dimer; thus factor XIa has 2 identical active sites.

From Jackson and Nemerson . Reproduced with permission from the Annual Review of Biochemistry, vol. 49, © 1980 by Annual Reviews Inc
Figure 2. Figure 2.

Contact activation of factor XII, XI, and prekallikrein (PK). A: factor XII from the blood fluid phase binds directly to a foreign negatively charged surface. Factor XI‐high‐molecular‐weight kininogen (HMWK) complex and prekallikrein‐HMWK complex each bind to the surface via HMWK. B: factor XII is converted to active enzyme factor XIIa by autoactivation and/or a conformational change. Factor XIIa then enzymatically catalyzes conversion of its substrates factor XI and prekallikrein to active enzymes. C: active enzymes XIa and kallikrein (K) remain attached to HMWK and to surface. About half of the kallikrein molecules dissociate and may attack factor XIIa to yield factor XII fragments, which dissociate from the surface. Kallikrein may also attack factor XII zymogen to cleave it to an active enzyme during a positive feedback reaction.

Figure 3. Figure 3.

In the presence of a surface (e.g., kaolin), factor XII and prekallikrein are activated in the presence of contact phase and of cofactor high‐molecular‐weight (HMW) kininogen, respectively. Factor XIIa converts factor XI to factor XIa, a reaction that also requires HMW kininogen. Factor XIa activates factor IX to IXa. Factor IXa cleaves factor X to factor Xa in the presence of cofactors factor VIII, phospholipid, and Ca2+. Similarly, factor Xa hydrolyzes factor II (prothrombin) to thrombin in the presence of cofactors factor V, phospholipid, and Ca2+. Thrombin then attacks fibrinogen to form the fibrin clot.

From Handin and Rosenberg , © 1981 by MIT Press
Figure 4. Figure 4.

Extrinsic coagulation. Factor VII is converted to factor VIIa by autoactivation, factor XIIa, or in a feedback reaction by factor Xa. Factor VIIa in presence of tissue factor and Ca2+ can convert factor X to factor Xa. Once factor Xa is formed, pathway is identical to intrinsic coagulation (see Fig. ).

From Rosenberg , © 1981 by MIT Press
Figure 5. Figure 5.

Prothrombin activation. Prothrombin is activated to thrombin initially by right‐hand pathway. The NH2‐terminal (N‐terminal) “pro” piece containing fragment 1 (F1) and fragment 2 (F2) is cleaved by factor Xa. Prothrombin 2 (Pr2 intermediate) results, which in turn is cleaved by factor Xa at an Ile‐Arg bond to yield a serine active center on the larger polypeptide chain (β‐chain) and a small α‐chain still attached by a disulfide bridge. Left‐hand pathway may operate in the test tube once thrombin is formed with cleavage between fragment 1 and fragment 2 preceding final cleavage between fragment 2 and Pr2 intermediate, but only the right‐hand pathway occurs at in vivo Ca2+ concentration.

Figure 6. Figure 6.

Formation of receptor on platelets and phospholipids by attachment of factor Va required to bind factor Xa. Factor V is converted by thrombin (factor Ha) to factor Va. Factor Va in the presence of Ca2+ binds to phospholipid micelle or platelet membrane. Prothrombin (factor II) binds to phospholipid through Ca2+ attached to the fragment 1 domain containing Gla residues. Factor Xa is formed from factor X via either the intrinsic pathway (factor IXa) or the extrinsic pathway (factor VIIa). Factor Xa then binds to factor Va and phospholipid markedly accelerates its ability to cleave factor II to Ha.

Figure 7. Figure 7.

Mechanism of thrombin inhibition by heparin‐antithrombin III. Antithrombin III (antithrombin on figure), the major inhibitor of thrombin in plasma, serves as substrate for thrombin. 1) Active site of thrombin containing reactive serine attacks a peptide bond adjacent to an arginine residue in antithrombin III. Covalent ester bond forms to stabilize the complex. 2) Heparin can markedly accelerate this reaction by combining with antithrombin III at lysine‐binding sites and inducing a conformational change on the inhibitor. 3) Heparin dissociates after combination of thrombin with antithrombin III. 4) Heparin can then accelerate the combination of a 2nd molecule of antithrombin III with thrombin, thus acting in a catalytic fashion.

From Rosenberg , © 1981 by MIT Press
Figure 8. Figure 8.

Electron micrographs of fibrinogen and fibrin oligomers. A: shadow‐casting pattern of fibrinogen demonstrating appearance of trinodular molecules. Technique did not permit visualization of connections between central and outer nodules. × 215,000. B: specimen stained negatively with uranyl acetate confirms elongated trinodular shape of fibrinogen molecules. Flexibility of molecules and thickness of connector that links nodules are apparent, × 194,000. C: fibrin oligomer, a protofibril, stained negatively. Interpretive drawing indicates half‐staggered overlap of fibrin monomers, which form 2 parallel strands. Staggered association is basis of a 22.5‐nm periodicity of fibrin fibers. Arrows, end‐to‐end junctions of outer nodules in adjacent fibrin monomers. × 194,000.

A from Hall and Slayter ; B from Williams ; C from Hantgan et al.
Figure 9. Figure 9.

Model of fibrinogen molecule. Dimeric structure of molecule with probable rotational symmetry. Overall length, ˜45 nm; diameter of outer nodules, 6.5 nm; connector length, 15 nm; Mr = 340,000. Two pairs of 3 polypeptide chains; thrombin cleaves fibrinopeptides A and B (FPA and FPB, thickened segments) from NH2 terminals of Aα‐ and Bβ‐chains, respectively; γ‐chain is not affected by thrombin. Four oligosaccharides (CHO), each Mr ˜ 2,500, are attached to the Bβ‐ and γ‐chains, endowing fibrinogen as a glycoprotein. There are 29 disulfide bonds (SS), 3 of which link 2 halves of the fibrinogen molecule: 1 bond is between Aα‐chains and 2 bonds between γ‐chains. Sites available for factor XIIIa‐catalyzed cross‐linking between lysine donors (XL, arrow pointing upward) and glutamine acceptors (XL, arrow pointing downward) are located in COOH terminals of Aα‐ and γ‐chains. COOH terminals of Bβ‐ and γ‐chains and adjacent part of connector are cleaved by plasmin as fragment D; corresponding portion of fibrinogen molecule is depicted by electron microscopy as outer nodule and defined as the structural D domain. NH2 terminals of all 3 chains and adjacent part of connector are removed by plasmin as fragment E; this region is demonstrated on electron micrographs of fibrinogen as the central nodule and is called E domain. COOH terminals of Aα‐chains (polar appendages) are loosely structured and possibly fill the space around connector.

Figure 10. Figure 10.

Formation of fibrin. Driving force for assembly of fibrin network originates from specific association of complementary binding sites. One polymerization site (a) is present on fibrinogen molecule D domain. Complementary sites (A) are activated by thrombin in fibrin E domain. Due to a probable rotational symmetry, right half of fibrin molecule is a mirror reflection of left half. Binding between a and A sites on 2 fibrin monomer molecules forms 2 links that hold molecules in a half‐staggered orientation. Extension of this process leads to end‐to‐end polymerization and generation of protofibrils. A new polymerization site (bb) appears on fibrin oligomer, probably because of alignment of 2 D domains; this site is apparently absent in fibrin monomer or dimer. A complementary site (B) is present in E domain of fibrin. Binding of a and A sites may propagate formation of linear fibrin protofibrils, whereas binding of bb with 2 B sites may be responsible for side‐to‐side coalescence of protofibrils.

Figure 11. Figure 11.

Degradation of fibrinogen by plasmin. Initial proteolytic attack removes the COOH terminal of Aα‐chain as fragment P45 and its degradation product fragment A. Fragment X is a group of derivatives, the less degraded of which are coagulable by thrombin. Fragments X and Y are cleaved asymmetrically to form terminal degradation products, fragments D and E. From 1 fibrinogen molecule 2 molecules of fragment D and 1 of fragment E are formed.

Figure 12. Figure 12.

Degradation of cross‐linked fibrin by plasmin. Initial enzyme action cleaves cross‐linked α‐chain COOH‐terminal fragments as a mixture of derivatives. Next exposed connectors are disrupted and a (DD)E complex liberated. Components of the complex are derived from 3 different fibrin monomer molecules and 2 fragments D are kept together by covalent cross‐link bonds. Fragment E in the complex still has A and B polymerization sites; however, after long proteolysis with plasmin the sites are damaged and the complex falls apart.

Figure 13. Figure 13.

Plasminogen activation. Human plasminogen, a single polypeptide chain protein, contains 790 amino acid residues, NH2‐terminal glutamic acid, 5 homologous loop structures (“krinkles”), and 24 disulfide bonds. On action of plasmin on Glu‐plasminogen a cleavage at Lys76‐Lys77 occurs, releasing NH2‐terminal peptide and yielding Lys‐plasminogen. Cleavage of the Arg560‐Val561 bond by activators results in formation of Lys‐plasmin, composed of 2 chains (A and B) linked by 2 disulfide bonds. Lys‐plasminogen activation seems approximately 10 times faster than that of Gluplasminogen. In presence of plasmin inhibitors the cleavage of NH2‐terminal peptide is significantly decreased and Glu‐plasmin (potentially convertible into Lys‐plasmin) is formed.

Figure 14. Figure 14.

Physiological fibrinolysis. During physiological dynamic equilibrium, histidine‐rich glycoprotein and other antiactivators regulate interaction of plasminogen in blood with plasminogen activators. Even if minute amounts of plasmin are generated (e.g., after release of vascular plasminogen activator following stress) the enzyme is promptly inactivated by α2‐antiplasmin. On activation of the blood coagulation system, fibrin clot is formed, which not only strongly binds vascular plasminogen activator and plasminogen from blood but also significantly accelerates the activation rate. Resulting plasmin is protected from inhibitors while attached to fibrin. Enzyme is inactivated by α2‐antiplasmin and α2‐macroglobulin after proteolytic dissolution of fibrin and liberation into the liquid phase of blood. Thus the fibrin network catalyzes initiation and regulation of fibrinolysis. Kallikrein and factor XIa can activate plasminogen in the liquid phase, but their role appears less significant and not specifically associated with fibrin clot.



Figure 1.

Stick models of zymogens involved in coagulation, kinin formation, and fibrinolysis. Dark bars, polypeptide chain containing the active‐site serine. Dotted lines, 1 or more disulfide bridges. Numbers, zymogen domains, in most cases defined by sites of proteolytic cleavage. Bar size is roughly proportional to molecular weight. Dark triangles, location of active serine residue. Domain 1 of prothrombin, factor VII, IX, and X contains the Gla residues responsible for Ca2+ binding and thus phospholipid attachment. Domain 1 in factor XI, XII, and prekallikrein represents the heavy chain, probably the site of attachment to negatively charged surfaces. Domain 1 in plasminogen represents the peptide cleaved by plasmin to convert Glu‐plasminogen to Lys‐plasminogen. Domain 3 of prothrombin is the factor V‐binding site and is cleaved from domain 2 by thrombin. In factors IX and X, bonds between domain 2 and 3 are cleaved during zymogen activation. In prothrombin, cleavage between dark and light halves of the molecule by factor Xa is not sufficient to form thrombin but does remove prothrombin from its phospholipid attachment. Cleavage between domain 4 and 5 to form 2‐chain thrombin forms the active enzyme. In all other cases zymogen conversion to enzyme occurs by cleavage between dark and light portions to form 2 polypeptide chains connected by disulfide bridges. Only factor XI exists as a dimer; thus factor XIa has 2 identical active sites.

From Jackson and Nemerson . Reproduced with permission from the Annual Review of Biochemistry, vol. 49, © 1980 by Annual Reviews Inc


Figure 2.

Contact activation of factor XII, XI, and prekallikrein (PK). A: factor XII from the blood fluid phase binds directly to a foreign negatively charged surface. Factor XI‐high‐molecular‐weight kininogen (HMWK) complex and prekallikrein‐HMWK complex each bind to the surface via HMWK. B: factor XII is converted to active enzyme factor XIIa by autoactivation and/or a conformational change. Factor XIIa then enzymatically catalyzes conversion of its substrates factor XI and prekallikrein to active enzymes. C: active enzymes XIa and kallikrein (K) remain attached to HMWK and to surface. About half of the kallikrein molecules dissociate and may attack factor XIIa to yield factor XII fragments, which dissociate from the surface. Kallikrein may also attack factor XII zymogen to cleave it to an active enzyme during a positive feedback reaction.



Figure 3.

In the presence of a surface (e.g., kaolin), factor XII and prekallikrein are activated in the presence of contact phase and of cofactor high‐molecular‐weight (HMW) kininogen, respectively. Factor XIIa converts factor XI to factor XIa, a reaction that also requires HMW kininogen. Factor XIa activates factor IX to IXa. Factor IXa cleaves factor X to factor Xa in the presence of cofactors factor VIII, phospholipid, and Ca2+. Similarly, factor Xa hydrolyzes factor II (prothrombin) to thrombin in the presence of cofactors factor V, phospholipid, and Ca2+. Thrombin then attacks fibrinogen to form the fibrin clot.

From Handin and Rosenberg , © 1981 by MIT Press


Figure 4.

Extrinsic coagulation. Factor VII is converted to factor VIIa by autoactivation, factor XIIa, or in a feedback reaction by factor Xa. Factor VIIa in presence of tissue factor and Ca2+ can convert factor X to factor Xa. Once factor Xa is formed, pathway is identical to intrinsic coagulation (see Fig. ).

From Rosenberg , © 1981 by MIT Press


Figure 5.

Prothrombin activation. Prothrombin is activated to thrombin initially by right‐hand pathway. The NH2‐terminal (N‐terminal) “pro” piece containing fragment 1 (F1) and fragment 2 (F2) is cleaved by factor Xa. Prothrombin 2 (Pr2 intermediate) results, which in turn is cleaved by factor Xa at an Ile‐Arg bond to yield a serine active center on the larger polypeptide chain (β‐chain) and a small α‐chain still attached by a disulfide bridge. Left‐hand pathway may operate in the test tube once thrombin is formed with cleavage between fragment 1 and fragment 2 preceding final cleavage between fragment 2 and Pr2 intermediate, but only the right‐hand pathway occurs at in vivo Ca2+ concentration.



Figure 6.

Formation of receptor on platelets and phospholipids by attachment of factor Va required to bind factor Xa. Factor V is converted by thrombin (factor Ha) to factor Va. Factor Va in the presence of Ca2+ binds to phospholipid micelle or platelet membrane. Prothrombin (factor II) binds to phospholipid through Ca2+ attached to the fragment 1 domain containing Gla residues. Factor Xa is formed from factor X via either the intrinsic pathway (factor IXa) or the extrinsic pathway (factor VIIa). Factor Xa then binds to factor Va and phospholipid markedly accelerates its ability to cleave factor II to Ha.



Figure 7.

Mechanism of thrombin inhibition by heparin‐antithrombin III. Antithrombin III (antithrombin on figure), the major inhibitor of thrombin in plasma, serves as substrate for thrombin. 1) Active site of thrombin containing reactive serine attacks a peptide bond adjacent to an arginine residue in antithrombin III. Covalent ester bond forms to stabilize the complex. 2) Heparin can markedly accelerate this reaction by combining with antithrombin III at lysine‐binding sites and inducing a conformational change on the inhibitor. 3) Heparin dissociates after combination of thrombin with antithrombin III. 4) Heparin can then accelerate the combination of a 2nd molecule of antithrombin III with thrombin, thus acting in a catalytic fashion.

From Rosenberg , © 1981 by MIT Press


Figure 8.

Electron micrographs of fibrinogen and fibrin oligomers. A: shadow‐casting pattern of fibrinogen demonstrating appearance of trinodular molecules. Technique did not permit visualization of connections between central and outer nodules. × 215,000. B: specimen stained negatively with uranyl acetate confirms elongated trinodular shape of fibrinogen molecules. Flexibility of molecules and thickness of connector that links nodules are apparent, × 194,000. C: fibrin oligomer, a protofibril, stained negatively. Interpretive drawing indicates half‐staggered overlap of fibrin monomers, which form 2 parallel strands. Staggered association is basis of a 22.5‐nm periodicity of fibrin fibers. Arrows, end‐to‐end junctions of outer nodules in adjacent fibrin monomers. × 194,000.

A from Hall and Slayter ; B from Williams ; C from Hantgan et al.


Figure 9.

Model of fibrinogen molecule. Dimeric structure of molecule with probable rotational symmetry. Overall length, ˜45 nm; diameter of outer nodules, 6.5 nm; connector length, 15 nm; Mr = 340,000. Two pairs of 3 polypeptide chains; thrombin cleaves fibrinopeptides A and B (FPA and FPB, thickened segments) from NH2 terminals of Aα‐ and Bβ‐chains, respectively; γ‐chain is not affected by thrombin. Four oligosaccharides (CHO), each Mr ˜ 2,500, are attached to the Bβ‐ and γ‐chains, endowing fibrinogen as a glycoprotein. There are 29 disulfide bonds (SS), 3 of which link 2 halves of the fibrinogen molecule: 1 bond is between Aα‐chains and 2 bonds between γ‐chains. Sites available for factor XIIIa‐catalyzed cross‐linking between lysine donors (XL, arrow pointing upward) and glutamine acceptors (XL, arrow pointing downward) are located in COOH terminals of Aα‐ and γ‐chains. COOH terminals of Bβ‐ and γ‐chains and adjacent part of connector are cleaved by plasmin as fragment D; corresponding portion of fibrinogen molecule is depicted by electron microscopy as outer nodule and defined as the structural D domain. NH2 terminals of all 3 chains and adjacent part of connector are removed by plasmin as fragment E; this region is demonstrated on electron micrographs of fibrinogen as the central nodule and is called E domain. COOH terminals of Aα‐chains (polar appendages) are loosely structured and possibly fill the space around connector.



Figure 10.

Formation of fibrin. Driving force for assembly of fibrin network originates from specific association of complementary binding sites. One polymerization site (a) is present on fibrinogen molecule D domain. Complementary sites (A) are activated by thrombin in fibrin E domain. Due to a probable rotational symmetry, right half of fibrin molecule is a mirror reflection of left half. Binding between a and A sites on 2 fibrin monomer molecules forms 2 links that hold molecules in a half‐staggered orientation. Extension of this process leads to end‐to‐end polymerization and generation of protofibrils. A new polymerization site (bb) appears on fibrin oligomer, probably because of alignment of 2 D domains; this site is apparently absent in fibrin monomer or dimer. A complementary site (B) is present in E domain of fibrin. Binding of a and A sites may propagate formation of linear fibrin protofibrils, whereas binding of bb with 2 B sites may be responsible for side‐to‐side coalescence of protofibrils.



Figure 11.

Degradation of fibrinogen by plasmin. Initial proteolytic attack removes the COOH terminal of Aα‐chain as fragment P45 and its degradation product fragment A. Fragment X is a group of derivatives, the less degraded of which are coagulable by thrombin. Fragments X and Y are cleaved asymmetrically to form terminal degradation products, fragments D and E. From 1 fibrinogen molecule 2 molecules of fragment D and 1 of fragment E are formed.



Figure 12.

Degradation of cross‐linked fibrin by plasmin. Initial enzyme action cleaves cross‐linked α‐chain COOH‐terminal fragments as a mixture of derivatives. Next exposed connectors are disrupted and a (DD)E complex liberated. Components of the complex are derived from 3 different fibrin monomer molecules and 2 fragments D are kept together by covalent cross‐link bonds. Fragment E in the complex still has A and B polymerization sites; however, after long proteolysis with plasmin the sites are damaged and the complex falls apart.



Figure 13.

Plasminogen activation. Human plasminogen, a single polypeptide chain protein, contains 790 amino acid residues, NH2‐terminal glutamic acid, 5 homologous loop structures (“krinkles”), and 24 disulfide bonds. On action of plasmin on Glu‐plasminogen a cleavage at Lys76‐Lys77 occurs, releasing NH2‐terminal peptide and yielding Lys‐plasminogen. Cleavage of the Arg560‐Val561 bond by activators results in formation of Lys‐plasmin, composed of 2 chains (A and B) linked by 2 disulfide bonds. Lys‐plasminogen activation seems approximately 10 times faster than that of Gluplasminogen. In presence of plasmin inhibitors the cleavage of NH2‐terminal peptide is significantly decreased and Glu‐plasmin (potentially convertible into Lys‐plasmin) is formed.



Figure 14.

Physiological fibrinolysis. During physiological dynamic equilibrium, histidine‐rich glycoprotein and other antiactivators regulate interaction of plasminogen in blood with plasminogen activators. Even if minute amounts of plasmin are generated (e.g., after release of vascular plasminogen activator following stress) the enzyme is promptly inactivated by α2‐antiplasmin. On activation of the blood coagulation system, fibrin clot is formed, which not only strongly binds vascular plasminogen activator and plasminogen from blood but also significantly accelerates the activation rate. Resulting plasmin is protected from inhibitors while attached to fibrin. Enzyme is inactivated by α2‐antiplasmin and α2‐macroglobulin after proteolytic dissolution of fibrin and liberation into the liquid phase of blood. Thus the fibrin network catalyzes initiation and regulation of fibrinolysis. Kallikrein and factor XIa can activate plasminogen in the liquid phase, but their role appears less significant and not specifically associated with fibrin clot.

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How to Cite

Robert W. Colman, Andrei Z. Budzynski. Blood Coagulation and Fibrinolysis. Compr Physiol 2011, Supplement 10: Handbook of Physiology, The Respiratory System, Circulation and Nonrespiratory Functions: 495-544. First published in print 1985. doi: 10.1002/cphy.cp030116