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Journal articles on the topic 'Fibrin-monomers'

Author: Grafiati

Published: 2 June 2025

Last updated: 31 July 2025

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1

Bleyl, U. "Die Atemnotsyndrom-Lunge-Sequestrationsorgan für lösliches Fibrin." Hämostaseologie 05, no. 03 (1985): 103–7. http://dx.doi.org/10.1055/s-0038-1655109.

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SummaryMultifactorial permeability disorders of the alveolo-capillary exchange membranes are one of the main pathophysiologic principles of pulmonary failure in the ARDS. Under the conditions of a generalized activation of coagulation these permeability disorders result in a leakage of circulating fibrin monomers and oligomers into the pulmonary interstitia and alveoli, even before the monomers and oligomers may precipitate intravascularly to disseminated microthrombi. Under the patho-physiologic conditions of an ARDS the lungs thus become an organ of excretion for soluble, intravascularly cir

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2

Refaai, Majed, Paul Riley, Tatsiana Mardovina, and Phoenix Bell. "The Clinical Significance of Fibrin Monomers." Thrombosis and Haemostasis 118, no. 11 (2018): 1856–66. http://dx.doi.org/10.1055/s-0038-1673684.

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Introduction Fibrin monomer (FM) concentrations reflect pro-thrombin activity and have the potential to predict thrombotic events relatively earlier than other haemostatic markers. Most often, FM are compared with D-dimer (DD) as increased DD have been documented in disseminated intravascular coagulation (DIC), deep vein thrombosis (DVT) and pulmonary embolism. Although DD have a high sensitivity and negative predictive value, their specificity is much lower depending on the assay chosen, clinical pre-test probability and patient condition. There are limited reports investigating the utility o

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3

Hunziker, E. B., P. W. Straub, and A. Haeberli. "Molecular morphology of fibrin monomers and early oligomers during fibrin polymerization." Journal of Ultrastructure and Molecular Structure Research 98, no. 1 (1988): 60–70. http://dx.doi.org/10.1016/s0889-1605(88)80934-0.

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4

Wada, Yasuo, Kazuki Niwa, Hisato Meakawa та ін. "A New Type of Congenital Dysfibrinogen, Fibrinogen Bremen, with an Aα Gly-17 to Val Substitution Associated with Hemorrhagic Diathesis and Delayed Wound Healing". Thrombosis and Haemostasis 70, № 03 (1993): 397–403. http://dx.doi.org/10.1055/s-0038-1649593.

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SummaryWe have identified a new type of Aα Gly-17 to Val substitution in a congenital dysfibrinogen, fibrinogen Bremen, derived from a 15-year-old boy having manifested easy bruising and delayed wound healing. The functional abnormality was characterized by altered fibrin monomer polymerization, which became evident by increasing the salt concentration and pH. A synthetic tetrapeptide with a sequence of the amino-terminal segment of normal fibrin α-chain, Gly-Pro-Arg-Val, substantially inhibited polymerization of both normal and the patient-derived fibrin monomers. A synthetic tetrapeptide wit

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5

Miszta, Adam, Leonie Pelkmans, Theo Lindhout, et al. "Thrombin-Dependent Incorporation of Von Willebrand Factor into a Fibrin Network." Blood 124, no. 21 (2014): 101. http://dx.doi.org/10.1182/blood.v124.21.101.101.

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Abstract Attachment of platelets from the circulation onto a growing thrombus is a process involving multiple platelet receptors, endothelial matrix components and coagulation factors. It has been indicated that VWF crosslinks to polymerizing fibrin. Bound VWF further recruits and activates platelets via interactions with the platelet receptor complex glycoprotein Ib (GPIb). The aim of our study was to investigate the mechanism of VWF incorporation into a fibrin network and thereby characterize the role of VWF in arterial thrombus growth. We monitored the interactions of von Willebrand factor

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6

Sugo, Teruko, Chizuko Nakamikawa, Hiroshi Takano та ін. "Fibrinogen Niigata With Impaired Fibrin Assembly: An Inherited Dysfibrinogen With a Bβ Asn-160 to Ser Substitution Associated With Extra Glycosylation at Bβ Asn-158". Blood 94, № 11 (1999): 3806–13. http://dx.doi.org/10.1182/blood.v94.11.3806.

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Abstract A novel BβAsn-160 (TAA) to Ser (TGA) substitution has been identified in fibrinogen Niigata derived from a 64-year-old asymptomatic woman, who is heterozygotic for this abnormality. The mutation creates an Asn-X-Ser–type glycosylation sequence, and a partially sialylated biantennary oligosaccharide was linked to the BβAsn-158 residue. The functional abnormality was attributed to delayed lateral association of normally formed double-stranded protofibrils based on normal cross-linking of fibrin γ-chains and tissue-type plasminogen activator-catalyzed plasmin generation by polymerizing f

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7

Sugo, Teruko, Chizuko Nakamikawa, Hiroshi Takano та ін. "Fibrinogen Niigata With Impaired Fibrin Assembly: An Inherited Dysfibrinogen With a Bβ Asn-160 to Ser Substitution Associated With Extra Glycosylation at Bβ Asn-158". Blood 94, № 11 (1999): 3806–13. http://dx.doi.org/10.1182/blood.v94.11.3806.423a17_3806_3813.

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A novel BβAsn-160 (TAA) to Ser (TGA) substitution has been identified in fibrinogen Niigata derived from a 64-year-old asymptomatic woman, who is heterozygotic for this abnormality. The mutation creates an Asn-X-Ser–type glycosylation sequence, and a partially sialylated biantennary oligosaccharide was linked to the BβAsn-158 residue. The functional abnormality was attributed to delayed lateral association of normally formed double-stranded protofibrils based on normal cross-linking of fibrin γ-chains and tissue-type plasminogen activator-catalyzed plasmin generation by polymerizing fibrin mon

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8

Dardik, BN, and JR Shainoff. "Kinetic characterization of a saturable pathway for rapid clearance of circulating fibrin monomer." Blood 65, no. 3 (1985): 680–88. http://dx.doi.org/10.1182/blood.v65.3.680.680.

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Abstract The mechanism of clearance of circulating fibrin monomer was investigated in rabbits through (1) study of decay in plasma concentrations of 125I-labeled monomers with variant fibrinopeptide content and (2) concurrent analysis of decay of the monomers relative to coinjected 131I-fibrinogen. Under the conditions employed, essentially all of the fibrin became distributed in a soluble form in plasma and decayed independently of the coinjected fibrinogen. Among the species of fibrin studied, monomer lacking fibrinopeptide A alone (alpha-fibrin) underwent very rapid clearance by a saturable

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9

Dardik, BN, and JR Shainoff. "Kinetic characterization of a saturable pathway for rapid clearance of circulating fibrin monomer." Blood 65, no. 3 (1985): 680–88. http://dx.doi.org/10.1182/blood.v65.3.680.bloodjournal653680.

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The mechanism of clearance of circulating fibrin monomer was investigated in rabbits through (1) study of decay in plasma concentrations of 125I-labeled monomers with variant fibrinopeptide content and (2) concurrent analysis of decay of the monomers relative to coinjected 131I-fibrinogen. Under the conditions employed, essentially all of the fibrin became distributed in a soluble form in plasma and decayed independently of the coinjected fibrinogen. Among the species of fibrin studied, monomer lacking fibrinopeptide A alone (alpha-fibrin) underwent very rapid clearance by a saturable mechanis

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10

Godal, H. C., U. Abildgaard, and P. Kierulf. "24. ETHANOL GELATION AND FIBRIN MONOMERS IN PLASMA." Scandinavian Journal of Haematology 8, S13 (2009): 189–91. http://dx.doi.org/10.1111/j.1600-0609.1971.tb02006.x.

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11

Holtkötter, H., and E. Zimmermann. "Determination of fibrin monomers in pathological plasma samples." Fibrinolysis 4 (January 1990): 23. http://dx.doi.org/10.1016/0268-9499(90)90085-x.

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12

Rabaud, M., F. Lefebvre, M. T. Martin, M. Aprahamian, R. Schmitthaeusler, and J. P. Cazenave. "Adduct formation between soluble fibrin monomers and elastin." Biomaterials 8, no. 3 (1987): 217–22. http://dx.doi.org/10.1016/0142-9612(87)90067-6.

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13

Nilsen, D. W. T., F. Brosstad, P. Kierulf, and H. C. Godal. "Binding of Various Thrombin Fractions to Fibrin and the Influence of AT-III on Their Adsorption." Thrombosis and Haemostasis 55, no. 03 (1986): 352–56. http://dx.doi.org/10.1055/s-0038-1661562.

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SummaryHuman thrombin with high affinity for fibrin was obtained by subjecting purified thrombin to affinity chromatography on Sepharose insolubilized fibrin monomers, after addition of a radioiodinated subsample of thrombin, molar ratio 1:600. As judged by radioprofiling of the electrophoretic distribution of high-affinity thrombin on 10 per cent polyacrylamide gel containing urea/SDS, the preparation consisted of 70 per cent a-thrombin, 28 per cent β-thrombin and only 2 per cent γ-thrombin. Although a-thrombin was bound more strongly to insolubilized fibrin monomers than the other subfractio

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14

Chernysh, Irina N., Chandrasekaran Nagaswami, and John W. Weisel. "Visualization and identification of the structures formed during early stages of fibrin polymerization." Blood 117, no. 17 (2011): 4609–14. http://dx.doi.org/10.1182/blood-2010-07-297671.

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AbstractWe determined the sequence of events and identified and quantitatively characterized the mobility of moving structures present during the early stages of fibrin-clot formation from the beginning of polymerization to the gel point. Three complementary techniques were used in parallel: spinning-disk confocal microscopy, transmission electron microscopy, and turbidity measurements. At the beginning of polymerization the major structures were monomers, whereas at the middle of the lag period there were monomers, oligomers, protofibrils (defined as structures that consisted of more than 8 m

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15

Bouchama, Abderrezak, Françoise Bridey, Muhammad M. Hammami, et al. "Activation of Coagulation and Fibrinolysis in Heatstroke." Thrombosis and Haemostasis 76, no. 06 (1996): 0909–15. http://dx.doi.org/10.1055/s-0038-1650685.

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SummaryHemorrhagic diathesis and widespread microthrombosis are common in heatstroke. To assess the early stages of coagulopathy in heatstroke, thrombin-antithrombin III (TAT), fibrin monomers, plasmin-a2-antiplasmin (PAP), plasminogen and D-Dimer were measured in 16 heatstroke patients (means ± SE rectal temperature 42.3 ± 0.2° C) pre- and postcooling and compared with 8 heatstressed and 23 normal controls.Comparing heatstroke patients with normal controls, TAT, fibrin monomers, PAP and D-Dimer were elevated to (median (range)) 16.5 (4-1000) versus 3.5 (2-7.2) Μg/l p<0.001,16 (4-113) versu

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16

Morris, Timothy A., James J. Marsh, Roberto Fagnani, Michael Hagan та Kenneth M. Moser. "Degree of Polymer Organization Decreases the Binding of a Monoclonal Antibody Raised against the β-Chain Amino Terminus of Fibrin". Thrombosis and Haemostasis 77, № 04 (1997): 704–9. http://dx.doi.org/10.1055/s-0038-1656038.

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SummaryAccurate non-invasive diagnosis of deep venous thrombosis and pulmonary embolism remains an elusive goal. Radiolabeled antibodies specific for the epitope exposed on the β-chain of fibrin after fibrino- peptide B release (anti-β) enabled in situ imaging of thrombi in experimental subjects with nuclear medicine techniques. When used in patients anticoagulated for thrombo-embolic disease, however, the antibody was unable to reliably image the thrombi. We postulated that the neoepitope on the β-chain of fibrin is covered up as fibrin organizes into a polymer network and is therefore expose

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17

Collen, D. "8. HYDROSTATIC PRESSURE AND REVERSIBLE POLYMERIZATION OF FIBRIN MONOMERS*." Scandinavian Journal of Haematology 8, S13 (2009): 75. http://dx.doi.org/10.1111/j.1600-0609.1971.tb01987.x.

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18

Lütjens, A., T. W. Jonkhoff-Slok, C. Sandkuijl, E. A. v. d. Veen, and J. v. d. Meer. "Polymerisation and crosslinking of fibrin monomers in diabetes mellitus." Diabetologia 31, no. 11 (1988): 825–30. http://dx.doi.org/10.1007/bf00277485.

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19

Bänninger, H., B. Lämmle, and M. Furlan. "Polymerization of fibrin monomers results in increased thrombin binding." Fibrinolysis 4 (January 1990): 8. http://dx.doi.org/10.1016/0268-9499(90)90045-l.

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20

Janmey, Paul A., and John D. Ferry. "Gel formation by fibrin oligomers without addition of monomers." Biopolymers 25, no. 7 (1986): 1337–44. http://dx.doi.org/10.1002/bip.360250712.

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21

Galanakis, Dennis K., Anna Protopopova, Liudi Zhang, et al. "Fibers Generated by Plasma Des-AA Fibrin Monomers and Protofibril/Fibrinogen Clusters Bind Platelets: Clinical and Nonclinical Implications." TH Open 05, no. 03 (2021): e273-e285. http://dx.doi.org/10.1055/s-0041-1725976.

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Abstract Objective Soluble fibrin (SF) is a substantial component of plasma fibrinogen (fg), but its composition, functions, and clinical relevance remain unclear. The study aimed to evaluate the molecular composition and procoagulant function(s) of SF. Materials and Methods Cryoprecipitable, SF-rich (FR) and cryosoluble, SF-depleted (FD) fg isolates were prepared and adsorbed on one hydrophilic and two hydrophobic surfaces and scanned by atomic force microscopy (AFM). Standard procedures were used for fibrin polymerization, crosslinking by factor XIII, electrophoresis, and platelet adhesion.

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22

Adam, Soheir S., Nigel S. Key, and Charles S. Greenberg. "D-dimer antigen: current concepts and future prospects." Blood 113, no. 13 (2009): 2878–87. http://dx.doi.org/10.1182/blood-2008-06-165845.

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AbstractThe D-dimer antigen is a unique marker of fibrin degradation that is formed by the sequential action of 3 enzymes: thrombin, factor XIIIa, and plasmin. First, thrombin cleaves fibrinogen producing fibrin monomers, which polymerize and serve as a template for factor XIIIa and plasmin formation. Second, thrombin activates plasma factor XIII bound to fibrin polymers to produce the active transglutaminase, factor XIIIa. Factor XIIIa catalyzes the formation of covalent bonds between D-domains in the polymerized fibrin. Finally, plasmin degrades the crosslinked fibrin to release fibrin degra

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23

Seeger, W., G. Stohr, H. R. Wolf, and H. Neuhof. "Alteration of surfactant function due to protein leakage: special interaction with fibrin monomer." Journal of Applied Physiology 58, no. 2 (1985): 326–38. http://dx.doi.org/10.1152/jappl.1985.58.2.326.

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In isolated rabbit lungs standardized amounts of edema were induced. Stimulation with the Ca ionophore A23187, leukotriene C4, Pseudomonas aeruginosa cytotoxin and human serum (activated complement) all resulted in protein leakage into the alveolar space with no change in the total phospholipid content. The pressure-volume characteristics of the lungs and the characteristics of the lavage surfactant (Wilhelmy balance) were markedly altered, correlating to the lavage protein content. The surfactant alterations were reproduced by addition of perfusion fluid protein to control surfactant in vitro

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24

Vogel, G., and E. Spanuth. "Predictive value of fibrin monomers in postoperative deep vein thrombosis." Klinische Wochenschrift 68, no. 20 (1990): 1020–26. http://dx.doi.org/10.1007/bf01646548.

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25

Martin, M. T., F. Lefebvre, M. Rabaud, and P. V. Graves. "Biochemical study of adduct synthesis between fibrin monomers and elastin." Biomaterials 9, no. 6 (1988): 519–24. http://dx.doi.org/10.1016/0142-9612(88)90048-8.

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26

Hunter, Robert L., Christine Papadea, Christopher J. Gallagher, Donald C. Finlayson, and Irene J. Check. "Increased Whole Blood Viscosity during Coronary Artery Bypass Surgery." Thrombosis and Haemostasis 63, no. 01 (1990): 006–12. http://dx.doi.org/10.1055/s-0038-1645676.

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SummaryThis study was designed to test the hypothesis that soluble fibrin complexes resulting from the trauma of surgery could produce elevated blood viscosity, to characterize the soluble fibrin polymers, and to evaluate in vitro the effect of a new hemorheologic agent, poloxamer 188, on viscosity in these abnormal situations. Ten patients undergoing aortocoronary bypass surgery were studied before and at various times after surgery. By 6 h after surgery, the mean hematocrit decreased by 23%, fibrinogen decreased 48%, and erythrocyte sedimentation rate decreased 33%, whole blood viscosity at

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27

Wasser, M. N. J. M., M. Welling, G. Lamers, E. K. J. Pauwels, and W. Nieuwenhuizen. "Effects of an Antifibrin Monoclonal Antibody and Fragments thereof on Some Properties of Fibrin." Thrombosis and Haemostasis 63, no. 01 (1990): 039–43. http://dx.doi.org/10.1055/s-0038-1645683.

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SummaryAntifibrin monoclonal antibody Y22, of IgG1-subclass, has its epitope in the D-domain of fibrin. In a thrombin time assay, Y22 and its F(ab)2 fragments interfere with clotting of citrated plasma. Transmission and scanning electronmicroscopic studies show that clotting of citrated blood or plasma in the presence of Y22 results in formation of thin, short fibrin fibres. The (smaller) Fab fragments of Y22 did not have an anti-clotting effect. This suggests that the anticoagulant effect of Y22 is due to steric hindrance of the association of fibrin monomers. A control antibody and its F(ab)

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28

Hamano, Akiei, Jun Mimuro, Motonori Aoshima та ін. "Thrombophilic dysfibrinogen Tokyo V with the amino acid substitution of γ Ala327Thr: formation of fragile but fibrinolysis-resistant fibrin clots and its relevance to arterial thromboembolism". Blood 103, № 8 (2004): 3045–50. http://dx.doi.org/10.1182/blood-2003-07-2569.

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Abstract Thrombophilic dysfibrinogen Tokyo V was identified in a 43-year-old man with recurrent thromboembolism. Based on analyses of the patient fibrinogen genes, the amino acid sequence of the aberrant fibrinogen peptide, and deglycosylation experiments, fibrinogen Tokyo V was shown to have an amino acid substitution of γ Ala327Thr and possibly extra glycosylation at γ Asn325 because the mutation confers the N-linked glycosylation consensus sequence Asn-X-Thr. The mutation resulted in impaired function and hypofibrinogenemia (hypodysfibrinogen). Polymerization of fibrin monomers derived from

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29

Dempfle, Carl-Erik, Sotiria Argiriou, Klaus Kucher, H. Müller-Peltzer, Klaus Rübsamen, and Dieter L. Heene. "Analysis of fibrin formation and proteolysis during intravenous administration of ancrod." Blood 96, no. 8 (2000): 2793–802. http://dx.doi.org/10.1182/blood.v96.8.2793.

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Abstract Ancrod is a purified fraction of venom from the Malayan pit viper, Calloselasma rhodostoma, currently under investigation for treatment of acute ischemic stroke. Treatment with ancrod leads to fibrinogen depletion. The present study investigated the mechanisms leading to the reduction of plasma fibrinogen concentration. Twelve healthy volunteers received an intravenous infusion of 0.17 U/kg body weight of ancrod for 6 hours. Blood samples were drawn and analyzed before and at various time points until 72 hours after start of infusion. Ancrod releases fibrinopeptide A from fibrinogen,

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30

Dempfle, Carl-Erik, Sotiria Argiriou, Klaus Kucher, H. Müller-Peltzer, Klaus Rübsamen, and Dieter L. Heene. "Analysis of fibrin formation and proteolysis during intravenous administration of ancrod." Blood 96, no. 8 (2000): 2793–802. http://dx.doi.org/10.1182/blood.v96.8.2793.h8002793_2793_2802.

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Ancrod is a purified fraction of venom from the Malayan pit viper, Calloselasma rhodostoma, currently under investigation for treatment of acute ischemic stroke. Treatment with ancrod leads to fibrinogen depletion. The present study investigated the mechanisms leading to the reduction of plasma fibrinogen concentration. Twelve healthy volunteers received an intravenous infusion of 0.17 U/kg body weight of ancrod for 6 hours. Blood samples were drawn and analyzed before and at various time points until 72 hours after start of infusion. Ancrod releases fibrinopeptide A from fibrinogen, leading t

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31

Chernysh, Irina N., Prashant K. Purohit, Chandrasekaran Nagaswami, and John W. Weisel. "Remodeling of Clots without Proteolytic Digestion." Blood 118, no. 21 (2011): 1184. http://dx.doi.org/10.1182/blood.v118.21.1184.1184.

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Abstract Abstract 1184 Fibrin polymerization is a necessary part of hemostasis but thrombi can obstruct blood vessels and cause heart attacks and strokes, so the possibility of reversing clot formation has significant clinical implications. It is generally assumed that fibrin polymerization is an irreversible process and that clots and thrombi are stable structures until proteolytic digestion, but this supposition has not been critically tested. Using the technique of fluorescence recovery after photobleaching (FRAP) of individual fluorescently labeled fibrin fibers in a clot, we demonstrate h

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32

Whyte, Claire S., Irina N. Chernysh, Marco M. Domingues, et al. "Polyphosphate delays fibrin polymerisation and alters the mechanical properties of the fibrin network." Thrombosis and Haemostasis 116, no. 11 (2016): 897–903. http://dx.doi.org/10.1160/th16-01-0062.

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SummaryPolyphosphate (polyP) binds to fibrin(ogen) and alters fibrin structure, generating a heterogeneous network composed of ‘knots’ interspersed by large pores. Here we show platelet-derived polyP elicits similar structural changes in fibrin and examine the mechanism by which polyP alters fibrin structure. Polymerisation of fibrinogen with thrombin and CaCl2 was studied using spinning disk confocal (SDC) microscopy. PolyP delayed fibrin polymerisation generating shorter protofibrils emanating from a nucleus-type structure. Consistent with this, cascade blue-polyP accumulated in fibrin ‘knot

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33

Rosenfeld, M. A., V. B. Leonova, M. L. Konstantinova, and S. D. Razumovskii. "Self-assembly of fibrin monomers and fibrinogen aggregation during ozone oxidation." Biochemistry (Moscow) 74, no. 1 (2009): 41–46. http://dx.doi.org/10.1134/s0006297909010064.

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34

Ketelhut, R. G., K. Ketelhut, G. Badtke, and H. Philipp. "FIBRIN-MONOMERS - AN EARLY MARKER OF CARDIOVASCULAR JEOPARDY DURING STRENUOUS EXERCISE?" Medicine & Science in Sports & Exercise 34, no. 5 (2002): S290. http://dx.doi.org/10.1097/00005768-200205001-01631.

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Toomes, M., G. Petroianu, WA Werth, and R. Rufer. "FIBRIN MONOMERS (FM) IN MINI PIGS DURING AND AFTER PARAOXON EXPOSURE." Anesthesia & Analgesia 86, Supplement (1998): 156S. http://dx.doi.org/10.1097/00000539-199802001-00155.

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36

Niwa, K., M. Takebe, T. Sugo, et al. "A gamma Gly-268 to Glu substitution is responsible for impaired fibrin assembly in a homozygous dysfibrinogen Kurashiki I." Blood 87, no. 11 (1996): 4686–94. http://dx.doi.org/10.1182/blood.v87.11.4686.bloodjournal87114686.

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A new type of gamma Gly-268 (GGA) to Glu (GAA) substitution has been identified in a homozygous dysfibrinogen by analyses of the affected polypeptide and its encoding gene derived from a 58 year-old man manifesting no major bleeding or thrombosis. The functional abnormality was characterized by impaired fibrin assembly most likely due to failure to construct properly aligned double-stranded fibrin protofibrils. This presumption was deduced from the following findings: (1) Factor XIIIa-catalyzed cross-linking of the fibrin gamma-chains progressed in a normal fashion, indicating that the contact

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37

Janiak, A., T. Plucinski, G. Kupryszewski, and C. S. Cierniewski. "The amino acids that constitute sequence gamma 268-282 of fibrinogen are not involved in fibrin monomer polymerization." Acta Biochimica Polonica 40, no. 4 (1993): 515–20. http://dx.doi.org/10.18388/abp.1993_4792.

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Congenitally abnormal fibrinogens with impaired fibrin monomer polymerization have been described to contain single amino-acid substitutions localized in certain positions of the gamma 275-330 peptide region. To evaluate the role of the amino-acid sequence in the vicinity of Arg275 in fibrin monomer polymerization, the peptide fragment corresponding to gamma 268-282 was synthesized and used to obtain peptide-specific antibodies. These antibodies, when purified immunochemically on the immobilized peptide, bound to the intact fibrinogen and fibrin monomers with the same binding affinity. However

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Baradet, T., J. W. Weisel, and L. D. Peachey. "A study of fibrin clot structure under various ionic conditions using stereoscopic IVEM images." Proceedings, annual meeting, Electron Microscopy Society of America 49 (August 1991): 194–95. http://dx.doi.org/10.1017/s0424820100085277.

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Fibrin clots are formed by the conversion of fibrinogen into fibrin monomers which assemble to produce two-stranded protofibrils that aggregate to form fibers. These fibers may also aggregate laterally with other fibers to form larger fiber bundles. Investigations of fibrin clot structures under various ionic conditions using SEM showed dramatic differences in fiber morphology and clot structure. Fibrin clots formed under various ionic conditions were investigated by the examination of stereoscopic IVEM images. This technique provides greater depth discrimination and higher resolution images o

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39

Sobel, JH, I. Trakht, HQ Wu, S. Rudchenko, and R. Egbring. "Alpha-Chain cross-linking in fibrin(ogen) Marburg." Blood 86, no. 3 (1995): 989–1000. http://dx.doi.org/10.1182/blood.v86.3.989.989.

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Abstract The fibrinogen structural variant, Marburg (A alpha 1–460B beta gamma)2, is comprised of normal B beta and gamma chains but contains severely truncated A alpha chains that are missing approximately one half of their factor XIIIa cross-linking domain. Immunochemical studies of fibrin(ogen) Marburg were conducted to characterize the degree to which deletion of a defined A alpha-chain segment, A alpha 461–610, can affect the process of fibrin stabilization, ie, the factor XIIIa- mediated covalent interaction that occurs between alpha chains of neighboring fibrin molecules and between alp

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Sobel, JH, I. Trakht, HQ Wu, S. Rudchenko, and R. Egbring. "Alpha-Chain cross-linking in fibrin(ogen) Marburg." Blood 86, no. 3 (1995): 989–1000. http://dx.doi.org/10.1182/blood.v86.3.989.bloodjournal863989.

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The fibrinogen structural variant, Marburg (A alpha 1–460B beta gamma)2, is comprised of normal B beta and gamma chains but contains severely truncated A alpha chains that are missing approximately one half of their factor XIIIa cross-linking domain. Immunochemical studies of fibrin(ogen) Marburg were conducted to characterize the degree to which deletion of a defined A alpha-chain segment, A alpha 461–610, can affect the process of fibrin stabilization, ie, the factor XIIIa- mediated covalent interaction that occurs between alpha chains of neighboring fibrin molecules and between alpha chains

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Zhmurov, Artem, Andre E. X. Brown, Rustem I. Litvinov, Ruxandra I. Dima, John W. Weisel, and Valeri Barsegov. "Molecular Structural Origins of Clot and Thrombus Mechanical Properties." Blood 118, no. 21 (2011): 2257. http://dx.doi.org/10.1182/blood.v118.21.2257.2257.

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Abstract Abstract 2257 Although the mechanical function of blood clots to stem bleeding is obvious and higher clot stiffness has been associated with premature coronary thrombosis, we are only now beginning to understand the origins of these vital mechanical characteristics. Fibrinogen, the precursor of fibrin, provides building blocks for the fibrin polymer, the scaffold of blood clots and thrombi. The mechanical properties of fibrin molecules are essential for the ability of clots to accomplish hemostasis and are an important determinant of the pathological properties of thrombi, as they con

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42

Tijburg, P. N., M. J. Ijsseldijk, J. J. Sixma, and P. G. de Groot. "Quantification of fibrin deposition in flowing blood with peroxidase-labeled fibrinogen. High shear rates induce decreased fibrin deposition and appearance of fibrin monomers." Arteriosclerosis and Thrombosis: A Journal of Vascular Biology 11, no. 2 (1991): 211–20. http://dx.doi.org/10.1161/01.atv.11.2.211.

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Gorkun, Oleg V., Yuri I. Veklich, John W. Weisel, and Susan T. Lord. "The Conversion of Fibrinogen to Fibrin: Recombinant Fibrinogen Typifies Plasma Fibrinogen." Blood 89, no. 12 (1997): 4407–14. http://dx.doi.org/10.1182/blood.v89.12.4407.

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Abstract Plasma fibrinogen is a mixture of multiple molecular forms arising mainly through alternative mRNA processing and subsequent posttranslational modification. Recombinant fibrinogen is synthesized without alternative mRNA processing in a cultured cell system that may generate novel posttranslational modifications. Thus, to show that recombinant fibrinogen can serve as a functional model for plasma fibrinogen, we have examined the conversion of fibrinogen to fibrin, comparing the recombinant with the plasma protein. We examined the kinetics of (1) thrombin-catalyzed fibrinopeptide releas

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Ariëns, Robert A. S., Thung-Shenq Lai, John W. Weisel, Charles S. Greenberg, and Peter J. Grant. "Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms." Blood 100, no. 3 (2002): 743–54. http://dx.doi.org/10.1182/blood.v100.3.743.

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Abstract Factor XIII and fibrinogen are unusual among clotting factors in that neither is a serine protease. Fibrin is the main protein constituent of the blood clot, which is stabilized by factor XIIIa through an amide or isopeptide bond that ligates adjacent fibrin monomers. Many of the structural and functional features of factor XIII and fibrin(ogen) have been elucidated by protein and gene analysis, site-directed mutagenesis, and x-ray crystallography. However, some of the molecular aspects involved in the complex processes of insoluble fibrin formation in vivo and in vitro remain unresol

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Baker, D. C., and R. A. Green. "Coagulation Defects of Aflatoxin Intoxicated Rabbits." Veterinary Pathology 24, no. 1 (1987): 62–70. http://dx.doi.org/10.1177/030098588702400111.

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Twelve New Zealand white rabbits were intoxicated with aflatoxin B1. Most rabbits developed a coagulation defect near the time of death. Immediately prior to death there were significant decreases in factors V, VII, and VIII coagulant activities and fibrinogen concentration without a change in plasma fibrin(ogen) degradation product concentration, platelet number, and detectable plasma fibrin monomers. Microscopic evidence of disseminated intravascular coagulation was present in one rabbit with marked, diffuse hepatic necrosis. Terminal serum albumin concentration was significantly correlated

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46

Furlan, Miha, Bettina Stucki, Colette Steinmann, Myriam Jungo та Bernhard Lämmle. "Normal Binding of Calcium to Five Fibrinogen Variants with Mutations in the Carboxy Terminal Part of the γ-Chain". Thrombosis and Haemostasis 76, № 03 (1996): 377–83. http://dx.doi.org/10.1055/s-0038-1650587.

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SummaryCalcium ions are known to accelerate polymerization of fibrin monomers. Each of the two carboxy terminal domains of normal fibrinogen contains one high-affinity calcium binding site that seems to be situated close to the polymerization site in the γ-chain. Most hitherto described functionally defective fibrinogen variants showed impaired clot formation. Since the tightly bound calcium ions may influence the conformation of the polymerization site, the question arises whether the abnormal clotting of a dysfibrinogen might be due to defective calcium binding. We investigated binding of ca

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Janmey, PA, and SE Lind. "Capacity of human serum to depolymerize actin filaments." Blood 70, no. 2 (1987): 524–30. http://dx.doi.org/10.1182/blood.v70.2.524.524.

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Abstract Human blood depolymerizes filamentous (F-)actin. The interaction of actin filaments and monomers with human serum was studied by following the kinetics and extent of the depolymerization of pyrene-labeled F- actin and by analysis of serum proteins adhering to immobilized actin monomers. In physiologic Ca2+ concentrations, the depolymerization of F- actin proceeds in two stages: a rapid phase, attributed to direct severing of filaments by plasma gelsolin, and a slow phase attributed to the binding of actin monomers to vitamin D-binding protein (DBP). Without Ca2+, only the slow phase i

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48

Janmey, PA, and SE Lind. "Capacity of human serum to depolymerize actin filaments." Blood 70, no. 2 (1987): 524–30. http://dx.doi.org/10.1182/blood.v70.2.524.bloodjournal702524.

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Human blood depolymerizes filamentous (F-)actin. The interaction of actin filaments and monomers with human serum was studied by following the kinetics and extent of the depolymerization of pyrene-labeled F- actin and by analysis of serum proteins adhering to immobilized actin monomers. In physiologic Ca2+ concentrations, the depolymerization of F- actin proceeds in two stages: a rapid phase, attributed to direct severing of filaments by plasma gelsolin, and a slow phase attributed to the binding of actin monomers to vitamin D-binding protein (DBP). Without Ca2+, only the slow phase is observe

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Bouvier, Sylvie, Eva Cochery-Nouvellon, Jean-Luc Faillie, Géraldine Lissalde-Lavigne, Jean-Yves Lefrant, and Jean-Christophe Gris. "Fibrin-related markers in patients with septic shock: Individual comparison of D-dimers and fibrin monomers impacts on prognosis." Thrombosis and Haemostasis 106, no. 12 (2011): 1228–30. http://dx.doi.org/10.1160/th11-07-0489.

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Weisberg, LJ, DT Shiu, PR Conkling, and MA Shuman. "Identification of normal human peripheral blood monocytes and liver as sites of synthesis of coagulation factor XIII a-chain." Blood 70, no. 2 (1987): 579–82. http://dx.doi.org/10.1182/blood.v70.2.579.579.

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Abstract Factor XIII is the fibrin-stabilizing factor that covalently cross- links fibrin monomers to form a highly organized, stable fibrin clot. The plasma form of factor XIII is a heterodimer, a2b2, consisting of two a-chains and two b-chains; the intracellular form, such as in platelets and placenta, is a dimer, a2, consisting of a-chains only. The catalytic function of factor XIII, a transglutaminase, resides in the a-chain. To address questions regarding sites of synthesis of factor XIII a-chain, an EcoRI restriction fragment from the protein- coding region of the factor XIII a-chain cDN

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