Relevant bibliographies by topics / Fibrin-monomers

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Academic literature on the topic 'Fibrin-monomers'

Author: Grafiati
Published: 2 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Fibrin-monomers"

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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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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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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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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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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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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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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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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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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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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Conference papers on the topic "Fibrin-monomers"

1

Oehler, G., H. Klaus, E. Spanuth, and K. E. Stötzer. "DETECTION OF SOLUBLE FIBRIN MONOMER COMPLEXES - COMPARISON OF A HAEMAGGLUTINATION ASSAY WITH THE ETHANOL GELATION TEST." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644886.

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Hypercoagulability and disseminated intravascularcoagulation (DIC) are characterized by the presenceof circulating fibrin monomer complexes in plasma.In342 patients with possible DIC fibrin monomers, fibrinogen, reptilase time, antithrombin III and othercoagulation parameters were determined at frequent intervals.Testing of soluble fibrin monomer complexeswas performed using a sensitive and reliable haemagglut- ination assay, with red cells sensitized by fibrin monomers (FM-Test) and the ethanol gelation test(EGT). Method comparison regarding the influence offibrinogen levels and fibrin degrad
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Meusburger, S., R. Beckmann, J. Wojta, and B. R. Binder. "RELATION OP FIBRIN STIMULATION OF tPA MEDIATED PLASMINOGEN ACTIVATION AND FIBRIN BINDING TOWARDS FIBRONEKTIN AS REVEALED BY A MONOCLONAL ANTIBODY (MAB) AGAINST FCB-2 FIBRINOGEN FRAGMENTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644403.

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Fibrin binds to the finger domain of fibronektin via the C-terminal end of the chain and it was reported previously by us that in a fluid phase assay fibronektin inhibits fibrin enhancement of plasminogen activation by tPA. However, other have shown that tPA binds to fibronectin thereby possibly mediating enhanced matrix bound plasmin formation. In the present study we tried to further characterize the interaction between fibronectin and fibrin in regard to fibrin dependent enhancement of plasminogen activation by tPA. For fibrin binding to fibronectin we have developed an ELISA system using f
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Minno, G. Di, A. M. Cerbone, F. Cirillo, et al. "ABNORMAL FIBRINOGEN (FIBRINOGEN NAPLES) CHARACTERIZED BY DETECTIVE INTERACTION WITH THROMBIN AND PLASMIN IN TWO YOUNG SIBLINGS WITH ARTERIAL THROMBOSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644698.

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Prolonged thrombin time (partially corrected by calcium chloride) and normal reptilase time were found in the plasma of two siblings with arterial thrombosis. Their purified fibrinogen showed similar abnormalities as well as impaired fibrino-peptide release in response to thrombin, delayed polymerization of pre-formed fibrin monomers and normal sialic content. Binding of radiolabelled thrombin by patient's fibrin was 30% of normal. Supernatants from patients' fibrin clots contained abnormal amounts of thrombin (not adsorbed by fibrin) and caused abnormal enhancement of platelet aggregation and
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LAU, H. K. F. "PROPERTIES OF A HUMAN FIBRINOGEN A α-CHAIN DEGRADATION FRAGMENT". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643333.

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A fragment of human fibrinogen was obtained by a 30-min digest of fibrinogen with plasmin. The reaction was terminated by 10 mM diisopropyl fluorophosphate and the fragment obtained by sequential gel filtrations on Sephacryl S-200 and Bio Gel P-30. This fragment displayed a single band on both reduced and nonreduced SDS polyacrylamide electrophoreses with a relative Mr of ∼25,000. It did not crossreact with antisera against fibrinogen, fragment D or fragment E and suggested its sequestered location in native fibrinogen. An antiserum raised against this fragment reacted with the fragment itself
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Bögli, C., A. Hofer, M. Furlan, E. A. Beck, F. Baudo та R. Redaelli. "FIBRINOGEN MILANO III, A NEW ABNORMAL HEREDITARY FIBRINOGEN VARIANT WITH A DEFECT IN THE Aα-CHAIN". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644699.

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A new congential dysfibrinogenemia, denoted as Milano III, was found in a 13-year-old girl with recurrent thrombophlebitis. Plasma of the patient exhibited prolonged thrombin and reptilase times. Plasma fibrinogen concentration, determined by a functional assay, was less than 0.2 g/1 while the immunological method revealed normal fibrinogen levels. Fibrinopeptide release, induced by thrombin, was normal whereas polymerization of fibrin monomers was delayed. Under conventional conditions for normal fibrin aggregation, with and without added calcium, the final turbidity of abnormal fibrin was lé
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Ersdel, E., M. Andersson, and S. Rosen. "DETERMINATION OF SOLUBLE FIBRIN IN PLASMA WITH A CHR0M0GENIC KIT METHOD UTILIZING THE HIGH AFFINITY PLASMIN SUBSTRATE S-2390." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643058.

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A sensitive and quantitative assay of soluble fibrin is of clinically diagnostic relevance in an early thrombotic state where there is a risk for development of DIC. Recently Wiman and Ranby (Thromb. Haemostas 55, 189-193 (1986)) published a spectro-photometric assay which met these criterions. The single-stage assay procedure is based upon activation of Glu-Plasminogen to Plasmin by t-PA in the presence of soluble fibrin and hydrolysis of the chromogenic plasmin substrate S-2390, H-D-Val-Phe-Lys-pNA, which has a high affinity for plasmin. The rate of plasmin generation is correlated to the am
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Arocha Piñango, C. L., A. Torres, R. Marchi, et al. "A NEW THROMBOTIC DYSFIBRINOGENEMIA PRESENT IN SEVERAL MEMBERS OF A VENEZUELAN FAMILY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643340.

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Up to the present, 16 dysfibrinogenemias have been described with thrombotic symptomatology, of which 3 cases showed low affinity of the fibrin for thrombin.In this study, we describe a family with an elevated frequency of thrombotic episodes which may be due to an alteration in the fibrinogen molecule causing a defective adsorption of thrombin by the fibrin formed.Two women, mother and daughter, were admitted to our clinic with a history of repeated pulmonary thromboembolisms. Coagulation studies (which included Antithrombin III, Protein C, etc.) revealed only a prolonged thrombin time with h
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Berk, H. R. "THE EFFECT OF SHEAR ON OLIGOMER FORMATION; EFFECTIVE REMOVAL OF MONOMERS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644220.

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Fibrin polymerization has been found to be influenced by shear flow conditions (Puryear,1980). In order to determine which mechanisms are responsible for theeffect reported it is necessary to look at the various stages in fibrin polymerization. It is known that the enzymatic attack of thrombin on fibrinogen is not influenced by shear (Sellers,1981). The next step, which is investigated in this study, is the oligomer-early protofibril stage.Fibrinogen (human, Kabi) is reacted with thrombin (human, Sigma) under Couette flow conditions (volume-averaged shear 0-250sec-l) in a pH 6.8, 4mM CaC12, HE
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Ruf, W., A. Bender, K. T. Preissner, D. A. Lane, and G. Müller-Berghaus. "FIBRINOPEPTIDE B RELEASE FROM NORMAL FIBRINOGEN AND FIBRINOGEN LONDON I IN THE PRESENCE OF INHIBITORS OF FIBRIN POLYMERIZATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643341.

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The fibrinopeptides A and B (FPA and FPB) are cleaved from the fibrinogen molecule with different rates. In the initial phase of the thrombin-fibrinogen reaction, FPB is released with a slow rate, which is enhanced upon polymerization of desA-fi-brin monomers. The aim of the present study was to further characterize the mechanism leading to the enhanced rate of FPB release during polymerization. For this purpose, the release of FPB from normal fibrinogen and from fibrinogen London I, which exhibits a polymerization defect located in the D-domain, was studied in the presence and absence of the
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Francis, C. W., and V. J. Marder. "RAPID FORMATION OF LARGE MOLECULAR WEIGHT O-P0LYMERS IN CROSSLINKED FIBRIN INDUCED BY HIGH FACTOR XIII CONCENTRATIONS: ROLE OF PLATELET FACTOR XIII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643311.

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Following fibrin polymerization, activated factor XIII stabilizes the clot by catalyzing the formation of specific intermolecular covalent crosslinks between pairs of y chains to form dimers and also among two or more a chains to form polymers. We have identified a series of previously uncharacterized a chain polymers with a wide range of sizes, including some with apparent Mr in excess of several million. Additionally, we establish the role of high concentrations of factor XIII in the extent and rate of α-polymer formation and provide evidence that the factor XIII required can be provided by
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