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Journal articles on the topic 'Fibrinogen. Polymerization'

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Published: 4 June 2021

Last updated: 7 February 2022

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1

Hogan, Kelly, Susan Lord, Nobuo Okumura та ін. "A Functional Assay Suggests that Heterodimers Exist in Two C-Terminal γ-Chain Dysfibrinogens: Matsumoto I and Vlissingen/Frankfurt IV". Thrombosis and Haemostasis 83, № 04 (2000): 592–97. http://dx.doi.org/10.1055/s-0037-1613869.

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SummaryBecause it contains three pairs of polypeptides, fibrinogen isolated from heterozygous individuals is expected to be a mixture of homodimers and heterodimers. Nevertheless, heterozygous individuals with only homodimers have been identified. We synthesized two recombinant fibrinogens with the mutations from fibrinogen Vlissingen/ Frankfurt IV (γΔ319, 320) and Matsumoto I (γD364H), both identified in heterozygous individuals. We found that polymerization of these fibrinogens was undetectable in 30 min; polymerization of a 1:1 mixture of variant and normal fibrinogen was the same as polyme

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2

Rodeghiero, F., G. C. Castaman, A. Dal Belin Peruffo, et al. "Fibrinogen Vicenza and Genova II: Two New Cases of Congenital Dysfibrinogenemia with Isolated Defect of Fibrin Monomer Polymerization and Inhibitory Activity on Normal Coagulation." Thrombosis and Haemostasis 57, no. 03 (1987): 252–58. http://dx.doi.org/10.1055/s-0038-1651111.

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SummaryTwo new cases of congenital dysfibrinogenemia are presented in which defective fibrin monomer polymerization and inhibitory activity on normal coagulation were observed. They have been tentatively called fibrinogen Vicenza and Genova II. The first was discovered in a family with mild bleeding diathesis, the second in an asymptomatic family. In almost all reported cases of fibrinogens with defective fibrin monomer polymerization, additional functional or structural defects have been detected. In our cases, on the contrary, detailed investigations failed to show any other abnormality. Fib

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3

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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4

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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5

Huang, Lihong, and Susan T. Lord. "From Fibrinogen to Fibrin: Dynamic Light Scattering to Probe the Mechanism of Protofibril Assembly Into Fibers." Blood 116, no. 21 (2010): 1156. http://dx.doi.org/10.1182/blood.v116.21.1156.1156.

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Abstract Abstract 1156 The conversion from fibrinogen to fibrin, and fibrin clot structure and function, are important problems in cardiovascular research. The mechanism of fibrin clot formation remains undefined after more than 50 years of study. We have developed a new method to monitor polymerization and examine the products formed prior to gelation. We monitored polymerization by dynamic light scattering (DLS), a sensitive method to measure formation of small complexes. We “stopped” thrombin-catalyzed polymerization at different phases by crosslinking the polymers with formaldehyde and ana

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6

Mosesson, M. W. "Fibrinogen and fibrin polymerization." Blood Coagulation & Fibrinolysis 8, no. 5 (1997): 257–67. http://dx.doi.org/10.1097/00001721-199707000-00001.

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7

Siebenlist, Kevin, Marijke Voskuilen, Willem Nieuwenhuizen, and Michael Mosesson. "Evaluation of the Factors Contributing to Fibrin–dependent Plasminogen Activation." Thrombosis and Haemostasis 79, no. 04 (1998): 796–801. http://dx.doi.org/10.1055/s-0037-1615067.

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SummaryPolymerized fibrin strongly enhances tissue plasminogen activator (tPA)-mediated plasminogen activation, concomitant with exposure of ‘fibrin-specific’ epitopes at ‘Aα148-160’ and ‘γ312-324’. To investigate which aspects of polymerization are involved in these activities, we explored the fibrin polymerization process by evaluating the ability of factor XIIIa-crosslinked fibrinogen polymers to expose ‘fibrin-specific’ epitopes and enhance plasminogen activation. Crosslinked normal fibrinogen, fibrinogen with deficient [des Bβ1-42] or defective [Birmingham (AαR16H)] fibrin ‘D:E’ assembly

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8

Park, Rojin, Lifang Ping, Jaewoo Song та ін. "Fibrinogen residue γAla341 Is Necessary for Calcium Binding and ‘A-a’ interaction." Blood 116, № 21 (2010): 1154. http://dx.doi.org/10.1182/blood.v116.21.1154.1154.

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Abstract Abstract 1154 Fibrinogen, a 340-kDa glycoprotein has essential roles in blood coagulation and platelet aggregation. Fibrinogen is a complex molecule consisting of 3 pairs of Aα, Bβ, and γ chains intertwined to form a tri-nodular molecule with 2 terminal D regions and a central E region. The fibrinogen γ-nodule, a part of D region, has several important sites relating to fibrinogen function, which are the high affinity calcium binding site, hole ‘a’ that binds with knob ‘A’, and the D:D interface. Residue γAla341, which is located in the vicinity of those sites and conserved between al

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9

Keller, Margaret A., Josè Martinez, Timothy C. Baradet та ін. "Fibrinogen Philadelphia, a hypodysfibrinogenemia characterized by abnormal polymerization and fibrinogen hypercatabolism due to γ S378P mutation". Blood 105, № 8 (2005): 3162–68. http://dx.doi.org/10.1182/blood-2004-04-1621.

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AbstractFibrinogen Philadelphia, a hypodysfibrinogenemia described in a family with a history of bleeding, is characterized by prolonged thrombin time, abnormal fibrin polymerization, and increased catabolism of the abnormal fibrinogen. Turbidity studies of polymerization of purified fibrinogen under different ionic conditions reveal a reduced lag period and lower final turbidity, indicating more rapid initial polymerization and impaired lateral aggregation. Consistent with this, scanning and transmission electron microscopy show fibers with substantially lower average fiber diameters. DNA seq

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10

Tanaka, Hitoshi, Fumiko Terasawa, Toshiro Ito та ін. "Fibrinogen Matsumoto V: a Variant with Aα19 Arg → Gly (AGG → GGG)". Thrombosis and Haemostasis 85, № 01 (2001): 108–13. http://dx.doi.org/10.1055/s-0037-1612912.

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SummaryFibrinogen Matsumoto V (M-V) is a dysfibrinogen identified in a 52-year-old woman with systemic lupus erythematous. The triplet AGG encoding the amino acid residue Aα19 was replaced by GGG, resulting in the substitution of Arg→Gly. Residue Aα19 has been shown to be one of the most important amino acids in the so-called ‘A’ site or α-chain knob. The thrombin-catalyzed release of fibrinopeptide A from M-V fibrinogen was only slightly delayed yet release of fibrinopeptide B was significantly delayed. Both thrombin-catalyzed fibrin polymerization and fibrin monomer polymerization were marke

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11

Kubota, Kenji, Yoshiharu Toyama, Nobukazu Nameki, and Kaori Wakamatsu. "Desialylation of N-Linked Carbohydrate Chain of Fibrinogen." Key Engineering Materials 534 (January 2013): 241–46. http://dx.doi.org/10.4028/www.scientific.net/kem.534.241.

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Acceleration of fibrin polymerization occurs by the cleavage of sialic acids at the nonreducing terminal ends of N-linked carbohydrate chains as well as the cleavage of the entity of carbohydrate chains. In order to characterize and clarify the role of terminal sialic acid in the fibrin polymerization, mixing effects of desialylated fibrinogen with the intact one on the polymerization behavior were investigated by turbidity measurements in the course of polymerization. Marked accelerated fibrin polymerization was observed for the mixing of even a little amount of desialylated fibrinogen. Cleav

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12

Kamijo, Tomu, Takahiro Kaido, Masahiro Yoda, Shinpei Arai, Kazuyoshi Yamauchi та Nobuo Okumura. "Recombinant γY278H Fibrinogen Showed Normal Secretion from CHO Cells, but a Corresponding Heterozygous Patient Showed Hypofibrinogenemia". International Journal of Molecular Sciences 22, № 10 (2021): 5218. http://dx.doi.org/10.3390/ijms22105218.

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We identified a novel heterozygous hypofibrinogenemia, γY278H (Hiroshima). To demonstrate the cause of reduced plasma fibrinogen levels (functional level: 1.12 g/L and antigenic level: 1.16 g/L), we established γY278H fibrinogen-producing Chinese hamster ovary (CHO) cells. An enzyme-linked immunosorbent assay demonstrated that synthesis of γY278H fibrinogen inside CHO cells and secretion into the culture media were not reduced. Then, we established an additional five variant fibrinogen-producing CHO cell lines (γL276P, γT277P, γT277R, γA279D, and γY280C) and conducted further investigations. W

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13

DiOrio, J. P., K. R. Siebenlist, S. Terukina, K. Yamazumi, M. Matsuda та M. W. Mosesson. "The ultrastructure of fibrin prepared from fibrinogen ASAHI (γ 310 met→thr) and fibrinogen morioka (γ 275 arg→cys)". Proceedings, annual meeting, Electron Microscopy Society of America 50, № 2 (1992): 1090–91. http://dx.doi.org/10.1017/s0424820100130080.

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Fibrinogen is composed of three pairs of polypeptide chains, termed Aα, Bβ and γ, respectively, covalently linked at their amino termini by disulfide bonds. Fibrinogen is proteolytically activated to fibrin monomer by thrombin which cleaves two A (FPA) and two B (FPB) fibrinopeptides from the respective N-termini of Aα, Bβ chains, each exposing a different type of polymerization site [“A” or “B”]. Exposure of either site leads to fibrin monomer assembly to form two-stranded fibrils with subsequent lateral fibril association to a branched three-dimensional fiber network. Fibrinogen Asahi is a c

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14

Bantia, S., WR Bell, and CV Dang. "Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308- ---Ile mutation." Blood 75, no. 8 (1990): 1659–63. http://dx.doi.org/10.1182/blood.v75.8.1659.1659.

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Abstract Fibrinogen Baltimore III, a congenital abnormal fibrinogen with impaired fibrin monomer polymerization, displays a normal gamma-chain and a gamma-variant that has an apparently lower relative molecular weight (mol wt) than normal on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Reverse phase high-performance liquid chromatography (HPLC) analysis of the lysyl endopeptidase digest of the purified gamma-chains of fibrinogen Baltimore III revealed the presence of a peptide that is not found in the digest of the normal fibrinogen gamma-chain. Amino acid sequence ana

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15

Bantia, S., WR Bell, and CV Dang. "Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308- ---Ile mutation." Blood 75, no. 8 (1990): 1659–63. http://dx.doi.org/10.1182/blood.v75.8.1659.bloodjournal7581659.

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Fibrinogen Baltimore III, a congenital abnormal fibrinogen with impaired fibrin monomer polymerization, displays a normal gamma-chain and a gamma-variant that has an apparently lower relative molecular weight (mol wt) than normal on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Reverse phase high-performance liquid chromatography (HPLC) analysis of the lysyl endopeptidase digest of the purified gamma-chains of fibrinogen Baltimore III revealed the presence of a peptide that is not found in the digest of the normal fibrinogen gamma-chain. Amino acid sequence analysis of

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16

Bithell, T. C. "Hereditary dysfibrinogenemia." Clinical Chemistry 31, no. 4 (1985): 509–16. http://dx.doi.org/10.1093/clinchem/31.4.509.

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Abstract Inherited qualitative abnormalities of fibrinogen have been documented in more than 100 families. These dysfibrinogenemias usually are clinically silent, but in some cases are associated with bleeding, thrombosis, or defective wound healing. Abnormalities of the fibrinogen molecule may impair any of the major steps involved in the conversion of fibrinogen into stabilized fibrin; i.e., cleavage of the fibrinopeptides by thrombin, polymerization, and cross-linking of fibrin. Biochemical studies of several abnormal fibrinogens have demonstrated that the functional defects are the result

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17

Amri, Y., H. Jouini, M. Becheur, et al. "Fibrinogen Mahdia: A congenitally abnormal fibrinogen characterized by defective fibrin polymerization." Haemophilia 23, no. 4 (2017): e340-e347. http://dx.doi.org/10.1111/hae.13268.

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18

Reber, P., M. Furlan, A. Henschen та ін. "Three Abnormal Fibrinogen Variants with the Same Amino Acid Substitution (γ 275 Arg → His): Fibrinogens Bergamo II, Essen and Perugia". Thrombosis and Haemostasis 56, № 03 (1986): 401–6. http://dx.doi.org/10.1055/s-0038-1661691.

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SummaryWe report on three unrelated individuals with the same uncommon type of dysfibrinogenemia, originating from Bergamo, Essen and Perugia. None of them showed bleeding symptoms while the Bergamo patient and members of her family presented with a thrombotic tendency. The presence of a defective fibrinogen was suggested by prolonged thrombin and rep-tilase times. Furthermore, fibrinogen concentrations of less than 0.28 g/L were determined by the functional assay whereas values of 1.5-2.4 g/L were measured by heat precipitation or electroimmunoassay. Fibrinogen was isolated by affinity chroma

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19

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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20

Bantia, S., SM Mane, WR Bell, and CV Dang. "Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly----Val (GGC----GTC) mutation." Blood 76, no. 11 (1990): 2279–83. http://dx.doi.org/10.1182/blood.v76.11.2279.2279.

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Abstract Fibrinogen Baltimore I is one of the very first congenital abnormal fibrinogens reported over several decades ago; however, the molecular defect of this dysfibrinogen has eluded identification. In fact, several reports misidentified the functional defect of Baltimore I, which has impaired fibrin monomer polymerization. Reversed-phase high- performance liquid chromatography analysis of lysyl endopeptidase digest of the purified Baltimore I gamma-chain showed an abnormal peptide not found in the co-existing normal gamma-chain of this heterozygote. Amino acid sequencing of this peptide i

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21

Bantia, S., SM Mane, WR Bell, and CV Dang. "Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly----Val (GGC----GTC) mutation." Blood 76, no. 11 (1990): 2279–83. http://dx.doi.org/10.1182/blood.v76.11.2279.bloodjournal76112279.

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Fibrinogen Baltimore I is one of the very first congenital abnormal fibrinogens reported over several decades ago; however, the molecular defect of this dysfibrinogen has eluded identification. In fact, several reports misidentified the functional defect of Baltimore I, which has impaired fibrin monomer polymerization. Reversed-phase high- performance liquid chromatography analysis of lysyl endopeptidase digest of the purified Baltimore I gamma-chain showed an abnormal peptide not found in the co-existing normal gamma-chain of this heterozygote. Amino acid sequencing of this peptide indicated

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22

Steinmann, C., C. Bogli, M. Jungo, et al. "A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization." Blood 84, no. 6 (1994): 1874–80. http://dx.doi.org/10.1182/blood.v84.6.1874.1874.

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Abstract Fibrinogen Milano VII is a hereditary fibrinogen variant detected in a woman with no clinical symptoms of bleeding or thrombosis. Thrombin and reptilase clotting times were prolonged in six family members from three generations. Release of fibrinopeptides A and B was normal. Fibrin polymerization was strongly delayed both in the presence and in the absence of calcium. The structural defect was determined by sequence analysis of a 290-bp fragment of genomic DNA amplified by polymerase chain reaction and cloned in M13mp19. The triplet TCT coding for the amino acid residue gamma 358 was

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23

Steinmann, C., C. Bogli, M. Jungo, et al. "A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization." Blood 84, no. 6 (1994): 1874–80. http://dx.doi.org/10.1182/blood.v84.6.1874.bloodjournal8461874.

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Fibrinogen Milano VII is a hereditary fibrinogen variant detected in a woman with no clinical symptoms of bleeding or thrombosis. Thrombin and reptilase clotting times were prolonged in six family members from three generations. Release of fibrinopeptides A and B was normal. Fibrin polymerization was strongly delayed both in the presence and in the absence of calcium. The structural defect was determined by sequence analysis of a 290-bp fragment of genomic DNA amplified by polymerase chain reaction and cloned in M13mp19. The triplet TCT coding for the amino acid residue gamma 358 was found to

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24

Franke, Kathrin, Walter Richter, Frank Steiniger та ін. "New molecular defects in the γ subdomain of fibrinogen D-domain in four cases of (hypo)dysfibrinogenemia: fibrinogen variants Hannover VI, Homburg VII, Stuttgart and Suhl". Thrombosis and Haemostasis 89, № 04 (2003): 637–46. http://dx.doi.org/10.1055/s-0037-1613585.

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SummaryFour new molecular abnormalities in the γ subdomain of the D domain elucidated in three unrelated thrombophilic patients and in one asymptomatic case of hypofibrinogenemia are reported: fibrinogen Suhl, γ 326,Cys →Tyr, fibrinogen Hannover VI, γ 336 Met →Ile, fibrinogen Stuttgart, γ 345, Asn→Asp and fibrinogen Homburg VII, γ354,Tyr→Cys. In all cases, fibrin polymerization in plasma is impaired. In the case of fibrinogen Suhl, there was a normalization of fibrin polymerization in plasma at higher Ca2+ concentration. The protective effect of Ca2+ on plasmic degradation of fibrinogen was in

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25

Nakayama-Hamada, M., A. Suzuki, H. Furukawa, R. Yamada, and K. Yamamoto. "Citrullinated Fibrinogen Inhibits Thrombin-catalysed Fibrin Polymerization." Journal of Biochemistry 144, no. 3 (2008): 393–98. http://dx.doi.org/10.1093/jb/mvn079.

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26

Popescu, Alina L., Kathryn K. Gersh, Dan Safer, and John W. Weisel. "Single Molecule TIRF Study of Fibrinogen Polymerization." Biophysical Journal 100, no. 3 (2011): 153a. http://dx.doi.org/10.1016/j.bpj.2010.12.1049.

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27

Kubota, Kenji, Yoshiharu Toyama, Nobukazu Nameki, and Kaori Wakamatsu. "Effect of Deglycosylation on the Fibrin Polymerization Depending on NaCl Concentration." Key Engineering Materials 596 (December 2013): 213–18. http://dx.doi.org/10.4028/www.scientific.net/kem.596.213.

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Cleavage of carbohydrate chains linked to fibrinogen molecule results in an acceleration of fibrin polymerization, fibrin gel formation, by promoting the lateral aggregation of protofibrils. Sialic acid at the unreduced terminus of carbohydrate chain plays an essentially important role in the lateral aggre-gation. Fibrin polymerization is significantly affected by the solvent condition, e.g., pH and ionic strength. Terminal sialic acid are supposed to interact with amino terminal region of Bβ chain, in which there are many basic amino acid residues, and thus such interactions are expected to b

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28

Wang, Lei, Rui Li, Lianzhi Li, Huaisheng Wang, and Jifeng Liu. "Study on the interaction between Fe3+and fibrinogen and its influence on the polymerization behavior of fibrin networks." RSC Advances 6, no. 79 (2016): 75207–14. http://dx.doi.org/10.1039/c6ra17661e.

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The interactions between fibrinogen molecule and Fe<sup>3+</sup>were studied and applied to explicate the polymerization behavior of fibrinogen mediated with Fe<sup>3+</sup>. Overloading Fe<sup>3+</sup>in the fibrinogen solution will accelerate the amorphous aggregation of fibrin.

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29

Lulla, Premal, Swapan Dasgupta, Lawrence Rice, John J. McCarthy та Perumal Thiagarajan. "Characterization Of An Acquired IgG Autoantibody To Bβ and γ Chains Of Fibrinogen Resulting In Delayed Fibrin Polymerization and Severe Bleeding". Blood 122, № 21 (2013): 2362. http://dx.doi.org/10.1182/blood.v122.21.2362.2362.

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Abstract A 88 year-old woman was referred to our center for 3 weeks of gastrointestinal bleeding and a spontaneous right rectus femoris hematoma. The prothrombin time (PT), activated partial thromboplastin time (aPTT), thrombin time (TT) and reptilase time (RT) were markedly prolonged (Table 1). Assays for coagulation factors V, VIII, IX and X were normal. A fibrinogen concentration of < 50 mg/dl was measured by Clauss method while fibrinogen concentration measured by radial immunodiffusion was 180 mg/dl. Following infusions of cryoprecipitate there was accelerated clearance of fibrinogen a

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30

Ponczek, Michał, Michał Bijak, Joanna Saluk, Joanna Kolodziejczyk-Czepas, and Paweł Nowak. "The comparison of peroxynitrite action on bovine, porcine and human fibrinogens." Open Life Sciences 9, no. 3 (2014): 233–41. http://dx.doi.org/10.2478/s11535-013-0259-9.

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AbstractSubjects of bovine and porcine flocks are sometimes susceptible to death before time of slaughter, and some of those deaths may be due to cardiovascular problems connected with stress. The role of oxidative stress in farm animals is yet unexplored. Human fibrinogen seems to be highly susceptible to nitration. Peroxynitrite produced from superoxide and nitric oxide initiates noticeable changes in the structure of human fibrinogen molecule. The objective of this work is to compare the in vitro interactions of peroxynitrite with human fibrinogen and with fibrinogen from mammals of great e

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31

Nellenbach, Kimberly A., Nina A. Guzzetta, and Ashley C. Brown. "Differential Sialic Acid Content in Adult and Neonatal Fibrinogen Mediate Differences in Clot Polymerization." Blood 136, Supplement 1 (2020): 21–22. http://dx.doi.org/10.1182/blood-2020-139965.

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Recent studies have identified several major qualitative and quantitative differences in important hemostatic proteins between adult and neonatal humans, including the primary coagulation protein fibrinogen.Despite these differences, neonates with post-operative bleeding from procedures requiring cardiopulmonary bypass (CPB) or extracorporeal membrane oxygenation (ECMO) are treated with transfusions of adult blood products, namely adult fibrinogen. The effectiveness of such transfusions is inconsistent in neonates and often results in a deficient fibrin matrix structure which may not be suffic

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32

Kaido, Takahiro, Masahiro Yoda, Tomu Kamijo та ін. "A Novel Amino Acid Substitution, Fibrinogen Bβp.Pro234Leu, Associated with Hypofibrinogenemia Causing Impairment of Fibrinogen Assembly and Secretion". International Journal of Molecular Sciences 21, № 24 (2020): 9422. http://dx.doi.org/10.3390/ijms21249422.

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We identified a novel heterozygous variant, Bβp.Pro234Leu (fibrinogen Tokorozawa), which was suspected to be associated with hypofibrinogenemia. Therefore, we analyzed the assembly and secretion of this fibrinogen using Chinese hamster ovary (CHO) cells. To determine the impact on the synthesis and secretion of fibrinogen of the Bβp.P234L and γp.G242E substitutions, we established recombinant variant fibrinogen-producing CHO cell lines. Synthesis and secretion analyses were performed using an enzyme-linked immunosorbent assay (ELISA) and immunoblotting analysis with the established cell lines.

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33

Lounes, Karim Chabane, Claudine Soria, Antoine Valognes, Marie France Turchini, Jaap Koopman та Jeannette Soria. "Fibrinogen Bastia (γ 318 Asp → Tyr) a Novel Abnormal Fibrinogen Characterized by Defective Fibrin Polymerization". Thrombosis and Haemostasis 82, № 12 (1999): 1639–43. http://dx.doi.org/10.1055/s-0037-1614892.

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SummaryA new congenital dysfibrinogen, Fibrinogen Bastia, was discovered in a 20-year-old woman with no clinical symptoms. The plasma thrombin-clotting time was severely prolonged. The functional plasma fibrinogen concentration was low (0.2 mg/ml), whereas the immunological concentration was normal (2.9 mg/ml). Purified fibrinogen Bastia displayed a markedly prolonged thrombin-clotting time related to a delayed thrombin-induced fibrin polymerization. Both the thrombin-clotting time and the fibrin polymerization were partially corrected by the addition of calcium ions. The anomaly of fibrinogen

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34

Kamiguti, Aura S., Joseph R. Slupsky, Mirko Zuzel, and Charles R. M. Hay. "Properties of Fibrinogen Cleaved by Jararhagin, a Metalloproteinase from the Venom of Bothrops jararaca." Thrombosis and Haemostasis 72, no. 02 (1994): 244–49. http://dx.doi.org/10.1055/s-0038-1648847.

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SummaryHaemorrhagic metalloproteinases from Bothrops jararaca and other venoms degrade vessel-wall and plasma proteins involved in platelet plug and fibrin clot formation. These enzymes also cause proteolytic digestion of fibrinogen which has been suggested to cause defective platelet function. Fibrinogen degradation by jararhagin, a metalloproteinase from B. jararaca, and the effect of jararhagin fibrinogenolysis on both platelet aggregation and fibrin clot formation were investigated. Jararhagin was found to cleave human fibrinogen in the C-terminal region of the Aα-chain giving rise to a 28

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35

Siebenlist, K. R., M. W. Mosesson, J. P. Diorio, S. Tavori, I. Tatarsky та A. Rimon. "The Ultrastructure of Fibrin Prepared from Fibrinogen Haifa (γ275 Arg→His)". Proceedings, annual meeting, Electron Microscopy Society of America 46 (1988): 248–49. http://dx.doi.org/10.1017/s0424820100103309.

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Fibrinogen is composed of six polypeptide chains, 2 Aα, 2 Bβ and 2 γ chains, covalently linked at their amino termini by disulfide bonds. Fibrinogen is activated to α,β-fibrin by thrombin which cleaves 2 A (FPA) and 2B (FPB) fibrinopeptides from the N-termini. Release of FPA and FPB exposes'A'and'B' polymerization sites, respectively. The resulting fibrin self-associates into a branched 3-dimensional matrix. Two other types of fibrin can be formed in vitro: ct-fibrin [FPA release]and β-fibrin [FPB reelease). Fibrinogen Haifa is a congenital abnormal fibrinogen variant characterized by normal f

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Gersh, Kathryn C., та Susan T. Lord. "An Investigation of Factor XIII Binding to Recombinant γ′/γ′ and γ/γ′ Fibrinogen." Blood 108, № 11 (2006): 1705. http://dx.doi.org/10.1182/blood.v108.11.1705.1705.

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Abstract Increased levels of the alternatively spliced γ′ chain of fibrinogen have been measured in patients suffering from coronary artery disease (Lovely et al. Thromb. Haemost.2002;88:26–31). Others have suggested that the γ′ chain serves as a binding site for factor XIII (Siebenlist et al. Biochemistry1996;35:10448–10453), thus increasing the amount of cross-linking and therefore the stability of the γ′-containing clots (Falls and Farrell JBC1997;272:14251–14256). We have expressed recombinant γ′/γ′ homodimer and γ/γ′ heterodimer fibrinogen variants in CHO cells and characterized their pol

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Lounes, Karim C., Jerry B. Lefkowitz, Agnes H. Henschen-Edman, Andrew I. Coates, Roy R. Hantgan та Susan T. Lord. "The impaired polymerization of fibrinogen Longmont (Bβ166Arg→Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers". Blood 98, № 3 (2001): 661–66. http://dx.doi.org/10.1182/blood.v98.3.661.

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Abstract This study identified a new substitution in the Bβ chain of an abnormal fibrinogen, denoted Longmont, where the residue Arg166 was changed to Cys. The variant was discovered in a young woman with an episode of severe hemorrhage at childbirth and a subsequent mild bleeding disorder. The neo-Cys residues were always found to be disulfide-bridged to either an isolated Cys amino acid or to the corresponding Cys residue of another abnormal fibrinogen molecule, forming dimers. Removing the dimeric molecules using gel filtration did not correct the fibrin polymerization defect. Fibrinogen Lo

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38

Wang, Lei, Lianzhi Li, Huaisheng Wang, and Jifeng Liu. "Study on the influence of oxidative stress on the fibrillization of fibrinogen." Biochemical Journal 473, no. 23 (2016): 4373–84. http://dx.doi.org/10.1042/bcj20160702.

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Human fibrinogen is an important coagulation factor as well as an independent predictor of coronary heart disease and stroke. Analysis of dysfibrinogens may provide useful information and help us to understand the molecular defects in fibrin polymerization. In the present study, we investigated the influence of oxidative stress of fibrinogen induced by H2O2 on the polymerization state of fibrin. UV absorbance spectroscopy, circular dichroism, ζ-potential, dynamic light scattering and steady shear viscosity were all employed to study the influence of oxidative stress on the molecular structure,

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de Vries, Judith J., Charlotte J. M. Snoek, Dingeman C. Rijken, and Moniek P. M. de Maat. "Effects of Post-Translational Modifications of Fibrinogen on Clot Formation, Clot Structure, and Fibrinolysis." Arteriosclerosis, Thrombosis, and Vascular Biology 40, no. 3 (2020): 554–69. http://dx.doi.org/10.1161/atvbaha.119.313626.

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Objective: Post-translational modifications of fibrinogen influence the occurrence and progression of thrombotic diseases. In this systematic review, we assessed the current literature on post-translational modifications of fibrinogen and their effects on fibrin formation and clot characteristics. Approach and Results: A systematic search of Medline, Embase, Cochrane Library, and Web of Science was performed to find studies reporting post-translational modifications of fibrinogen and the effects on clot formation and structure. Both in vitro studies and ex vivo studies using patient material w

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Stucki, Bettina, Peter Schmutz, Luzius Schmid, André Haeberli, Bernhard Lämmle та Miha Furlan. "Fibrinogen St. Gallen I (γ 292 Gly → Val): Evidence for Structural Alterations Causing Defective Polymerization and Fibrinogenolysis". Thrombosis and Haemostasis 81, № 02 (1999): 268–74. http://dx.doi.org/10.1055/s-0037-1614456.

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SummaryFibrinogen St. Gallen I was detected in an asymptomatic Swiss woman. Routine coagulation tests revealed a prolonged thrombin and reptilase time. Functionally measured fibrinogen levels were considerably lower than those determined immunologically. Polymerization of fibrin monomers derived from purified fibrinogen was delayed in the presence of either calcium or EDTA. Normal fibrinopeptide A and B release by thrombin was established. An abnormal degradation of fibrinogen St. Gallen I by plasmin was observed. Fragment D1 of normal fibrinogen was fully protected against further proteolysis

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Palacio, Luis A., Christopher B. Stanley, Lucas Burke, Ryan Lybarger, and Horia I. Petrache. "Small Angle Neutron Scattering of Fibrinogen Polymerization Kinetics." Biophysical Journal 110, no. 3 (2016): 385a. http://dx.doi.org/10.1016/j.bpj.2015.11.2081.

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Preissner, Klaus T., Jürgen Rötker, Eberhard Selmayr, Hugo Fasold, and Gert Müller-Berghaus. "Influence of fibrinogen on fibrin polymerization. Ultracentrifugation studies." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 829, no. 3 (1985): 358–64. http://dx.doi.org/10.1016/0167-4838(85)90245-6.

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Blombäck, Birger. "Fibrinogen structure, activation, polymerization and fibrin gel structure." Thrombosis Research 75, no. 3 (1994): 327–28. http://dx.doi.org/10.1016/0049-3848(94)90245-3.

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Okumura, Nobuo, Kenichi Furihata, Fumiko Terasawa, Ritsuko Nakagoshi, Ichiro Ueno та Tsutomu Katsuyama. "Fibrinogen Matsumoto I: A γ364 Asp → His (GAT→CAT) Substitution Associated with Defective Fibrin Polymerization". Thrombosis and Haemostasis 75, № 06 (1996): 887–91. http://dx.doi.org/10.1055/s-0038-1650389.

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SummaryFibrinogen Matsumoto I is a novel hereditary dysfibrinogen identified in a 1-year-old boy with Down’s syndrome. Though he showed no apparent bleeding or thrombotic tendency, he had a congenital heart disease. Preoperative coagulation tests of his plasma revealed a prolonged thrombin time and the fibrinogen level determined by the thrombin time method was markedly decreased. Molecular weight of fibrinogen chains showed apparently normal Aα, Bβ-, and γ-chains. The rate of fibrinopeptide release was normal, whereas fibrin polymerization was delayed. Fibrinogen γ-chain gene fragments from t

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Reber, P., M. Furlan, C. Rupp, et al. "Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp----Val impairs fibrin polymerization." Blood 67, no. 6 (1986): 1751–56. http://dx.doi.org/10.1182/blood.v67.6.1751.1751.

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Abstract An abnormal fibrinogen was found in two asymptomatic members (father and daughter) of the same family, originating from northern Italy. Routine coagulation studies revealed prolonged thrombin and reptilase clotting times. Plasma fibrinogen levels, as determined by a functional assay, were markedly diminished, whereas the heat precipitation method indicated normal fibrinogen values. On the basis of these findings, a tentative diagnosis of dysfibrinogenemia was made, and according to the accepted nomenclature, this fibrinogen variant was called “fibrinogen Milano l.” The time course of

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46

Reber, P., M. Furlan, C. Rupp, et al. "Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp----Val impairs fibrin polymerization." Blood 67, no. 6 (1986): 1751–56. http://dx.doi.org/10.1182/blood.v67.6.1751.bloodjournal6761751.

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An abnormal fibrinogen was found in two asymptomatic members (father and daughter) of the same family, originating from northern Italy. Routine coagulation studies revealed prolonged thrombin and reptilase clotting times. Plasma fibrinogen levels, as determined by a functional assay, were markedly diminished, whereas the heat precipitation method indicated normal fibrinogen values. On the basis of these findings, a tentative diagnosis of dysfibrinogenemia was made, and according to the accepted nomenclature, this fibrinogen variant was called “fibrinogen Milano l.” The time course of fibrinope

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Zhou, Jingyi, Qiulan Ding, Wenman Wu та ін. "Dysfibrinogenemia-associated novel heterozygous mutation, Shanghai (FGA c.169_180+2 del), leads to N-terminal truncation of fibrinogen Aα chain and impairs fibrin polymerization". Journal of Clinical Pathology 70, № 2 (2016): 145–53. http://dx.doi.org/10.1136/jclinpath-2016-203862.

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AimsA novel heterozygous variant, FGA c.169_180+2 del (designated fibrinogen Shanghai), was identified in a patient with dysfibrinogenemia with antiphospholipid antibody syndrome (APS) and recurrent venous thrombosis, and in his asymptomatic father. We aimed to reveal the functional implication of structural change caused by this variant.MethodsTranscription analysis was performed with FGA minigene transfection assay to evaluate the impact of nucleosides deletion on mRNA editing. The fibrinogen isolated from propositus' plasma was used to characterise its functional defects. Fibrin polymerizat

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Luzak, Boguslawa, Magdalena Boncler, Marcin Kosmalski, et al. "Fibrinogen Glycation and Presence of Glucose Impair Fibrin Polymerization—An In Vitro Study of Isolated Fibrinogen and Plasma from Patients with Diabetes Mellitus." Biomolecules 10, no. 6 (2020): 877. http://dx.doi.org/10.3390/biom10060877.

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Background: Fibrin formation and structure may be affected by a plethora of factors, including both genetic and posttranslational modifications, such as glycation, nitration or acetylation. Methods: The present study examines the effect of fibrinogen glycation on fibrin polymerization, measured in fibrinogen concentration-standardized plasma of subjects with type 2 diabetes mellitus (T2DM) and in a solution of human fibrinogen exposed to 30 mM glucose for four days. Results: The fibrin polymerization velocity (Vmax) observed in the T2DM plasma (median 0.0056; IQR 0.0049‒0.0061 AU/s) was signif

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Zamarron, Concepcion, Mark H. Ginsberg, and Edward F. Plow. "Monoclonal Antibodies Specific for a Conformationally Altered State of Fibrinogen." Thrombosis and Haemostasis 64, no. 01 (1990): 041–46. http://dx.doi.org/10.1055/s-0038-1647251.

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SummaryFour monoclonal antibodies were selected by their ability to discriminate surface-bound from soluble fibrinogen. These antibodies reacted with insolubilized fibrinogen but not other immobilized proteins and their reaction with surface-bound fibrinogen was not diminished by a 100-fold excess of sotuble fibrinogen. The antibodies reacted with the same or spatially proximal epitopes, and the recognized epitope(s) resided within the gamma chain segment of the D domain of fibrinogen. Fab fragments of the antibodies inhibited fibrin polymerization in a dose dependent manner, suggesting that t

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Homer, V. M., J. L. Mullin, S. O. Brennan, A. Barr та P. M. George. "Novel Aα chain truncation (fibrinogen Perth) resulting in low expression and impaired fibrinogen polymerization". Journal of Thrombosis and Haemostasis 1, № 6 (2003): 1245–50. http://dx.doi.org/10.1046/j.1538-7836.2003.00224.x.

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