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Journal articles on the topic 'Fibin'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Lakner, Johannes, Christian Seyer, Thomas Hermsdorf, and Torsten Schöneberg. "Characterization of the expression, promoter activity and molecular architecture of fibin." BMC Biochemistry 12, no. 1 (2011): 26. http://dx.doi.org/10.1186/1471-2091-12-26.

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2

Lee, Hyunjung, Young In Kim, Farida S. Nirmala, Ji-Sun Kim, Hyo-Deok Seo, Tae Youl Ha, Young-Jin Jang, Chang Hwa Jung, and Jiyun Ahn. "MiR-141-3p promotes mitochondrial dysfunction in ovariectomy-induced sarcopenia via targeting Fkbp5 and Fibin." Aging 13, no. 4 (February 3, 2021): 4881–94. http://dx.doi.org/10.18632/aging.202617.

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3

Wakahara, Takashi, Naoki Kusu, Hajime Yamauchi, Ikuo Kimura, Morichika Konishi, Ayumi Miyake, and Nobuyuki Itoh. "fibin, a novel secreted lateral plate mesoderm signal, is essential for pectoral fin bud initiation in zebrafish." Developmental Biology 303, no. 2 (March 2007): 527–35. http://dx.doi.org/10.1016/j.ydbio.2006.11.041.

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4

Weisel, John W., Tatiana Lebedeva, Chandrasekaran Nagaswami, Vincent M. Hayes, Walter Massefski, Rustem I. Litvinov, Lubica Rauova, Thomas J. Lowery, and Douglas B. Cines. "Polyhedrocytes: Compressed Polyhedral Erythrocytes In Contracted Blood Clots and Thrombi." Blood 122, no. 21 (November 15, 2013): 452. http://dx.doi.org/10.1182/blood.v122.21.452.452.

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Background Contraction of blood clots is necessary for hemostasis, wound healing and to restore flow past obstructive thrombi. However, little has been known about the structure of contracted clots and mechanisms of contraction. Erythrocytes, biconcave cells that are highly deformable to allow their passage through the microvasculature, are abundant in venous thrombi, and to a lesser extent in arterial thrombi. Erythrocytes promote hemostasis, but their participation in clot contraction has not been reported. Here we study the mechanisms of clot contraction and the roles of erythrocytes, platelets and fibrin, and show that erythrocyte shape change into compressed polyhedrocytes allows tight packing consistent with the major function of clots to stem bleeding. Methods Whole blood was clotted by recalcification and addition of thrombin or kaolin, while following the process of clotting, including contraction, with a new technique using T2 magnetic resonance. We examined the structure and composition of contracted whole blood clots by scanning electron microscopy and confocal light microscopy. Results Contracted clots display a remarkable structure, with a close-packed, tessellated array (or mosaic tiling of space) of compressed polyhedral erythrocytes (called polyhedrocytes) on the interior and a meshwork of fibrin and platelet aggregates on the exterior. Little fibin and few platelets were found on the interior of the contracted clots. The same results were obtained with both thrombin and kaolin as activators of clotting and also with reconstituted human blood and clots prepared from mouse blood. Confocal microscopy of hydrated clots confirms the results of scanning electron microscopy. The mechanical nature of this shape change was confirmed by polyhedrocyte formation from the forces of centrifugation of blood without clotting. Platelets (with their cytoskeletal motility proteins) and fibrin(ogen) (as the substrate bridging platelets for contraction) are required to generate the forces necessary to segregate platelets/fibrin from erythrocytes and to compress erythrocytes into a closely packed polyhedral array. To assess the density of packing of the polyhedral erythrocytes, we replaced the water surrounding the clots with D2O and observed by T2 magnetic resonance that hydrogen/deuterium exchange for the contracted clots was very slow, consistent with their very tightly packed, almost impermeable structure. The same polyhedrocyte structures were observed from in vivo thrombi aspirated by cardiologists from the coronary arteries of ST-elevation myocardial infarction patients. Summary/Conclusions We have observed a previously undiscovered, naturally occurring erythrocyte function and morphology, closely packed polyhedra, in contracted clots and thrombi, and an unexpected spatial redistribution of platelets and fibrin that occurs during contraction. Clot contraction is an essential part of hemostasis, since both human genetic disorders of platelet myosin IIA and megakaryocyte myosin IIA-knock out mice show a bleeding phenotype. These observations on contracted clots imply that they are stiff, rigid structures that can form an impermeable, watertight seal. On the one hand, contraction of clots within the vasculature may relieve obstruction of blood vessels and allow recanalization, especially in the venous system. On the other hand, these results account for long-standing clinical observations that fibrinolysis is greatly prolonged following clot contraction, since perfusion or diffusion of lytic enzymes into these tightly packed polyhedral erythrocytes would be nearly impossible. These results suggest a vital role for erythrocytes and clot contraction in hemostasis and wound healing. Disclosures: No relevant conflicts of interest to declare.

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5

Tutwiler, Valerie, Alina D. Peshkova, Giang Le Minh, Sergei Zaitsev, Rustem I. Litvinov, Douglas B. Cines, and John W. Weisel. "Fibrinolysis of Contracted Blood Clots Depends on Whether Plasminogen Activator Acts from inside or Outside." Blood 132, Supplement 1 (November 29, 2018): 3773. http://dx.doi.org/10.1182/blood-2018-99-119659.

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Abstract Fibrinolysis involves the dissolution of polymeric fibrin networks that is required to restore blood flow through vessels obstructed by clots and thrombi. The efficiency of lysis depends on the susceptibility of fibrin to enzymatic digestion, which is governed by the structure and spatial organization of fibrin fibers as well as porosity and composition of the clot. Platelet-driven clot contraction results in compaction of the erythrocytes into the core of the clot, effectively reducing the permeability of the clot, and influences fibrin network structure. We have shown that clot contraction is reduced in blood from patients with thrombotic conditions such ischemic stroke and deep vein thrombosis, which points to the clinical importance of understanding the influence of clot contraction on efficacy of fibrinolysis. Here, we examined the effects of clot contraction on the rate of internal fibrinolysis emanating from within the clot to simulate (patho)physiological conditions, and external fibrinolysis initiated from the clot exterior to simulate therapeutic thrombolysis. Fibrinolysis was induced and the kinetics of lysis was measured in parallel in contracted versus uncontracted clots from the same citrated human blood samples. Clot formation and platelet activation were initiated with 1 U/ml thrombin and 2 mM CaCl2. Clot contraction was either unaffected or impaired by inhibiting platelet non-muscle myosin IIa (blebbistatin), actin polymerization (latrunculin A), and platelet-fibin(ogen) binding (abciximab). To examine internal fibrinolysis, 75 ng/ml of human recombinant tissue plasminogen activator (tPA) was added prior to initiation of clotting, allowing for tPA to be uniformly distributed through the clot volume and for fibrinolysis occur after the clot has formed. We used optical tracking to follow clot size in a time dependent manner. Contracted clots were completely lysed at a rate that was at least 2 times faster than clots with impaired contraction. Specifically, the average time to complete lysis was 33±4 minutes for contracted clots versus 59±3, 84±4, 75±3 minutes when contraction was impaired by blebbistatin, latrunculin A, and abciximab, respectively (p<0.001). To examine external fibrinolysis, blood spiked with purified human 125I-fibrinogen was allowed to clot and contract (unless contraction was inhibited) prior to the addition of 75 ng/ml tPA. Clots with impaired contraction released 2-4-fold more radiolabeled soluble degradation products during the first 30 minutes and continued to lyse at a rate 4-fold faster than contracted clots over the initial 4 hours following addition of tPA. This reduction of the fibrinolysis rate in contracted clots was not due to the expulsion of serum-soluble anti-fibrinolytic compounds during the contraction process because serum replacement with a buffer did not affect the lysis rate. This difference in the susceptibility of contracted and uncontracted clots to internal versus external lysis suggests that the lysis rate is dominated by the interplay of clot permeability to fibrinolytic enzymes and the spatial proximity of the fibrin fibers themselves. Despite limitations of in vitro experimental models, numerous studies on fibrinolysis have demonstrated the relevance of experimental findings to pathophysiological fibrinolysis and therapeutic thrombolysis. Enhancement of fibrinolysis in contracted blood clots is consistent with the need to dissolve mature clots once they have performed their hemostatic function in a vessel on in a wound. The reduced rates of dissolution of contracted clots in our model of externally applied tPA could account for the inefficacy of therapeutic thrombolysis of old thrombi that likely underwent more compaction compared to newer thrombi. Our studies point to the clinical importance of understanding how mechanical remodeling of clots and thrombi may influence their fibrinolytic resolution and could inform the development of improved thrombolytic therapies. This work, in part, was supported by the Program for Competitive Growth at KFU. Disclosures No relevant conflicts of interest to declare.

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6

Pokharel, Nitesh R., Anil Dev Pant, Raghavendra Rao, and Surakchya Koirala. "A study of clinical and Immunofluorescence spectrum of Immunobullous diseases." Asian Journal of Medical Sciences 12, no. 7 (July 1, 2021): 117–21. http://dx.doi.org/10.3126/ajms.v12i7.36893.

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Background: Immunobullous disorders are a group of disorders involving the formation of a fluid filled cavity within or beneath the epidermis, due to the presence of autoantibodies against adhesion molecules in epidermis and dermis. Accurate diagnosis of these disorders requires clinicopathological correlation along with immunofluorescence study. Aims and Objectives: This study was undertaken to describe the clinical features of immunobullous disorders and to analyse the utility of Direct immunofluorescence (DIF) in the diagnosis of these disorders. Materials and Methods: A total of 42 Patients attending skin OPD between February 2014 and March 2017 who had a provisional diagnosis of immunobullous disease were enrolled in the study. Detailed clinical examination and DIF study were done in all cases. Results: Out of 42 cases studied, 31 were diagnosed as pemphigus vulgaris (PV) and 11 as bullous pemphigoid (BP) that was confirmed by DIF. There were 20 (46.61%) male patients and 22 (52.38%) female patients in the age group of 18 to 81 years with a mean age of 52.64 years. A slightly female preponderance was observed. Mean age of presentation of PV patients is 50.83 years with age group range was between 18 to 77 years. Majority of patients presented at 4th and 5th decade of life. Age group range for BP was between 34 to 81years with mean age of presentation being 57.72 years. Majority of our patients presented at 5th decade or later. DIF was positive in all 42 cases (100%) of immunobullous disease. DIF in all 31 cases of PV showed 100% IgG deposition in intercellular substance (ICS) and 64.51% C3 deposition in ICS. BP showed 100% C3 deposition in all 11 cases, 63.63% IgG in seven of the eleven,18.18% IgA in two and 9% IgM, fibin in one each as a linear band at basement membrane zone (BMZ). Conclusion: Both the clinical findings and the Imunofluorescence features are important in arriving at a definite diagnosis in immunobullous diseases. In all the cases DIF was absolutely essential tool to come to a final diagnosis.

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7

Avinash, Shashant, Gaurav Malhotra, Pradeep Shukla, and Prerna Kataria. "Autologous platelet rich fibrin." Asian Pacific Journal of Health Sciences 5, no. 3 (July 2018): 1–10. http://dx.doi.org/10.21276/apjhs.2018.5.3.1.

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8

Lugovska, N. E., I. M. Kolesnikova, Ye M. Stohnii, V. O. Chernyshenko, A. V. Rebriev, O. P. Kostiuchenko, G. K. Gogolinska, et al. "Novel monoclonal antibody to fibrin(ogen) ?C-region for detection of the earliest forms of soluble fibrin." Ukrainian Biochemical Journal 92, no. 3 (August 13, 2020): 58–70. http://dx.doi.org/10.15407/ubj92.03.058.

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9

Pozniak, T. A., L. P. Urvant, and P. G. Gritsenko. "Inhibition of fibrin polymerization by synthetic peptides corresponding to Аα195-205 and γ69-77 sites sites of fibrin molecule." Ukrainian Biochemical Journal 86, no. 04 (August 27, 2014): 119–25. http://dx.doi.org/10.15407/ubj86.04.119.

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10

DURMUŞ, Ali Said, and Havva Nur CAN. "Platelet-Rich Fibrin and Its Usage in Orthopaedic Surgery: Review." Turkiye Klinikleri Journal of Veterinary Sciences 7, no. 1 (2016): 24–29. http://dx.doi.org/10.5336/vetsci.2016-51892.

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11

Horan, John T., and Charles W. Francis. "Fibrin Degradation Products, Fibrin Monomer and Soluble Fibrin in Disseminated Intravascular Coagulation." Seminars in Thrombosis and Hemostasis 27, no. 06 (2001): 657–66. http://dx.doi.org/10.1055/s-2001-18870.

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12

Litvinov, Rustem I., and John W. Weisel. "Not fibrin(ogen), but fibrinogen or fibrin." Blood 126, no. 17 (October 22, 2015): 1977–78. http://dx.doi.org/10.1182/blood-2015-08-662551.

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13

Kui, Róbert, Judit Vasas, Győző Szolnoki, and Lajos Kemény. "Successful treatment of venous leg ulcer with platelet-rich fibrin." Bőrgyógyászati és Venerológiai Szemle 96, no. 6 (November 16, 2020): 303–6. http://dx.doi.org/10.7188/bvsz.2020.96.6.1.

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The autologous platelet-rich blood derivatives have been used in bioregenerative medicine for decades in various indications including the facilitation of wound healing. Leukocyte- and platelet-rich fibrin (PRF) is a second-generation autologous blood-derived product, which can be obtained relatively easily and at low cost. PRF is rich in growth factors and antimicrobial proteins that are released by activated platelets and leukocytes. The authors present a successful treatment of a venous leg ulcer providing a detailed presentation of the PRF method.

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14

Yatsenko, T. A., V. М. Rybachuk, O. I. Yusova, S. M. Kharchenko, and T. V. Grinenko. "Effect of fibrin degradation products on fibrinolytic process." Ukrainian Biochemical Journal 88, no. 2 (April 25, 2016): 16–24. http://dx.doi.org/10.15407/ubj88.02.016.

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15

Peker, Kemal. "Endoscopic treatment of anastomotic leakage with fibrin glue." Dicle Medical Journal/Dicle Tıp Dergisi 40, no. 3 (September 1, 2013): 490–91. http://dx.doi.org/10.5798/diclemedj.0921.2013.03.0317.

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16

ÖZTÜRK, Perihan, Mehmet Enes GÜNER, Hülya NAZİK, Mine Müjde KUŞ, Mehmet Kamil MÜLAYİM, and Mehmet BEKERECİOĞLU. "Is Platalet-Rich Fibrin Effect in Pyoderma Gangrenosum Ulcers?" Turkiye Klinikleri Journal of Dermatology 31, no. 1 (2021): 53–56. http://dx.doi.org/10.5336/dermato.2019-71841.

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17

Dunn, Christopher J., and Karen L. Goa. "Fibrin Sealant." Drugs 58, no. 5 (1999): 863–86. http://dx.doi.org/10.2165/00003495-199958050-00010.

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18

Banton, C. J., and B. G. Overell. "Fibrin Binding." Drugs 33, Supplement 3 (1987): 93–96. http://dx.doi.org/10.2165/00003495-198700333-00014.

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19

&NA;. "Fibrin sealant." Reactions Weekly &NA;, no. 1194-1195 (March 2008): 17–18. http://dx.doi.org/10.2165/00128415-200811940-00057.

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20

Clark, G. A. "Fixin' Racism." Anthropology News 39, no. 3 (March 1998): 7. http://dx.doi.org/10.1111/an.1998.39.3.7.

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21

Aghaloo, Tara L. "Fibrin Glue." Journal of Oral and Maxillofacial Surgery 63, no. 8 (August 2005): 15. http://dx.doi.org/10.1016/j.joms.2005.05.053.

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22

&NA;. "SpectrolyseTM/fibrin." Blood Coagulation & Fibrinolysis 4, no. 3 (June 1993): 509. http://dx.doi.org/10.1097/00001721-199306000-00022.

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23

Jackson, M. R., M. J. MacPhee, W. N. Drohan, and B. M. Alving. "Fibrin sealant." Blood Coagulation & Fibrinolysis 7, no. 8 (November 1996): 737–46. http://dx.doi.org/10.1097/00001721-199611000-00001.

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24

Cederholm-Williams, S. A. "Fibrin glue." BMJ 308, no. 6943 (June 11, 1994): 1570. http://dx.doi.org/10.1136/bmj.308.6943.1570.

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25

Ashraf, H., D. Pollock, and S. Subramanian. "Fibrin Glue." Annals of Thoracic Surgery 40, no. 2 (August 1985): 205. http://dx.doi.org/10.1016/s0003-4975(10)60023-9.

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26

Rousou, John A., Richard M. Engelman, Robert H. Breyer, and Richard Steingart. "Fibrin Glue." Annals of Thoracic Surgery 40, no. 2 (August 1985): 205. http://dx.doi.org/10.1016/s0003-4975(10)60024-0.

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27

Atrah, H. I. "Fibrin glue." BMJ 308, no. 6934 (April 9, 1994): 933–34. http://dx.doi.org/10.1136/bmj.308.6934.933.

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28

FAULK, W. PAGE. "Placental Fibrin." American Journal of Reproductive Immunology 19, no. 4 (April 1989): 132–35. http://dx.doi.org/10.1111/j.1600-0897.1989.tb00562.x.

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29

Martinowitz, Uri, and Renato Saltz. "Fibrin sealant." Current Opinion in Hematology 3, no. 5 (1996): 395–402. http://dx.doi.org/10.1097/00062752-199603050-00011.

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30

Rousou, J. A., R. M. Engelman, and R. H. Breyer. "Fibrin glue." Plastic and Reconstructive Surgery 76, no. 5 (November 1985): 812. http://dx.doi.org/10.1097/00006534-198511000-00096.

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31

&NA;. "Fibrin sealant." Reactions Weekly &NA;, no. 1410 (July 2012): 23. http://dx.doi.org/10.2165/00128415-201214100-00071.

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32

O??Sullivan, F., R. Dalton, and C. K. Rostron. "Fibrin Glue." Journal of Glaucoma 5, no. 6 (December 1996): 367???370. http://dx.doi.org/10.1097/00061198-199612000-00002.

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33

Saltz, Renato. "FIBRIN GLUE." Plastic and Reconstructive Surgery 90, no. 4 (October 1992): 726. http://dx.doi.org/10.1097/00006534-199210000-00034.

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34

Singh, Kimberly, Hunter Moyer, Joseph K. Williams, Zvi Schwartz, and Barbara D. Boyan. "Fibrin Glue." Annals of Plastic Surgery 66, no. 3 (March 2011): 301–5. http://dx.doi.org/10.1097/sap.0b013e3181fc0507.

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35

Vagefi, Parsia A., and Chris E. Freise. "Fibrin plug." Kidney International 78, no. 9 (November 2010): 942. http://dx.doi.org/10.1038/ki.2010.236.

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36

Drumheller, Glenn W. "Fibrin Glue." Ear, Nose & Throat Journal 82, no. 7 (July 2003): 483. http://dx.doi.org/10.1177/014556130308200706.

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37

Brennan, M. "Fibrin glue." Blood Reviews 5, no. 4 (December 1991): 240–44. http://dx.doi.org/10.1016/0268-960x(91)90015-5.

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38

Jen, C. J., and S. J. Hu. "Direct platelet-fibrin interaction that does not require platelet activation." American Journal of Physiology-Heart and Circulatory Physiology 253, no. 4 (October 1, 1987): H745—H750. http://dx.doi.org/10.1152/ajpheart.1987.253.4.h745.

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Interactions between platelets and fibrin are important in hemostasis but often confused with platelet-fibrinogen interactions. Fibrin solubilized in NaBr-acetic acid formed polymers in neutral pH buffers. A stirred mixture of solubilized fibrin and washed human platelets at neutral pH range showed drastic reduction in turbidity and concomitant platelet adhesion onto newly formed fibrin strands. Optimally, more than 99% of platelets could be associated with fibrin, whereas only 3% of erythrocytes were trapped in the fibrin network under similar conditions. This platelet-fibrin interaction was fibrin concentration dependent and polymerization stage dependent. It preceded any detectable platelet release of serotonin. Gly-Pro-Arg-Pro (250 times in excess) retarded the kinetics of fibrin polymerization as well as that of platelet-fibrin interaction. However, factors affecting platelet activation showed little effect on platelet-fibrin interaction. Our results support the existence of a platelet-fibrin interaction that does not require platelet activation.

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39

Soon, Allyson, Sarah Stabenfeldt, Cedric Paulou, Thomas Barker, and Wallace H. Coulter. "Engineering fibrin ECM using fibrin knob-pocket interactions." Matrix Biology 27 (December 2008): 53. http://dx.doi.org/10.1016/j.matbio.2008.09.394.

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40

Starmans, Lucas W. E., Sander M. J. van Duijnhoven, Raffaella Rossin, Silvio Aime, Mat J. A. P. Daemen, Klaas Nicolay, and Holger Grüll. "SPECT imaging of fibrin using fibrin-binding peptides." Contrast Media & Molecular Imaging 8, no. 3 (January 11, 2013): 229–37. http://dx.doi.org/10.1002/cmmi.1521.

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41

Bereczky, Zsuzsanna, Ëva Katona, and Läszlö Muszbek. "Fibrin Stabilization (Factor XIII), Fibrin Structure and Thrombosis." Pathophysiology of Haemostasis and Thrombosis 33, no. 5-6 (2003): 430–37. http://dx.doi.org/10.1159/000083841.

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42

Matveeva, Vera G., Mariam Yu Khanova, Tatyana V. Glushkova, and Larisa V. Antonova. "Influence of different concentrations of fibrinogen on the properties of a fibrin matrix for vascular tissue engineering." I.P. Pavlov Russian Medical Biological Herald 29, no. 1 (March 15, 2021): 21–34. http://dx.doi.org/10.23888/pavlovj202129121-34.

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Aim. To evaluate the potential utility of fibrin matrices containing 10, 20, and 25 mg/ml of fibrinogen (fibrin-10, fibrin-20, and fibrin-30, respectively) in vascular tissue engineering (VTE). Materials and Methods. Fibrinogen was isolated using the method of ethanol cryoprecipitation and polymerized using a solution of thrombin and CaCl2. The fibrin structure was studied in a scanning electron microscope, and the physical and mechanical properties of the material were tested on a Zwick/Roell test machine. The metabolic activity of endothelial cells (EC) on the fibrin surface was evaluated by the MTT assay, and the viability of fibroblasts in the thickness of fibrin and possibility for migration by in fluorescent and light microscopy. Percent of fibrin shrinkage was determined from the difference in the sample volumes before and after removal of moisture. Results. The fiber diameter did not differ among all fibrin samples, but the pore diameter in fibrin-30 was smaller than those in fibrin-10 and fibrin-20. A possibility for migration of fibroblasts into the depth of the fibrin matrix and preservation of 97-100% viability of cells at a depth 5 mm was confirmed. The metabolic activity of EC on the surface of fibrin-20 and fibrin-30 exceeded that on collagen, fibronectin, and fibrin-10. All fibrin samples shrank in volume to 95.5-99.5%, and the highest shrinkage was seen in fibrin-10. The physical and mechanical properties of fibrin were inferior to those of human A. mammaria by a factor of 10. Conclusion. Fibrin with fibrinogen concentrations of 20 and 30 mg/ml maintains a high metabolic and proliferative activity of EC on the surface and also a high viability of fibroblasts in the matrix. Its availability, ease of preparation, and a number of other favorable properties make fibrin a promising material for VTE. However, the problem of insufficient strength requires further investigations.

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43

Collet, J. P., J. W. Weisel, S. S. Mirshahi, M. Mirshahi, J. P. Caen, Z. Mishal, J. Soria, and C. Soria. "73. Platelet interaction with fibrin depends upon fibrin physical properties. Consequences on fibrin rigidity." Blood Coagulation & Fibrinolysis 9, no. 7 (October 1998): 705. http://dx.doi.org/10.1097/00001721-199810000-00093.

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44

Poole, Lauren G., Anna K. Kopec, Dafna J. Groeneveld, Asmita Pant, Kevin S. Baker, Holly M. Cline-Fedewa, Matthew J. Flick, and James P. Luyendyk. "Factor XIII cross-links fibrin(ogen) independent of fibrin polymerization in experimental acute liver injury." Blood 137, no. 18 (May 6, 2021): 2520–31. http://dx.doi.org/10.1182/blood.2020007415.

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Abstract Intravascular fibrin clot formation follows a well-ordered series of reactions catalyzed by thrombin cleavage of fibrinogen leading to fibrin polymerization and cross-linking by factor XIIIa (FXIIIa). Extravascular fibrin(ogen) deposits are observed in injured tissues; however, the mechanisms regulating fibrin(ogen) polymerization and cross-linking in this setting are unclear. The objective of this study was to determine the mechanisms of fibrin polymerization and cross-linking in acute liver injury induced by acetaminophen (APAP) overdose. Hepatic fibrin(ogen) deposition and cross-linking were measured following APAP overdose in wild-type mice, mice lacking the catalytic subunit of FXIII (FXIII−/−), and in FibAEK mice, which express mutant fibrinogen insensitive to thrombin-mediated fibrin polymer formation. Hepatic fibrin(ogen) deposition was similar in APAP-challenged wild-type and FXIII−/− mice, yet cross-linking of hepatic fibrin(ogen) was dramatically reduced (>90%) by FXIII deficiency. Surprisingly, hepatic fibrin(ogen) deposition and cross-linking were only modestly reduced in APAP-challenged FibAEK mice, suggesting that in the APAP-injured liver fibrin polymerization is not strictly required for the extravascular deposition of cross-linked fibrin(ogen). We hypothesized that the oxidative environment in the injured liver, containing high levels of reactive mediators (eg, peroxynitrite), modifies fibrin(ogen) such that fibrin polymerization is impaired without impacting FXIII-mediated cross-linking. Notably, fibrin(ogen) modified with 3-nitrotyrosine adducts was identified in the APAP-injured liver. In biochemical assays, peroxynitrite inhibited thrombin-mediated fibrin polymerization in a concentration-dependent manner without affecting fibrin(ogen) cross-linking over time. These studies depict a unique pathology wherein thrombin-catalyzed fibrin polymerization is circumvented to allow tissue deposition and FXIII-dependent fibrin(ogen) cross-linking.

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45

Zhang, Danmei, Mariam Ebrahim, Kristin Adler, Xavier Blanchet, Janina Jamasbi, Remco T. A. Megens, Kerstin Uhland, et al. "Glycoprotein VI is not a Functional Platelet Receptor for Fibrin Formed in Plasma or Blood." Thrombosis and Haemostasis 120, no. 06 (June 2020): 977–93. http://dx.doi.org/10.1055/s-0040-1710012.

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AbstractGlycoprotein VI (GPVI), a platelet collagen receptor, is crucial in mediating atherothrombosis. Besides collagen, injured plaques expose tissue factor (TF) that triggers fibrin formation. Previous studies reported that GPVI also is a platelet receptor for fibrinogen and fibrin. We studied the effect of anti-GPVI antibodies and inhibitors of GPVI signaling kinases (Syk and Btk) on platelet adhesion and aggregate formation onto immobilized fibrinogen and different types of fibrin under arterial flow conditions. Fibrin was prepared from isolated fibrinogen (“pure fibrin”), recombinant fibrinogen (“recombinant fibrin”), or generated more physiologically from endogenous fibrinogen in plasma (“plasma fibrin”) or by exposing TF-coated surfaces to flowing blood (“blood fibrin”). Inhibition of GPVI and Syk did not inhibit platelet adhesion and aggregate formation onto fibrinogen. In contrast anti-GPVI antibodies, inhibitors of Syk and Btk and the anti-GPIb antibody 6B4 inhibited platelet aggregate formation onto pure and recombinant fibrin. However, inhibition of GPVI and GPVI signaling did not significantly reduce platelet coverage of plasma fibrin and blood fibrin. Plasma fibrin contained many proteins incorporated during clot formation. Advanced optical imaging revealed plasma fibrin as a spongiform cushion with thicker, knotty, and long fibers and little activation of adhering platelets. Albumin intercalated in plasma fibrin fibers left only little space for platelet attachment. Pure fibrin was different showing a dense mesh of thin fibers with strongly activated platelets. We conclude that fibrin formed in plasma and blood contains plasma proteins shielding GPVI-activating epitopes. Our findings do not support a role of GPVI for platelet activation by physiologic fibrin.

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Tymkewycz, P. M., L. J. Creighton-Kempsford, D. Hockley, and P. J. Gaffney. "Screening for Fibrin Specific Monoclonal Antibodies: The Development of a New Procedure." Thrombosis and Haemostasis 68, no. 01 (1992): 048–53. http://dx.doi.org/10.1055/s-0038-1656316.

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SummaryThe acquisition of monoclonal antibodies specific for human fibrin has been impaired by the similarity in chemical composition between fibrinogen and fibrin and the conformational difference between immobilised and soluble fibrinogen. Five monoclonal antibodies (mabs) with a known affinity for fibrin have been subjected to screening procedures which involved the presentation of different forms of both fibrinogen and fibrin to the test mabs. It was observed by scanning electron microscopy that dried fibrin (denoted fibrin D), immobilised on the wells of PVC plates was morphologically similar to the fibrin found in human clots whereas PVC-immobilised fibrin monolayers (fibrin M) and a homogenised form of fibrin (fibrin FF) presented two very different morphological appearances. It was shown that lack of cross reactivity of a mab with an antigen (e.g. fibrinogen) was validly demonstrated only when both mab and antigen were present in the soluble state. These findings have allowed the generation of a screening procedure which involves the use of fibrin D on PVC plates in conjunction with whole human plasma incubated with the test antibody. This screening procedure has been validated using two mabs, one of which has an exclusive fibrin affinity while the other has a broad spectrum crossreactivity with both fibrinogen and fibrin. This procedure would ensure the acquisition of all the five fibrin-specific mabs used in this study while other less reliable screening procedures might not.

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Campbell, Robert A., Katherine A. Overmyer, Craig H. Selzman, Brett C. Sheridan, and Alisa S. Wolberg. "Contributions of extravascular and intravascular cells to fibrin network formation, structure, and stability." Blood 114, no. 23 (November 26, 2009): 4886–96. http://dx.doi.org/10.1182/blood-2009-06-228940.

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Abstract Fibrin is essential for hemostasis; however, abnormal fibrin formation is hypothesized to increase thrombotic risk. We previously showed that in situ thrombin generation on a cell's surface modulates the 3-dimensional structure and stability of the fibrin network. Currently, we compared the abilities of extravascular and intravascular cells to support fibrin formation, structure, and stability. Extravascular cells (fibroblasts, smooth muscle) supported formation of dense fibrin networks that resisted fibrinolysis, whereas unstimulated intravascular (endothelial) cells produced coarse networks that were susceptible to fibrinolysis. All 3 cell types produced a fibrin structural gradient, with a denser network near, versus distal to, the cell surface. Although fibrin structure depended on cellular procoagulant activity, it did not reflect interactions between integrins and fibrin. These findings contrasted with those on platelets, which influenced fibrin structure via interactions between β3 integrins and fibrin. Inflammatory cytokines that induced prothrombotic activity on endothelial cells caused the production of abnormally dense fibrin networks that resisted fibrinolysis. Blocking tissue factor activity significantly reduced the density and stability of fibrin networks produced by cytokine-stimulated endothelial cells. Together, these findings indicate fibrin structure and stability reflect the procoagulant phenotype of the endogenous cells, and suggest abnormal fibrin structure is a novel link between inflammation and thrombosis.

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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 sites (‘EA’), or with defective end-to-end self-association sites (‘D:D’) [Cedar Rapids (γR275C)], exposed both ‘fibrin-specific’ epitopes and enhanced tPA-dependent plasminogen activation, whereas non-crosslinked fibrinogens showed minimal or no such activities. Epitope expression in cross-linked fibrinogen was retained in the presence of the fibrin EA site peptide homolog, gly-pro-arg-pro (GPRP), which inhibits fibrin D:E association, except for the Aα148-160 epitope in des Bβ1-42 fibrinogen, which was not expressed. Fibrin prepared from crosslinked normal or abnormal fibrinogen, except for the des Bβ1-42 fibrin epitopes, which were reduced or absent, expressed ‘fibrin-specific’ epitopes even in the presence of GPRP, which otherwise impairs such expression in noncrosslinked fibrin. Epitope exposure in fibrin prepared from non-cross-linked fibrinogen was nearly normal in Cedar Rapids fibrin (heterozygous D:D defect), but reduced in Birmingham fibrin (heterozygous EA defect), nil in des Bβ1-42 fibrin (EA deficient), and absent in all cases in the presence of GPRP. In contrast, plasminogen activation stimula-tory activity that had been exposed in crosslinked normal fibrinogen or in crosslinked des Bβ1-42 or Cedar Rapids fibrin, was preserved to a large extent in the presence of GPRP, suggesting that once enhanced stimulatory activity and epitopes are exposed, they are not completely reversible. The findings indicate that end-to-end intermolecular associations (D:D) are not critical for ‘fibrin-specific’ epitope exposure, but that polymerization brought about in fibrinogen through factor XIIIa crosslinking, or in fibrin through ‘D:E’ interactions, is necessary for ‘fibrin-specific’ (more correctly, ‘polymerization-specific’) epitope exposure and enhancement of plasminogen activation.

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Sage, August, Angela A. Chang, Barbara L. Schumacher, Robert L. Sah, and Deborah Watson. "Cartilage Outgrowth in Fibrin Scaffolds." American Journal of Rhinology & Allergy 23, no. 5 (September 2009): 486–91. http://dx.doi.org/10.2500/ajra.2009.23.3347.

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Background Fibrin glue has been a favorable hydrogel in cartilage tissue engineering, but implantation of chondrocyte-fibrin suspensions have resulted in volume loss. In this study, human septal cartilage chips were seeded onto a fibrin scaffold, and cellular proliferation and production of cartilaginous extracellular matrix (ECM) were evaluated. Methods Human septal cartilage was diced into cartilage chips and encased with and without fibrin glue. Four conditions were initially tested for DNA content and glycosaminoglycan (GAG) production: (1) control medium in tissue culture, (2) control medium with fibrin glue, (3) collagenase-supplemented medium in tissue culture, and (4) collagenase-supplemented medium seeded in fibrin glue. Cartilage chips cultured in collagenase-treated medium were then seeded onto either cell culture plates, suspended in alginate, or mixed with fibrin. Cellular proliferation, GAG production, and histochemistry were evaluated. Results Fibrin preparations increased cellular proliferation and DNA content. GAG levels were highest in collagenase-treated samples encased in fibrin. Cartilage chips treated with collagenase showed increased cellular proliferation in the fibrin preparations compared with preparations without fibrin. GAG increased with the addition of fibrin when compared with explant. Histochemistry revealed increased GAG accumulation in the regions between the cartilage chips with the addition of fibrin. Conclusion Adding fibrin glue to collagenase-treated cartilage chips results in increased proliferation and maintains ECM production and, therefore, may facilitate generation of cartilaginous tissue for use in reconstructive surgery.

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Sporn, LA, LA Bunce, and CW Francis. "Cell proliferation on fibrin: modulation by fibrinopeptide cleavage." Blood 86, no. 5 (September 1, 1995): 1802–10. http://dx.doi.org/10.1182/blood.v86.5.1802.bloodjournal8651802.

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Fibrin forms the cohesive network of hemostatic plugs and thrombi, and it also provides the temporary matrix for initial support of healing and revascularization. Because cell proliferation is needed for revascularization after vessel injury, we have characterized structural requirements of fibrin needed to support cell proliferation on fibrin in vitro. Proliferation of cultured human endothelial cells and fibroblasts was measured by 3H-thymidine incorporation on fibrin surfaces varying in structure. Fibrin prepared with thrombin and lacking both fibrinopeptides A and B (desAB fibrin) supported proliferation of both endothelial cells and fibroblasts. In contrast, fibrin prepared with reptilase, which cleaves only fibrinopeptide A, supported significantly less proliferation. Also, fibrin prepared by thrombin treatment of fibrinogen lacking residues beta 1–42 supported only a low level of proliferation. Therefore, fibrinopeptide B cleavage and exposure of beta 15–42 enhanced proliferation of cells on fibrin. Specific proteolytic inhibitors were used to eliminate the potential mitogenic effects of residual fibrin-bound thrombin. Additional controls showed that neither catalytically inactive thrombin nor addition of the thrombin receptor-activating peptide (SFLLRNPNDKYEPF [SFLL]) stimulated proliferation on desA fibrin. The results indicate that cell proliferation on fibrin is enhanced by fibrinopeptide B cleavage and exposure of the amino terminus of the fibrin beta chain. They also show that specific structural features of the temporary fibrin matrix formed at sites of injury may modulate the proliferative response of vascular cells.

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