Relevant bibliographies by topics / Fibin

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Fibin'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Fibin.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Fibin"

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Fibin"

1

Seyer, Christian. "Funktionelle und proteinbiochemische Charakterisierung von Fibin." Doctoral thesis, Universitätsbibliothek Leipzig, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-109763.

Full text
Abstract:
Im Zebrafisch (Danio rerio) ist ein Protein identifiziert worden, das eine wichtige Rolle in der Entwicklung der Brustflossen zu besitzen scheint und als Fibin, dem englischen Akronym für Fin bud initiation factor (Flossenknospeninitiationsfaktor), bezeichnet wurde. Es zeigt keine Verwandtschaft zu anderen bekannten Proteinen, enthält keine typischen Strukturmotive, wird auf nur einem Exon kodiert und ist in allen bisher untersuchten Vertebraten, einschließlich des Menschen, evolutionär hoch konserviert. Ziel der vorliegenden Arbeit war die nähere funktionelle und proteinbiochemische Charakterisierung Fibins. In vielen Geweben adulter Mäuse (Mus musculus), v. a. in zerebralen und muskulären Proben, konnte Fibin mRNA nachgewiesen werden. Im Vergleich zum Adultus war die Expression in Geweben pränataler Mäuse bedeutend höher und unterschied sich in der Region der Vordergliedmaßen kaum von der im Torso. In L929 (Fibroblasten) und HEK Zellen (embryonale Nierenzellen) wurde eine hohe Expression von Fibin nachgewiesen, die in L929 Zellen durch Glukokortikoide und Aktivatoren des Proteinkinase C / MAP-Kinase , Proteinkinase A sowie des NF-κB / AP-1 bzw. Nrf2 / ARE Signalwegs erhöht werden konnte. Die nicht-proteinkodierende 5‘ Region des humanen Fibin Gens zeigte im Luciferase Reporterassay in L929 und HEK Zellen promotogene Eigenschaften, mit einem Aktivitätsmaximum der Sequenz – 836 Basenpaare bezogen auf den Translationsstartpunkt. In L929 Zellen wurde die promotogene Aktivität durch Glukokortikoide und Aktivatoren des Proteinkinase C / MAP-Kinase- sowie des NF κB / AP 1 bzw. Nrf2 / ARE Signalwegs erhöht. Fibin besitzt eine putative N terminale Signalsequenz und eine N Glykosylierungsstelle, die beide experimentell bestätigt wurden. Rekombinantes Fibin zeigte in der Fluoreszenzmikroskopie in COS-7 Zellen (Fibroblasten) eine hohe Kolokalisation mit dem Endoplasmatischen Retikulum, jedoch nur eine geringe mit dem Golgi Apparat. In COS-7 Zellen wurde es nicht über den sekretorischen Weg freigesetzt und zeigte in proteinbiochemischen Untersuchungen eine hohe Tendenz zur Aggregation und Ausbildung von Disulfidbrücken. Es ist anzunehmen, dass Fibin möglicherweise ein bisher unbekanntes Protein für die Ausbildung von Heteromeren benötigt, um erfolgreich sezerniert zu werden.
APA, Harvard, Vancouver, ISO, and other styles
2

Seyer, Christian [Verfasser], Torsten [Akademischer Betreuer] Schöneberg, Joachim [Gutachter] Thiery, and Rolf [Gutachter] Gebhardt. "Funktionelle und proteinbiochemische Charakterisierung von Fibin / Christian Seyer ; Gutachter: Joachim Thiery, Rolf Gebhardt ; Betreuer: Torsten Schöneberg." Leipzig : Universitätsbibliothek Leipzig, 2013. http://d-nb.info/1238366287/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

若原, 隆史. "ゼブラフィッシュの胸びれ形成に関与する新規分泌性タンパク質fibinの役割." 京都大学 (Kyoto University), 2007. http://hdl.handle.net/2433/137128.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Moreira, Marcos Mello. "Variaveis capnograficas e d-dimeros em pacientes com suspeita de tromboembolismo pulmonar." [s.n.], 2009. http://repositorio.unicamp.br/jspui/handle/REPOSIP/311721.

Full text
Abstract:
Orientadores: Renato Giuseppe Giovanni Terzi, Ilma Aparecida Paschoal
Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Ciencias Medicas
Made available in DSpace on 2018-08-12T22:30:15Z (GMT). No. of bitstreams: 1 Moreira_MarcosMello_D.pdf: 18313915 bytes, checksum: db1efb99a56b2256d14393f2e951147a (MD5) Previous issue date: 2009
Resumo: Métodos para confirmar o diagnóstico de tromboembolismo pulmonar (TEP) são relativamente invasivos, de alto custo e nem sempre disponíveis. Justifica-se a busca de métodos mais acessíveis, de baixo custo, minimamente invasivos e que possam ser realizados à beira do leito. Foi objetivo deste estudo estabelecer um protocolo de triagem diagnóstica de TEP, minimamente invasivo e de baixo custo, usando para isto a capnografia volumétrica (CV) e o Oímero-O (DO) (ELISA Rápido), para pacientes internados em diferentes unidades de um hospital terciário, atentanto para as possíveis limitações deste protocolo. Foi realizado um estudo prospectivo e observacional com 92 pacientes. Um estudo prévio de CV em 114 voluntários estabeleceu o padrão de normalidade para as variáveis analisadas. No grupo TEP, a CV foi associada à gasometria arterial para cálculo das variáveis do espaço morto e à dosagem do DO. O padrão-ouro para diagnóstico de TEP foi dado pela cintilografia de inalação/perfusão e/ou, tomografia computadorizada helicoidal e/ou, arteriografia pulmonar. Isoladamente, a variável capnográfica que apresentou melhor sensibilidade e especificidade foi a fração tardia do espaço morto alveolar (tO/ate) (91% e 98%, respectivamente). Obteve-se um resultado falso-negativo para o DO e, para a tO/ate, um falso-positivo e três falso-negativos. Quando a tO/ate ,foi associada ao DO, conseguiu-se 100% sensibilidade e 17% de especificidade. Uma outra variável capnográfica importante, por sugerir função pulmonar prévia anormal, e por esta razão, sinalizar uma possível limitação da tO/ate, foi o slope da fase III do capnograma. Por meio dos dados da CV de ambos os grupos (controle e doentes), estabeleceu-se um protocolo que ajuda a direcionar a equipe multiprofissionál quando da suspeita clínica de TEP.
Abstract :Background: Tests used to confirm a diagnosis of pulmonary embolism (PE) are relatively invasive, costly and not always available. Minimally invasive methods that are more accessible, less expensive and easily applied should be sought. Objective: To establish a low-cost, minimally invasive, PE diagnostic protocol in hospitalized patients, using capnographic variables and ELlSA D-dimer (DD) to rule out PE. Methods: A prospective observational study was conducted in 92 patients with suspected PE. The values of reference group for volumetric capnography (VCap) were used in order to compare with patterns of patients with PE. The patients were submitted to arterial blood gas analysis (to calculate the dead space variables) and had the DD values determined. The diagnosis was confirmed through ventilation/perfusion scintigraphy, spiral computed tomography, pulmonary arteriogram, or combinations of the three. Results: The capnographic variable that presented the greatest sensitivity and specificity (91 % and 98%, respectively) was the late dead space fraction (fDlate). Our findings include one false-negative DD result, as well as three false-positive and eight false-negative fDlate results. The combination of the fDlate and DD testing presented 100% sensitivity and 17% specificity. Another important capnographic variable, the phase 111 slope, indicated a possible limitation of VCap, since it interferes with the calculation of fDlate. Conclusion: The protocol established could guide multiprofessional teams in the management of clinical suspicion of PE. We were able to determine that the phase 111 slope might interfere with the calculation of fDlate, especially in patients with a history of abnormal lung function. Throught VCap variables (control group and sickness); was possible establishes a protocol that guide the multiprofissional team in cases of PE.
Doutorado
Pesquisa Experimental
Doutor em Cirurgia
APA, Harvard, Vancouver, ISO, and other styles
5

楠, 直樹. "分泌性因子SclerostinおよびFibinの骨形成における役割に関する研究." 京都大学 (Kyoto University), 2006. http://hdl.handle.net/2433/144286.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Sathananthan, Saranya. "Modulating fibrin matrix properties via fibrin knob peptide functionalized microgels." Thesis, Georgia Institute of Technology, 2012. http://hdl.handle.net/1853/44905.

Full text
Abstract:
Fibrin is the body's natural provisional matrix activated in response to vascular injury in which noncovalent knob:hole interactions between fibrin monomers lead to the assembly of fibrin for clot formation. In this study we aimed to exploit fibrin knob:hole affinity interactions with swelling, space filling microgels for the development of a potential bio-synthetic hybrid polymer system with hemostatic properties. Previous work has explored the inherent binding interactions of various fibrin knobs and their complementary polymerization holes, which have led to the development of fibrin knob peptide mimic (GPRPFPAC) with enhanced binding affinity for fibrin(ogen) holes. By coupling this enhanced fibrinogen binding peptide with a pNIPAm microgel system capable of being dynamically tuned and self-assembled, we hypothesized the specific and rapidly triggered formation of a bulk hydrogel in a wound environment (i.e. in the presence of fibrinogen). We found that at the peptide ligand density and concentrations of microgels used, that a rapid formation of a gel did not occur in the presence of fibrinogen alone. However with fibrinogen and thrombin, we found that fibrin network polymerization, structure, and viscoelastic properties were greatly altered in the presence of knob peptide-conjugated microgels.
APA, Harvard, Vancouver, ISO, and other styles
7

Soon, Allyson Shook Ching. "Exploiting fibrin knob:hole interactions for the control of fibrin polymerization." Diss., Georgia Institute of Technology, 2011. http://hdl.handle.net/1853/45917.

Full text
Abstract:
The minimization of blood loss represents a significant clinical need in the arena of surgery, trauma, and emergency response medicine. Fibrinogen is our body's native polymer system activated in response to tissue and vasculature injury, and forms the foundation of the most widely employed surgical sealant and hemostatic agent. Non-covalent knob:hole interactions are central to the assembly of fibrin that leads to network and clot formation. This project exploits these affinity interactions as a strategy to direct fibrin polymerization dynamics and network structure so as to develop a temperature-triggered polymerizing fibrin mixture for surgical applications. Short peptides modeled after fibrin knob sequences have been shown to alter fibrin matrix structure by competing with native fibrin knobs for binding to the available holes on fibrinogen and fibrin. The fusion of such knob peptides to a non-native component should facilitate binding of the fused component to fibrinogen/fibrin, and may permit the concomitant modification of the fibrin matrix. We examined this hypothesis in a three-step approach involving (a) analyzing the ability of tetrapeptide knob sequences to confer fibrin(ogen) affinity on a non-fibrin protein, (b) investigating the effect of knob display architecture on fibrin(ogen) structure, and (c) designing a temperature-responsive knob-displaying construct to modulate fibrin(ogen) affinity at different temperature regimes, thus altering fibrin(ogen) structure.
APA, Harvard, Vancouver, ISO, and other styles
8

Allan, Peter. "Microrheology of fibrin clots." Thesis, University of Leeds, 2012. http://etheses.whiterose.ac.uk/3042/.

Full text
Abstract:
An active particle tracking microrheology technique has been developed to study the viscoelastic properties of human fibrin and plasma clots. In order to perform microrheology measurements, a magnetic microrheometer device has been adapted and a technique developed, following the procedure of Evans et al., to measure the frequency dependent viscoelastic moduli (G() and G()). This technique has been supported by complementary investigation methodologies, such as protein analysis, turbidity, and multiple microscopy techniques. As a result of this study new insights into the viscoelastic dynamics of fibrin have been revealed. Three stress relaxation mechanisms, as predicted by Morse et al. for networks of semi-flexible fibres, were observed and occur on distinctly different timescales. The scaling of the tension dominated contribution was measured to scale as G ~ c2.7 0.2 in agreement with the prediction of Mackintosh. The presence of FXIII resulted in stiffer less deformable clots but was found to have no effect on the viscoelastic dynamics of clots. Frequency measurements of the loss tangent revealed that on timescales intermediate between stress relaxation modes clots were much more susceptible to permanent deformation. The effect of fibrinogen, thrombin and calcium on the viscoelastic behaviour of clots was also investigated. Increased fibrinogen levels produced clots which displayed predominantly elastic behaviour on shorter time-scales. The molecular mechanism underpinning the role of fibrinogen γ in fibrin clot polymerisation, structure and viscoelasticity was also investigated. We report new data which show that fibrinogen γ is associated with the formation of mechanically weaker, non-uniform clots composed of thinner fibres. This is caused by direct disruption of protofibril formation by and not through thrombin inhibition or binding to FXIII. In addition, the effects of the plasma proteins FVIIa, FIXa, FXIIa and FXIII on clot properties are also reported.
APA, Harvard, Vancouver, ISO, and other styles
9

Purves, Maud. "The D-domain of fibrin : structural and functional studies." Doctoral thesis, University of Cape Town, 1987. http://hdl.handle.net/11427/27202.

Full text
Abstract:
The D-domain of fibrin (ogen) was separated from the parent molecule by plasmin digestion in the presence of calcium and isolated by means of DEAE-anion exchange chromatography followed by gel-filtration in buffer containing 4 M urea. Fluorescent-D-dimer (f-D-dimer) was isolated from a plasmic digest of fibrin clotted in the presence of 2.45 mM dansyl cadaverine, a fluorescent lysine analogue. Fluorescent-D-monomer was a by-product of f-D-dimer purification, the yield being determined by the concentration of dansyl cadaverine. At 2.45 mM f-D-monomer was always present in the digest. The f-D-monomer is probably formed directly and not as a result of degradation of f-D-dimer. The molecule elutes in the fibrinogen-derived-D- monomer position on gel-filtration. A protease was isolated and partially purified from venom of the puffadder (Bitis arietans). Puffadder venom protease is characterized by its ability to cleave D-dimer into symmetrical D-monomers, smaller than plasmin-derived D-monomers from fibrinogen. This characteristic was used to detect the puffadder venom protease activity with fluorescent-D-dimer being used as the substrate. Fractions obtained were assayed for D-dimer cleavage activity and the samples analyzed by means of SDS-PAGE on 4-20% gradient gels under reducing (βME) and non-reducing conditions. The fluorescent bands were located under U.V light and photographed prior to staining with Coomassie Blue. Several methods for the purification of the protease were investigated.
APA, Harvard, Vancouver, ISO, and other styles
10

Fatah, Kamaran Tahir. "Studies on fibrin gel structure /." Stockholm, 1998. http://diss.kib.ki.se/search/diss.se.cfm?19980608fata.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Fibin"

1

Fitin. Moskva: Molodai︠a︡ gvardii︠a︡, 2015.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Rakotonavahy, Lila Hanitra Ratsifandrihamanana. Fihin-tanana. [Antanimena, Antananarivo: s.n., 1998.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Cilizoglu, Leman Eryilmaz. Firin Yemekleri. Istanbul: Remzi Kitabevi, 1995.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

1961-, Smoláriková Květa, and British Museum, eds. Kom Firin. London: British Museum, 2008.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

Fixin' to die. New York: Bantam Books, 1992.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Marshall, Gerald. Fixin' old glory. Fort Worth, Tex: Center for Freedom and Free Enterprise, 1993.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

Bryant, Helen. Fixin' to be Texan. Plano, Tex: Republic of Texas Press, 1999.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

Bryant, Helen. Fixin' to be Texan. Plano, Tex: Republic of Texas Press, 1999.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Marcel, Raymond. Marsile Ficin (1433-1499). Paris: Les Belles lettres, 2007.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

Kalim, Mazhar. Fiban society part 1. Multan: Yusuf Brothers, 1990.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Fibin"

1

Bährle-Rapp, Marina. "Fibrin." In Springer Lexikon Kosmetik und Körperpflege, 206. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_3978.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Kerbl, Markus, Philipp Heher, James Ferguson, and Heinz Redl. "Fibrin." In Biomaterials from Nature for Advanced Devices and Therapies, 159–75. Hoboken, New Jersey: John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119126218.ch10.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Salajegheh, Ali. "Fibrin." In Angiogenesis in Health, Disease and Malignancy, 103–9. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_17.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Stief, T. "Fibrin." In Springer Reference Medizin, 862. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_1111.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Stief, T. "Fibrin." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_1111-1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Cintron, José R. "Fibrin Sealant." In Anal Fistula, 69–81. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9014-2_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Tiedemann, Anne, Catherine Sherrington, Daina L. Sturnieks, Stephen R. Lord, Mark W. Rogers, Marie-Laure Mille, Paavo V. Komi, et al. "Fibrinogen/Fibrin." In Encyclopedia of Exercise Medicine in Health and Disease, 345–46. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2401.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Yudin, Andrey. "Pleural Mouse, Fibrin Body, Fibrin Ball, and Thoracolith." In Metaphorical Signs in Computed Tomography of Chest and Abdomen, 63. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-04013-4_32.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Pötzsch, B., and K. Madlener. "Fibrinogen und Fibrin." In Hämostaseologie, 213–18. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01544-1_22.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Muszbek, L., and R. Ádány. "Intratumoral Fibrin Stabilization." In Eicosanoids, Lipid Peroxidation and Cancer, 339–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73424-3_36.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Fibin"

1

Haber, Edgar, Marchall T. Runge, Christoph Bode, Betsy Branscomb, and Janet Schnee. "ANTIBODY TARGETED FIBRINOLYSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643723.

Full text
Abstract:
Chemical conjugates of fibrin-specificantibodies and plasminogen activators. Urokinase or tPA were linked covalently toamonoclonal antibody specific for the amino terminus of the beta chain of human fibrin (59D8) by means of the unidirectionalcross-linking reagent SPDP. The fibrinolytic potency of the conjugates at equal amidolytic activities was compared to the native plasminogen activators in an assay measuring lysis of 1251-fibrin monomer covalently linked to Sepharose CL-4B. Urokinase was least potent, tPA exhibited a 10fold increase in fibrinolysis whereas both the urokinase and tPA antibody conjugates and a urokinase-Fab conjugate were 250fold more potent than urokinase and 25 fold more potent than tPA. Enhanced fibrinolysis was fully inhibited by b peptide indicating its dependence on antigen binding. In a plasma assay conjugates of tPA orUK to antibody produced a 3.2- to 4.5-fold enhancement in clot lysis in human plasma over that of the respective unconjugated plasminogen activator. However, the UK-59D8 conjugate was only as potent as tPAalone. Antibody-conjugated tPA or UK consumed less fibrinogen, alpha 2-antiplasminand plasminogen than did the unconjugatedactivators, at equipotent thrombolytic concentrations. In a quantitative rabbit thrombolysis model, the activity of the purified conjugate was compared with that oftPA alone and that of a conjugate betweentPA and a digoxin-specific monoclonal antibody. After correction for spontaneous lysis, tPA-59D8 was shown to be 2.8 to,9.6times more potent than tPA alone. Unconjugated tPA and tPA-digoxin were equipotent.At equivalent thrombolytic concentrations, tPA-59D8 degraded less fibrinogen and consumed less alpha 2-antiplasmin than did tPA alone. These results suggest that tPA can be efficiently directed to the site of a thrombus by conjugation to an antifibrin monoclonal antibody, resulting in both more potent and more selective thrombolysis.A recombinant fusion protein comprising a fibrin-specific antibody site and theB chain of tPA. The rearranged 59D8 heavychain gene was cloned and combined in theexpression vector pSV2gpt withsequence coding for a portion of the Gamma 2b constant region and the catalytic beta chain of t-PA. This construct was transfected into heavy chain loss variant cells derived from the 59D8 hybridoma. Recombinant protein was purified by affinitychromatography and analyzed with Western blots. These revealed a 65-kD heavy chain-t-PA fusion protein that is secreted in association with the 59D8 light chain in the form of a 170-kD disulfide linked dimer. A chromogenic substrate assay showed the fusion protein to have 70 percent of the peptidolytic activity of native t-PA and to activate plasminogen as efficiently as t-PA. In a competitive binding assay, reconstituted antibody was shown to have a binding profile similar to that of native 59D8. Thus by recombinant techniques we have produced a novel hybrid protein capable of high affinity fibrin binding andplasminogen activation.Chemical conjugates between a fibrin-specific and a tPA-specific antibody. A heteroantibody duplex (duplex) with specificities for both tPA and fibrin was synthesized by conjugating iminothiolane-modified anti-tPA monoclonal antibody (TCL8) toantifibrin antibody 59D8. Addition of both duplex and tPA to a plasma clot assay gave more lysis (200 units produced 23.1 lysis; 400 units, 29.5 lysis) than did tPAalone (200 units, 1.8% lysis; 400 units,19% lysis). Despite increased potency associated with duplex addition, fibrinogen and alpha-2-antiplasmin levels at equal tPA concentrations did not differ. Thus, itis possible to concentrate tPA (added separately) to the site of a thrombus in plasma using a heteroantibody duplex with specificities for both tPA and fibrin.Biosynthetically produced heteroduplexantibodies that are both fibin and tPA-specific. The bispecific antibodies were prepared in two ways. First, polyethylene glycol-mediated fusions were performed with two different hybridoma cell lines: anti-fribrin b chain producer, 59D8 and anti-tPA producer, TCL8. TCL8 cells were selected for HPRT-minus variants and then fused with TK-deficient 59D8 cells. One cell line, F36.23, possessed both anti-human fibrin and anti-human t-PA immunoreactivities. A second method yielded another bispecific antibody, F32.1. This cell line was selected after fusing TCL8 (HPRT-minus) cells with spleen cells from a mouseimmunized with a fibrin-like peptide corresponding to the amino terminus of fibrinalpha-chains. Affinity-purified F32.1 andF36.23 retained anti-fibrin and anti-t-PAactivity and enhanced fibrinolytic potency of tPA by a factor of 10.
APA, Harvard, Vancouver, ISO, and other styles
2

Lai, Victor K., Edward A. Sander, Robert T. Tranquillo, and Victor H. Barocas. "Mechanical Properties of Collagen, Fibrin and Collagen-Fibrin Networks." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19138.

Full text
Abstract:
The macroscopic mechanical properties of bio-engineered tissues are inextricably linked to their microstructure. Often, their microstructure is a complex arrangement of several different components (e.g. collagen, fibrin) that interact with each other to give a tissue its overall properties. These microstructural complexities are further compounded by the dynamic cell interactions with the extracellular matrix (ECM). Our group [1] uses fibrin as the starting scaffold material for cell seeding and tissue growth; over time, the underlying microstructure undergoes dynamic remodeling as the fibrin network is degraded and gradually replaced with collagen. Currently, we have a modeling framework that incorporates a single-component microstructure network to predict the mechanical properties of the engineered tissue [2]. However, this model is unable to capture the transient intermediate stages of tissue growth, during which the tissue is composed of interpenetrating collagen and fibrin networks at varying compositions. In this work, we have incorporated a second network into our model and compared these modeling results with experimental data obtained from uniaxial tests on acellular collagen-fibrin co-gels. This work represents one step in the progression of our model to capture better the relationships between tissue microstructure and macroscopic mechanical properties, with the ultimate goal of developing a comprehensive model framework for rational design of functional engineered tissues.
APA, Harvard, Vancouver, ISO, and other styles
3

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.

Full text
Abstract:
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 fibronectin coated plates and antibodies against fibrin(ogen) to quantify bound fibrin. For determination of plasminogen activation we used a coupled spectrophotometric fluid phase assay with Glu-plasminogen as substrate and H-D-Val-Leu-Lys-pNA to quantify the formed plasmin. Fibrin binding to coated fibronectin was linear between 500ng and 1 mg/ml for fibrin monomers (reptilase), FCB-2 fragments and thrombin (3.3 U/ml) treated fibrinogen, respectively. A monoclonal antibody directed against the FCB-2 fibrinogen fragment which also could be shown to recognize fibirn but not fibrinogen did not recognize fibronectin bound fibrin and inhibited also the fibrin stimulatory effect on plasminogen activation indicating that the epitope against which the antibody is directed is closely related to both the fibronectin binding site and the site involved in t-PA stimulation.
APA, Harvard, Vancouver, ISO, and other styles
4

Zamarrón, C. "BINDING OF NATIVE PLASMINOGEN TO FIBRIN AND TO SOME FI BRINOGEN/FIBRIN DERIVATIVES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644832.

Full text
Abstract:
In the fibrinolytic process: (a) fibrin provides a surface on which the major reactions of fibrinolysis occurs: the conversion of plasminogen to plasmin, the cleavage of fibrin by plasmin and the inhibition of plasmin by α2-antiplasmin, (b) some fibrinogen derivatives (e.g. the cyanogen bromide digested fibrinogen fragment denominated FCB-2) can exert stimulatory properties on the plasminogen activation and (c) the initial cleavage of fibrin by plasmin increases the rate conversion of plasminogen to plasmin.The purpose of the present work has been to correlate these three aspects of the fibrinolytic process with the binding of native plasminogen (Glu-Pg) to fibrin (Fn) , fibrinogen (Fg) and Fn/Fg derivatives.The Glu-Pg-Fg interaction, if exists, it is not detectable in equilibrium conditions by analytical centrifu gation. By using a solid-phase fibrin clot system (purified system) the Glu-Pg-Fn interaction gives the following dissociation constants: Kd=3.5×10−6 M and 1.2×10−5 m (unwashed and washed clots respectively). Being two the number of plasminogen binding sites per fibrin fibrin monomer. By activation with streptokinase or urokinase the amount of Pg required for an effective lysis of the fibrin clots is lower when the Pg is endogenous (inside the clot) versus exogenous (outside the clot).The binding of the isolated fragments of the cyanogen bromide digested fibrinogen to Glu-Pg was studied by affinity chromatography on Glu-Pg-Sepharose. The only fragment bound to Glu-Pg and eluted with 10 mM ε-amino caproic acid (ε;-ACA) was the fragment denominated FCB-2 The soluble fibrin monomer after 20 min plasmin digestion also binds to immobilized Glu-Pg and it is eluted with ε-ACA.Therefore, the binding of native plasminogen to fibrin and to some fibrinogen/fibrin derivatives is a determinant factor in the three aspects of the fibrinolytic process mencioned above.
APA, Harvard, Vancouver, ISO, and other styles
5

Angles-Cano, E., R. Pannell, and V. Gurewich. "FIBRIN-BINDING STUDIES OF PRO-UROKINASE (PRO-UK) USING SOLID PHASE FIBRIN PLATES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642904.

Full text
Abstract:
Pro-UK is a single chain urokinase-type plasminogen activator (scu-PA) which has fibrin selective thrombolytic properties. However, quantitative data on pro-UK binding to fibrin and on the mechanism of its fibrin enhanced activation of plasminogen have been difficult to obtain. In the present study, a well defined fibrin network constructed on glutaraldehyde-activated PVC plates (Anal. Biochem. 153 : 201-210, 1986) and highly purified pro-UK (99 % scu-PA) were used. Binding was investigated as follows : varying dilutions of pro-UK in the presence of a trace amount of I-labeled pro-UK in buffer without or with glu-plasminogen, plasmin or oC -thrombin and in urine, plasma or serum, were incubated overnight at 4°C and then 2 h at 37°C in the fibrin plates. After washing, the wells were cut out and counted in a gamma-counter. The labeled pro-UK and the effect of enzymes on scu-PA were investigated by SDS-PAGE and autoradiography. In parallel experiments, the activity of the fibrin bound and unbound products was investigated spectrophotometrically by adding glu-plasminogen and a synthetic substrate selective for plasmin. The binding of pro-UK to fibrin was 1.7 ± 0.1 % in buffer and 0.2 ± 0.08 % in plasma, as determined from isotopic and spectro-photometric measurements. This binding is similar to that of (0.13 ± 0.05%) two-chain urokinase (plasmin-transformed scu-PA), but is extremely low compared to the specific binding of tPA (68 - 4%). By contrast, in urine, 11.2 ± 4.47 % binding of pro-UK to fibrin was observed. Thrombin did not modify the binding but transformed scu-PA into a two-chain molecule which had lost activity. These data indicate that pro-UK has little affinity for fibrin under these conditions but that some binding may be induced by a co-factor which is present in urine. Confirmation that thrombin degrades scu-PA was obtained and it is suggested that this effect may help to regulate fibrinolysis.
APA, Harvard, Vancouver, ISO, and other styles
6

Nica, Diana, Emilia Ianes, and Marius Pricop. "Platelet rich fibrin in jaw defects." In Sixth International Conference on Lasers in Medicine, edited by Darinca Carmen Todea, Adrian G. Podoleanu, and Virgil-Florin Duma. SPIE, 2016. http://dx.doi.org/10.1117/12.2189921.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Ferri, F., M. Greco, G. Arcovito, F. Andreasi Bassi, M. De Spirito, and M. Rocco. "Light scattering characterization of fibrin gels." In Photon Correlation and Scattering. Washington, D.C.: OSA, 2000. http://dx.doi.org/10.1364/pcs.2000.mc4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Weiss, H. J., V. T. Turitto, and H. R. Baumgartner. "FACTORS INFLUENCING FIBRIN DEPOSITION ON SUBENDOTHELIUM." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642950.

Full text
Abstract:
During the past several years, we have initiated studies to determine the role of plasma factors and platelets, and the properties of the blood vessel, which influence the activation of the coagulation mechanism on the subendothelium. Studies were performed by exposing everted segments of de-endothelialized rabbit aorta, mounted in a perfusion chamber, to non-anticoagulated human blood for 5 to 10 minutes under a range of flow conditions, and measuring fibrin and platelet deposition on the subendothelium, and fibrinopepstide A (FPA) levels in post-chamber blood. In normal subjects, platelet deposition increased progressively with increasing shear rates (50-2600 sec-1 ), whereas fibrin deposition and FPA levels decreased sharply at shear rates greater than 650 sec-1 . To examine the role of plasma coagulation factors, we utilized a shear rate of 650 sec-1 to study patients with severe deficiencies of factors XII, XI, IX or VIII. In contrast to the partial thromboplastin time (PTT), which was most strikingly abnormal in patients with factor XII or XI deficiency, fibrin deposition and FPA levels were greater in patients deficient in factor XII or XI than in those with factor VIII or IX deficiency. In addition, we observed smaller platelet thrombi in hemophilia (but not afibrinogenemia), suggesting that thrombin influenced the formation of platelet thrombi under these shear conditions. The findings suggested that tissue factor-Vila activation of factor IX could be important in mediating fibrin deposition on subendothelium and might explain why patients with factor XII deficiency (and some with factor XI deficiency) do not bleed. Initial studies to demonstrate tissue factor activity in subendothelium were inconclusive. More recently, utilizing shorter (1.5, 2 and 3 min) perfusion periods, we have observed decreased fibrin deposition and FPA levels in patients with factor VII deficiency and we have obtained further support for the presence of tissue factor in subendothelium in experiments utilizing a monoclonal antibody to tissue factor. Our studies suggest that activation of factor IX by tissue factor-Vila could account for the results obtained in patients with plasma coagulation defects. Direct experimental verification of this hypothesis will require more extensive studies on the kinetics governing the activation of coagulatjon factors on the subendothelium. In subsequent studies, we examined the role of platelets in mediating fibrin deposition. At a shear rate of 650 sec-1 we found (utilizing patients with thrombocytopenia) that platelets were required for fibrin deposition ; little or no fibrin was deposited on the subendothelium when platelet adhesion was less than 4%, corresponding to blood platelet counts less than 5000/ul. Studies performed in patients with functional platelet disorders provided additional information on the specific platelet properties that contribute to fibrin deposition at this shear rate. Decreased fibrin deposition was observed in a patient with Scott Syndrome, a disorder characterized by an impaired capacity of the platelets to catalyze the conversion of factor X to factor Xa (in the presence of factor IXa and VIII) and prothrombin to thrombin (in the presence of factor Va), the latter defect owing to a decreased factor Xa-binding capacity of the platelets. In contrast to the findings in Scott Syndrome, both fibrin deposition and FPA values were completely normal (and possibly increased) in patients with glycoprotein Ilb/IIIa deficiency. In patients with glycoprotein lb deficiency, the major defect was an impaired association of fibrin with platelets, but not subendothelium. The findings in patients with functional platelet disorders indicate that a monolayer of platelets (including those deficient in glycoprotein Ilb/IIIa) is completely active in promoting fibrin deposition on subendothelium. In addition, they suggest that an agent capable of inducing a platelet defect similar to that observed in Scott Syndrome might prevent platelet-fibrin thrombi at shear rates (200-800 sec-1 ) comparable to those in the coronary circulation. Studies performed at a variety of shear rates in both normal subject^ and patients with platelet disorders suggested that, under the conditions used, platelets were essential for fibrin formation at intermediate (650 sec-1 ), but not low (50 sec-1 ) shear rates. Since platelets have been shown to bind activated coagulation proteins (such as factor Xa, Va, and IXa) to their surface, the presence of adherent platelets on the subendothelium could, with increasing shear rates, serve to maintain activated coagulation proteins in the .boundary layer at a concentration that would otherwise be reduced through convective diffusion in their absence. Thus, at low shear rates (50 sec-1 ), the concentration of activated coagulation factors in the boundary layer might be sufficient to support fibrin deposition despite the absence of platelets, whereas at very high shear rates (2,600 sec-1 and above), even the presence of platelets is insufficient to maintain the required concentration. The shear-dependent defect of fibrin formation that we observed in Scott Syndrome is consistent with such a theory. The results of our various studies demonstrate the complex role of blood flow, plasma coagulation factors, specific platelet properties, and the procoagulant properties (tissue factor) of the vessel in mediating subendothelium-induced coagulation and suggest further experiments for studying the mechanisms involved.
APA, Harvard, Vancouver, ISO, and other styles
9

Arcovito, Giuseppe, F. A. Bassi, and Marco De Spirito. "Relaxation dynamic measurements in fibrin networks." In OE/LASE'93: Optics, Electro-Optics, & Laser Applications in Science& Engineering, edited by Ralph J. Nossal, Robert Pecora, and Alexander V. Priezzhev. SPIE, 1993. http://dx.doi.org/10.1117/12.148374.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

De Spirito, M., G. Arcovito, F. Andreasi Bassi, F. Ferri, and M. Rocco. "Internal dynamics of semiflexibles fibrin networks." In The 8th tohwa university international symposium on slow dynamics in complex systems. AIP, 1999. http://dx.doi.org/10.1063/1.58556.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Fibin"

1

Silva, Igor Iuco Castro da. Platelet-Rich Fibrin: A Versatile Purpose for Alveolar Ridge Preservation. Science Repository, July 2019. http://dx.doi.org/10.31487/j.dobcr.2019.03.05.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Moraschini, Vittorio, Richard Miron, and Anton Sculean. Use of Platelet-Rich Fibrin for the treatment of intrabony and furcation defects: A systematic review and meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, July 2020. http://dx.doi.org/10.37766/inplasy2020.7.0117.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Chan, M., M. Ballinger, and P. Owczarski. A computer code to estimate accidental fire and radioactive airborne releases in nuclear fuel cycle facilities: User's manual for FIRIN. Office of Scientific and Technical Information (OSTI), February 1989. http://dx.doi.org/10.2172/6329003.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Chen, Chen, Peng Chen, Xia Liu, and Hua Li. Combined 5-Fluorouracil and Low Molecular Weight Heparin for the Prevention of Postoperative Proliferative Vitreoretinopathy in Patients with Retinal Detachment. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, August 2021. http://dx.doi.org/10.37766/inplasy2021.8.0117.

Full text
Abstract:
Review question / Objective: The aim of this meta-analysis is to evaluate the efficacy and safety of intraoperative infusion of combined 5-fluorouracil and low molecular weight heparin (LMWH) for the prevention of postoperative proliferative vitreoretinopathy in patients with retinal detachment. Condition being studied: Postoperative proliferative vitreoretinopathy (PVR) is the primary cause of failure of retinal reattachment surgery. 5-fluorouracil (5-FU) inhibits the proliferation of fibroblasts, and suppresses collagen contraction. On the other hand, heparin reduces fibrin exudation, and inhibits the adhesion and migration of retinal pigment epithelial cells. We conduct this comprehensive literature search and meta-analysis to address whether intraoperative infusion of combined 5-FU and LWMH improves the primary success rate of pars plana vitrectomy, as well as reduces postoperative PVR. Our study aims to provide clinical evidence for retinal surgeons concerning their choice of intraoperative medication.
APA, Harvard, Vancouver, ISO, and other styles
5

Meza-Mauricio, Jonathan, Camila Pinheiro Furquim, Antonella Geldres, Gerardo Mendoza-Azpur, Belen Retamal-Valdes, and Marcelo Faveri. Is the use of platelet rich fibrin effective in the healing, pain and control of post-operative bleeding of palatine area after harvesting free gingival graft? A systematic review of randomized clinical studies. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, January 2021. http://dx.doi.org/10.37766/inplasy2021.1.0037.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Meza-Mauricio, Jonathan, Camila Pinheiro Furquim, Antonella Geldres, Gerardo Mendoza- Azpur, Belen Retamal-Valdes, Vittorio Moraschini, and Marcelo Faveri. Is the use of platelet rich fibrin effective in the healing, pain and control of post-operative bleeding of palatine area after harvesting free gingival graft? A systematic review of randomized clinical studies. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, January 2021. http://dx.doi.org/10.37766/inplasy2021.1.0113.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Floodflow characteristics of Filbin Creek for pre- and post-construction conditions, 1986, at North Charleston, South Carolina. US Geological Survey, 1987. http://dx.doi.org/10.3133/wri874157.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Fibin' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography