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Relevant bibliographies by topics / Proteins in blood coagulation

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Academic literature on the topic 'Proteins in blood coagulation'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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Journal articles on the topic "Proteins in blood coagulation"

1

SUZUKI, KOJI. "Blood coagulation control proteins." Nihon Naika Gakkai Zasshi 83, no. 4 (1994): 646–53. http://dx.doi.org/10.2169/naika.83.646.

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Patthy, László. "Evolutionary Assembly of Blood Coagulation Proteins." Seminars in Thrombosis and Hemostasis 16, no. 03 (July 1990): 245–59. http://dx.doi.org/10.1055/s-2007-1002677.

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Xu, Li-Chong, James W. Bauer, and Christopher A. Siedlecki. "Proteins, platelets, and blood coagulation at biomaterial interfaces." Colloids and Surfaces B: Biointerfaces 124 (December 2014): 49–68. http://dx.doi.org/10.1016/j.colsurfb.2014.09.040.

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Sonawani, Archana, Pravin Nilawe, Ram Shankar Barai, and Susan Idicula-Thomas. "ClotBase: a knowledgebase on proteins involved in blood coagulation." Blood 116, no. 5 (August 5, 2010): 855–56. http://dx.doi.org/10.1182/blood-2010-04-282616.

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Gryshchuk, Volodymyr, and Natalya Galagan. "Silica Nanoparticles Effects on Blood Coagulation Proteins and Platelets." Biochemistry Research International 2016 (2016): 1–6. http://dx.doi.org/10.1155/2016/2959414.

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Interaction of nanoparticles with the blood coagulation is important prior to their using as the drug carriers or therapeutic agents. The aim of present work was studying of the primary effects of silica nanoparticles (SiNPs) on haemostasisin vitro. We studied the effect of SiNPs on blood coagulation directly estimating the activation of prothrombin and factor X and to verify any possible effect of SiNPs on human platelets. It was shown that SiNPs shortened coagulation time in APTT and PT tests and increased the activation of factor X induced by RVV possibly due to the sorption of intrinsic pathway factors on their surface. SiNPs inhibited the aggregation of platelet rich plasma induced by ADP but in the same time partially activated platelets as it was shown using flow cytometry. The possibility of SiNPs usage in nanomedicine is strongly dependant on their final concentration in bloodstream and the size of the particles that are used. However SiNPs are extremely promising as the haemostatic agents for preventing the blood loss after damage.

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HANSSON, K., and J. STENFLO. "Post-translational modifications in proteins involved in blood coagulation." Journal of Thrombosis and Haemostasis 3, no. 12 (December 2005): 2633–48. http://dx.doi.org/10.1111/j.1538-7836.2005.01478.x.

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Harlos, K., S. K. Holland, C. W. G. Boys, A. I. Burgess, M. P. Esnouf, and C. C. F. Blake. "Vitamin K-dependent blood coagulation proteins form hetero-dimers." Nature 330, no. 6143 (November 1987): 82–84. http://dx.doi.org/10.1038/330082a0.

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Shibeko, A. M., A. N. Balandina, N. A. Podoplelova, and M. A. Panteleev. "Current trends in blood coagulation studies." Pediatric Hematology/Oncology and Immunopathology 19, no. 3 (October 9, 2020): 144–50. http://dx.doi.org/10.24287/1726-1708-2020-19-3-144-150.

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Blood coagulation occurs in flow or stasis conditions, it involves components of cell hemostasis and enzymatic cascades of reactions; it serves to stop bleeding yet it can lead to life-threatening blood thrombi. Despite the fact that a complete list of coagulation proteins was well known for decades, in recent years numerous facts has accumulated about its structure and regulation. All that has led to the creation of new methods for diagnosing of blood coagulation disorders and methods for their correction. Congenital and acquired coagulation disorders are still an acute clinical problem. This review shows modern ideas about the structure and functioning of the blood coagulation system in various conditions.

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Engelmann, Beatrice, Julia Bischof, Anne-Luise Dirk, Nele Friedrich, Elke Hammer, Thomas Thiele, Dagmar Führer, Georg Homuth, Georg Brabant, and Uwe Völker. "Effect of Experimental Thyrotoxicosis onto Blood Coagulation: A Proteomics Study." European Thyroid Journal 4, Suppl. 1 (2015): 119–24. http://dx.doi.org/10.1159/000381769.

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Background: Hyperthyroidism is known to induce a hypercoagulable state. It stimulates plasma levels of procoagulative factors and reduces fibrinolytic activity. So far most of the data have been derived from patients with endogenous hyperthyroidism with a wide variability in the underlying pathogenesis and severity of the disease. Objectives: In this study we experimentally induced thyrotoxicosis in healthy volunteers to explore the effects of thyroxine excess on the plasma proteome. Using a shotgun proteomics approach, the abundance of plasma proteins was monitored before, during and after thyrotoxicosis. Methods: Sixteen healthy male subjects were sampled at baseline, 4 and 8 weeks under 250 µg/day thyroxine p.o., as well as 4 and 8 weeks after stopping the application. Plasma proteins were analyzed after depletion of 6 high-abundance proteins (MARS6) by LC-ESI-MS/MS mass spectrometry. Mass spectrometric raw data were processed using a label-free, intensity-based workflow. Subsequently, the linear dependence between protein abundances and fT4 levels were calculated using a Pearson correlation. Results: All subjects developed biochemical thyrotoxicosis, and this effect was reversed within the first 4 weeks of follow-up. None of the volunteers noticed any subjective symptoms. Levels of 10 proteins involved in the coagulation cascade specifically correlated with fT4, supporting an influence of thyroid hormone levels on blood coagulation even at nonpathological levels. Conclusions: The results suggest that experimental thyrotoxicosis exerts selective and specific thyroxine-induced effects on coagulation markers. Our study design allows assessment of thyroid hormone effects on plasma protein levels without secondary effects of other diseases or therapies.

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Vannakambadi, Ganesh, Magnus Höök, Pietro Speziale, and Jose Rivera. "Fibrinogen-binding proteins of Gram-positive bacteria." Thrombosis and Haemostasis 98, no. 09 (2007): 503–11. http://dx.doi.org/10.1160/th07-03-0233.

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SummaryFibrinogen (Fg), the major clotting protein in blood plasma, plays key roles in blood coagulation and thrombosis. In addition, this 340 kD glycoprotein is a stress inducible protein; its synthesis is dramatically upregulated during inflammation or under exposure to stress such systemic infections.This regulation of Fg expression indicates that Fg also participates in the host defense system against infections. In fact, a number of reported studies have demonstrated the involvement of both the intrinsic and extrinsic pathways of coagulation; the thrombotic and the fibrinolytic systems in the pathophysiology of infectious diseases. It is, therefore, perhaps not surprising that many pathogenic bacteria can interact with Fg and manipulate its biology.This review focuses on the major Fg-binding proteins (Fgbps) from Gram-positive bacteria with an emphasis on those that are known to have an effect on coagulation and thrombosis

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Dissertations / Theses on the topic "Proteins in blood coagulation"

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Smith, Brian. "Protein models in blood coagulation and fibrinolysis." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.239327.

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Carlsson, Karin. "Tissue Factor in Complex : Studies of interactions between blood coagulation proteins." Doctoral thesis, Linköpings universitet, Biokemi, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-63688.

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Many biological processes rely on specific protein-protein interactions, for example immune responses, cell signaling, transcription, and blood coagulation. Blood coagulation is initiated when a vessel wall is damaged, exposing tissue factor (TF) to the circulating factor VII/factor VIIa (FVII/FVIIa) which results in the formation of the TF:FVIIa complex and thereby the initiation of blood coagulation. One of the substrates for the TF:FVIIa complex is factor X (FX), which is activated to factor Xa (FXa), subsequently leading to a series of reactions resulting in clot formation. Tissue factor pathway inhibitor (TFPI) is the major physiological inhibitor of the sTF:FVIIa complex, involved in regulation of coagulation by forming the TF:FVIIa:FXa:TFPI complex. Occasionally, the blood coagulation mechanism malfunctions, resulting in conditions such as the inability to stop bleeding or thrombosis. The fact that TF is the main initiator of the coagulation makes this an interesting protein to study, in the hunt for means to interfere with players involved in the blood clotting process. Throughout the studies included in this thesis the site-directed labeling technique is utilized to attach spectroscopic probes to cysteines, introduced at specific positions by mutagenesis, in the protein of interest. These fluorescent or spin-probes are sensitive for changes in their immediate environment and can thus, for example be used to monitor protein-protein complex formation and conformational changes. No complete structure has been obtained as yet for the large complex involving sTF, FVIIa, FXa, and TFPI. Therefore, we introduced a fluorescent probe at specific positions in soluble tissue factor (sTF) and the changes in fluorescence emission were detected upon sTF:FVIIa:FXa:TFPI complex formation. From these measurements it was concluded that not only parts of the C-terminal domain of sTF (TF2), but also residues in the N-terminal domain (TF1) are involved in binding to FXa in the quaternary complex. In order to investigate conformational changes occurring in the extended interface between sTF and FVIIa upon binding of different inhibitors spectroscopic probes were introduced in sTF, in the vicinity of the interaction region. From the obtained data it was concluded that the exosite-binding inhibitor E-76 induces equivalent structural changes at the interface of sTF and the protease domain (PD) of FVIIa, as do the active-site inhibitors FFR and TFPI, i.e. makes the region around the active-site more compact. Binding of these inhibitors shows similar effects despite their differences in size, binding site, and inhibitory mechanism. In addition, the Ca2+ dependence of the formation of the sTF:FVIIa complex was studied. Association between sTF and FVIIa during Ca2+ titration begins by Ca2+ binding to the first EGF-like domain of FVIIa. However, Ca2+ saturation of the γ-carboxyglutamic acid-rich (Gla) domain of FVIIa is required for complete sTF:FVIIa complex formation, and we were also able to detect that a Gla domain with vacant Ca2+ sites hinders the docking to sTF. Finally, we investigated the structural changes of free inhibited FVIIa upon sTF and Ca2+ binding by FRET and quenching measurements. From this it was concluded that inhibited FVIIa does not seem to undergo large global structural changes upon binding to sTF, when taking the dynamics of free FVIIa into account. However, Ca2+ binding induces minor local conformational changes in the active-site region of the PD of inhibited FVIIa and subsequent binding of sTF causesfurther structural rearrangements in this area.

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Brown, Anthony James Moginie. "Studies of the molecular structures of the blood coagulation fibrinolytic proteins." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294268.

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Holland, Susan Katrina. "X-ray studies of proteins of medical and biological interest." Thesis, University of Oxford, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.236327.

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Kassaar, Omar. "Structural and functional studies of histidine-rich glycoprotein in relation to its roles in angiogenesis and coagulation." Thesis, University of St Andrews, 2014. http://hdl.handle.net/10023/5548.

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Histidine-rich glycoprotein (HRG) is a plasma protein that regulates key cardiovascular processes such as coagulation, angiogenesis and immune response. The protein consists of six distinct functional domains: two N-terminal domains (N1 and N2), two proline-rich regions (PRR1 and PRR2), a central histidine-rich region (HRR) and a C-terminal domain. The HRR binds Zn²⁺, which alters the affinity of HRG towards various ligands including the anticoagulant, heparin. A key aim of this study was to structurally characterise HRG. The 1.93 Å crystal structure of the HRG N2 domain presented here represents the first crystallographic snapshot of the molecule. The N2 domain is cystatin-like and N-glycosylated at Asn184. An S-glutathionyl adduct was observed at Cys185, providing in vivo evidence that release of an anti-angiogenic HRR/PRR fragment is controlled in part by a redox mechanism, representing a novel further role for GSH in regulation of angiogenesis. Since Zn²⁺ regulates some of the functions of HRG, the dynamics of Zn²⁺ in plasma were investigated using a combination of ITC, ELISA and thrombin assay systems. Zn²⁺ is normally associated with albumin in circulation, but its ability to bind Zn²⁺ is allosterically inhibited upon fatty acids binding to albumin. Elevated plasma fatty acid levels are associated with some disease states. It is proposed that this may alter the proportion of Zn²⁺ bound to HRG, which could in turn activate thrombin to promote coagulation. These studies provide evidence to suggest that Zn²⁺-dependent activation of HRG (following fatty acid binding to albumin) may play a role in the development of haemostatic complications in susceptible individuals. Finally, the Zn²⁺ binding ability of albumin was probed in order to locate unidentified sites using recombinant albumin mutants. H9A, H67A, E252A, D256A and H288A mutants all exhibited diminished Zn²⁺ binding ability, indicating that these residues are involved directly or indirectly in Zn²⁺ binding.

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Grunkemeier, John M. "Effect of adhesion proteins and surface chemistry on the procoagulant state of adherent platelets /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/8087.

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Popescu, Narcis Ioan. "Regulation of procoagulant activity of cell surface tissue factor." Oklahoma City : [s.n.], 2010.

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8

Jenkins, Meredith E. "An examination of the human fibrinogen-like protein2 sequence variations and genetic expression by human endothelial cells /." unrestricted, 2005. http://etd.gsu.edu/theses/available/etd-07222005-093438/.

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Thesis (M.S.)--Georgia State University, 2005.
Title from title screen. Roberta Attanasio, committee chair; P.C. Tai, W.C. Hooper, committee members. Electronic text (57 p. : col. ill.) : digital, PDF file. Description based on contents viewed Aug. 15, 2007. Includes bibliographical references (p. 55-57).

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Evington, J. R. N. "Protein-polysaccaride interactions and the catalysis of the thrombin/antithrombin reaction." Thesis, University of Bristol, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.370826.

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Bakker, Harm Marten. "Accelerin the activated form(s) of human blood coagulation factor V /." Maastricht : Maastricht : Rijksuniversiteit Limburg ; University Library, Maastricht University [Host], 1994. http://arno.unimaas.nl/show.cgi?fid=6954.

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Books on the topic "Proteins in blood coagulation"

1

W, Hoyer Leon, and Drohan William, eds. Recombinant technology in hemostasis and thrombosis. New York: Plenum Press, 1991.

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Lindsay, Yvonne M. Reduction in the thrombogenicity of biomaterials using contrasting adsorbed proteins. Dublin: University College Dublin, 1996.

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International Workshop on NovoSeven (1998 Frankfurt am Main, Germany). Recombinant factor VIIa: RFVIIa : update on clinical experiences. Neckargemünd: Weller Verlag, 1999.

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Matthias, Fritz Reinhard. Blood Coagulation Disorders. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-83098-3.

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Sibinga, C. Th Smit, P. C. Das, and P. M. Mannucci, eds. Coagulation and Blood Transfusion. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3900-1.

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6

Coagulation-inflammation interface: Coagulation assembly on leukocytes. New York: Chapman & Hall, 1997.

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Essential guide to blood coagulation. 2nd ed. Chichester, West Sussex: Wiley-Blackwell, 2013.

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Antovic, Jovan P., and Margareta Blombäck, eds. Essential Guide to Blood Coagulation. Oxford, UK: Wiley-Blackwell, 2009. http://dx.doi.org/10.1002/9781444314465.

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Antovic, Jovan P., and Margareta Blombäck, eds. Essential Guide to Blood Coagulation. Oxford, UK: John Wiley & Sons Ltd, 2013. http://dx.doi.org/10.1002/9781118327517.

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Altieri, Dario C. The coagulation-inflammation interface: Coagulation assembly on leukocytes. New York: Springer, 1997.

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Book chapters on the topic "Proteins in blood coagulation"

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Hoyer, L. W. "Structure-Function Relationships of Human Coagulation Proteins." In Coagulation and Blood Transfusion, 17–28. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3900-1_2.

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Pflugshaupt, R., and G. Kurt. "Effect of Blood Collection on the Hemostatic Potential of Coagulation Proteins." In Coagulation and Blood Transfusion, 39–48. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3900-1_4.

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Ghosh, S. "Blood Products: Coagulation Protein Preparations." In Handbook of Blood and Blood Products, 29–36. London: Macmillan Education UK, 1988. http://dx.doi.org/10.1007/978-1-349-19289-2_5.

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Pflugshaupt, R., P. Baillod, W. Etter, and G. Kurt. "Protein C and S in Swiss Blood Donors." In Coagulation and Blood Transfusion, 187–91. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3900-1_18.

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Bauer, C., and W. Wuillemin. "Blood, Plasma Proteins, Coagulation, Fibrinolysis, and Thrombocyte Function." In Comprehensive Human Physiology, 1651–77. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-60946-6_84.

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Suzuki, Koji, and Junji Nishioka. "Recognition Sites for Thrombomodulin, Procoagulant and Anticoagulant Proteins around the Active Center of Thrombin." In Current Aspects of Blood Coagulation, Fibrinolysis, and Platelets, 17–22. Tokyo: Springer Japan, 1993. http://dx.doi.org/10.1007/978-4-431-68323-0_3.

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Ichinose, Akitada, and Earl W. Davie. "Repeating Domains in the Plasma Proteins Participating in Blood Coagulation and Fibrinolysis." In Methods in Protein Sequence Analysis, 285–92. Basel: Birkhäuser Basel, 1991. http://dx.doi.org/10.1007/978-3-0348-5678-2_29.

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Egberg, Nils. "Blood Coagulation and the Gastrointestinal Microflora: Vitamin-K Dependent Plasma Proteins." In The Regulatory and Protective Role of the Normal Microflora, 331–44. London: Palgrave Macmillan UK, 1989. http://dx.doi.org/10.1007/978-1-349-10723-0_21.

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Takayama, Masaomi, Keiichi Isaka, Yoshichika Suzuki, Hitoshi Funayama, Yasunobu Suzuki, Kiyoshi Akiya, and Hans Bohn. "Placental Protein 19 in Clinical Blood Coagulation Disorder." In Perinatal Thrombosis and Hemostasis, 155–63. Tokyo: Springer Japan, 1991. http://dx.doi.org/10.1007/978-4-431-65871-9_16.

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Morita, Takashi. "Blood Coagulation Factor IX/Factor X-Binding Protein." In Toxins and Hemostasis, 167–77. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9295-3_11.

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Conference papers on the topic "Proteins in blood coagulation"

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Hassan, H. J., A. Leonardi, C. Chelucci, R. Guerriero, P. M. Mannucci, and C. Peschle. "EXPRESSION IN ONTOGENESIS OF HUMAN BLOOD COAGULATION FACTORS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644610.

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We have analyzed the expression of several blood coagulation factors (IX, VIII, X, fibrinogen chains) and inhibitors (antithrombin III, protein C) in human embryonic and fetal livers, obtained from legal abortions at 6-11 week post-conception. The age was established by morphologic staging and particularly crown-rump lenght measurement.Total cellular RNA was isolated from partially purified hepatocytes or total liver homogenate using the guanidine isothiocyanate method. Poly(A)+ RNA was selected by oligodT cellulose chromatography. The size and the number of the embryonic and fetal transcripts are equivalent to those observed in adult liver, as evaluated by Northern blot analysis of total or poly(A)+ RNA hybridized to human cDNA probes.The level of coagulation factor transcripts in embryonic and fetal liver was evaluated by dot hybridization of total RNA (0.5-10 ug), as compared to RNA extracted from normal adult liver biopsies. The expression of blood coagulation factors in embryos is generally reduced for all factors, but at a different degree. In 5-11 wk liver, the level of factor IX is 5-10% of that observed in adults, while fibrinogen, protein C, antithrombin III RNA level rises from 25 to 50% and factor X is expressed at a level comparable to that observed in adult liver.We conclude that during these stages of development blood coagulation factors are expressed according to three different time, curves, possibly due to the effect of different types of regulatory mechanisms.

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Vehar, G. A. "THE PRESENT STATE OF GENE TECHNOLOGY IN THE MANUFACTURE OF HUMAN COAGULATION PROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644755.

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The production of pharmaceuticals from human plasma that are useful in the treatment of bleeding disorders had its beginning with the development of the Cohn fractionation procedure in the 1940's. As a result of these advances, concentrates became available for the treatment of the hemophilias. Although of low purity and subject to contamination by hepatitis virus, the availability of these compounds resulted in dramatic improvements in the life expectancy and quality of life of afflicted individuals. The numerous problems associated with production of pharmaceuticals from pooled plasma made these products obvious goals for recombinant DNA technology as soon as the commercial aspects of the field became apparent. The subsequent contamination of blood products with the AIDS virus has resulted in an urgent need for a production source that is independent of human plasma. Several industrial and academic laboratories have cloned the cDNA's for human factors VIII and IX. In addition to these proteins, the utility of factor Vila in the treatment of hemophiliacs with inhibitors has shown promise. Efforts to develop a recombinant preparation of factor Vila are at a comparable stage of development as factors VIII and IX. Continuing efforts have resulted in the successful expression of these recombinant proteins in mammalian cell lines, thereby successfully completing the first steps of commercial development.Although much interest has focused upon the theoretical superiority of recombinant proteins as therapeutics, one must keep in mind that there are numerous developmental aspects of large-scale production and regulatory issues that must be addressed and solved before these drugs will be available. The coagulation proteins are complex glycoproteins that will in all probability require mammalian cell cell culture in order to produce functional proteins. The fact that these preparations will be administered over the lifetime of the patient serves to reinforce that the recombinant products be as similar to the natural proteins as possible, further supporting the concept of mammalian cell expression systems.Regulatory approval of a recombinant product are fundamentally no different than those for any other product in regards to efficacy, potency, purity, and identity. There are, however, additional considerations that must be addressed in the production of recombinant cell culture derived biologies. These relate to the possible presence in the final product of pathogenic and tumorigenic agents, and possible contamination by cell culture and cell substrate compounds. A detailed characterization of the production cell line will therefore be required, including identification and characterization of any associated viral particles. These cells must be capable of being reproducibly grown, while maintaining protein production, on ascale (tens of thousands of liters) suitable to meet the market demand of the specific protein. Apurification process must be established capable of handling the resulting large volumes of feedstock, generating a protein preparation of high purity (greater than 99% pure). Numerous assays must be developed to quantitate the purity and identity of the resulting recombinant pharmaceutical on a lot by lot basis.Studies to date have shown that recombinant forms of factors VIII and IX, produced by laboratory processes, are very similar to the plasma-derived forms as assessed by a variety of in vitro and in vivo tests. Although these results are promising, the ultimate safety and efficacy testing of these drugs will have to await the initiation of human clinical trials. Such studies will have to await the successful completion of the certain regulatory concerns. Clinical trials should begin within the near future, hopefully leading to a source of these products independent of pooled human plasma.

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Aurousseau, M. H., V. Eclache, and J. Amiral. "CLINICAL RELEVANCE OF D.DIMER AND COAGULATION INHIBITORS IN LIVER CIRRHOSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643140.

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D.Dimer was measured by a latex agglutination assay and an enzyme immunoassay (E.I.A.) in 25 patients suffering from liver cirrhosis. High levels of D.Dimer (> 500 ng/ml) were found in 13/25 patients’ plasma, by the latex test as well as EIA. Fibrinogen Degradation Products (FDP), measured by the Merskey method, were present in 7/25 samples, whereas soluble fibrin monomer complexes were only detected in 2/25 patients. In both cases, D.Dimer was elevated and FDP were in the normal range. Only one patient developped a Disseminated Intravascular Coagulation (DIC). None of the others had any thromboembolic event.Anticoagulant plasma proteins, Protein C (pC), total and free Protein S (pS) and Antithrombin III (AT III), were measured, in these patients, using the Laurell method.Mean values measured were :AT III : 50 % ± 16 total pS : 69 % ± 20pC : 38 % ± 28 free pS : 63 % ± 30Using immunoassays, pS showed the lowest decrease, in comparison to the other coagulation inhibitors.These values were compared to some procoagulant activities : prothrombin, factors VII ± X and factor V.4 good correlation was observed between AT III and prothrombin (r = 0.752 p < 0.01), whereas a poorer one was obtained between pC and factors VII and X (r = 0.455 p < 0.02). There was no correlation between pC and pS, nor between pC and factor V. Despite marked decrease of coagulation inhibitors in liver cirrhosis, low incidence of thrombotic accidents was observed (1/25) probably due to a parallel decreased synthesis of procoagulant factors. However, an in vivo blood activation associated to a reactive fibrinolysis was evidenced by measurement of pathological levels of D.Dimer in 13/25 patients. In this way, D.Dimer is a more sensitive and specific marker, than total FDP, to evaluate blood activation in liver cirrhosis. D.Di Test allows a rapid estimation and gives similar results to the EIA method.

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Corbett, Scott C., Amin Ajdari, Ahmet U. Coskun, and Hamid N.-Hashemi. "Effect of Blood Viscosity on Thrombosis Potential Near a Step Wall Transition." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206629.

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Thrombosis and hemolysis are two problems encountered when processing blood in artificial organs. Physical factors of blood flow alone can influence the interaction of proteins and cells with the vessel wall, induce platelet aggregation and influence coagulation factors responsible for the formation of thrombus, even in the absence of chemical factors in the blood. These physical factors are related to the magnitude of the shear rate/stress, the duration of the applied force and the local geometry. Specifically, high blood shear rates (or stress) lead to damage (hemolysis, platelet activation), while low shear rates lead to stagnation and thrombosis [1].

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Van Haarlem, L. J. M., H. C. Hemker, B. A. M. Soute, and C. Vermeer. "GLA-CONTAINING PROTEINS FROM CALCIFIED HUMAN ATHEROSCLEROTIC PLAQUES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643747.

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Vitamin K-dependent carboxylase activity has been detected in human andbovine vessel wall. Studies comparingthe carboxylases from liver and vessel wall revealed that the enzyme systems may be regarded as isoenzymes withwidely different substrate specificities. The carboxylated product of vessel wall carboxylase has not yet been identified, but it seems plausible that it will be found amongst the Gla-containing proteins which are abundantly present in calcified atherosclerotic plaques (Gla= gammacarboxyglutamicacid, the abnormal amino acid formed by vitamin K-dependent carboxylase). Therefore we have started to characterize the protein constituents of hardened atherosclerotic plaques.The calcified areas from human aortae were solubilized in EDTA and the proteins extracted were partly purified by batch-wise adsorption onto QAE and elution with high salt. The crudeplaque-extract did not contain prothrombin, factor X or protein C. This excludes the possibility that Gla-containing coagulation factors are bound non-specifically from blood. Osteocalcin accounted for 20% of the total amount of protein-bound Gla-residues.Another Gla-containing protein waspurified from the crude plaque-extract by employing high performance liquid chromatography (HPLC). Gel filtration yielded a Gla-rich protein with anapparent Mr of 25 kD. In vitro boththe crude plaque-extract and the purified Gla-containing protein strongly inhibited the precipitation of calcium phosphate and calcium carbonate. A similar effect was not found with humanserum albumin nor with a thermallydecarboxylated plaque-extract. If also in vivo the Gla-containing proteinsproduced by vessel wall carboxylase prevent the precipitation of calcium salts remains to be investigated.

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6

Church, W., T. Messier, P. Howard, J. Amiral, D. Meyer, and K. Mam. "A SHARED EPITOPE ON HUMAN PROTEIN C, FACTOR X, FACTOR VII, AND PROTTOBIN DEFINED BY A MONOCLONAL ANTIBODY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643937.

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A monoclonal antibody prepared against hunan protein C (HPC) was found to react with several other vitamin K-dependent blood proteins. Using a competitive inhibition solid-phase radioinminoassay with HPC, binding of 125I-HPC to the antibody was inhibited by purified prothrombin, Factor X, and Factor VII in addition to protein C. Other vitamin K-dependent proteins including Factor IX, protein S, and bone-GLA protein did not compete for binding of 125I-HPC to the antibody. The effect of calciun ion on the binding of antibody to 125I-HPC was examined in a solid-phase imnunoassay system with the antibody bound to rabbit anti-mouse inminoglobulin adsorbed to microtiter plates. In the presence of 5 mM calciun ion, radiolabeled protein C did not bind to the antibody; radiolabeled protein C did bind, however, in the presence of 5 nM EDTA suggesting that the epitope is expressed only after removal of calciun ion. The antibody bound to prothrombin and to decarboxylated prothrombin after adsorption of the antigens onto nitrocellulose indicating that the presence of GLA was not required for antibody binding. Iimunoblotting of proteins which were reduced, the peptides separated by SDS-PAGE, and transferred to nitrocellulose showed that the antibody reacts with a determinant found on the light chains of protein C and Factor X and with prothrombin Fragment 1. Comparison of the protein sequences of protein C light chain, Factor X light chain, Factor VII, and prothrombin Fragment 1 identified a segment of amino acid sequence that is highly conserved in all four proteins and might contain the antigenic site. The monoclonal antibody thus defines an antigenic determinant which is masked by calcium ion and is found on the surface of several related, yet different coagulation proteins. This antibody should prove useful in understanding the evolutionary relationships amongst the vitamin K-dependent proteins and also in understanding the effect of calcium ion on the structure of protein C, Factor X, prothrombin, Factor VII and possibly other related proteins. (Supported by NIH grant MHLBI HL35058)

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7

Kehrel, B., L. Ballesian, R. Kokott, W. Stenzinger, K. J. Clemetson, and J. Van De Loo. "REVERSIBLE DEFICIENCY OF INTACT THROMBOSPONDIN AND MEMBRANE GLYCOPROTEIN Ia IN PLATELETS OF A PATIENT WITH A BLEEDING DISORDER." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644654.

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A 52 year old female patient with a severe bleeding tendency since the age of two was studied. Her history revealed recurrent petechial bleedings, two severe postoperative haemorrhagic episodes and intensivemenstrual bleedings which required blood transfusions. Coagulation studies ruled out any coagulation disorder including von Willebrand's disease. Platelet count and morphology(using light and electron microscopy) were normal. The patient had prolonged bleeding times (up to 15 min). Her platelets aggregated normally in response to ADP, arachidonic acid, thrombin, ionophore A 23187, epinephrine and ristocetin. In contrast, platelet aggregation in the presence of collagen and wheat germ agglutinin could only be achieved with very high doses of these agonists. Repeated analyses of the patient's platelet proteins by two-dimensional 0'Farrel gel electrophoresis followed by silver staining or blotting onto nitrocellulose and staining with a mixture of peroxidase-coupled lectins showed that glycoprotein la and intact thrombospondin were absent. An immunoblot for thrombospondin showed several proteins with lower molecular weight than thrombospondin. Preincubation of the patient's platelets with thrombospondin normalized collagen-induced aggregation.At a recent follow-up examination the patient had no petechial bleedings. Platelet protein analysis revealed thatintact thrombospondin and glycoprotein la were present. These results suggest that both glycoprotein la and thrombospondin have essential roles in collagen-induced platelet aggregation.

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8

D'Angelo, A., F. Gilardoni, M. P. Seveso, P. Poli, R. Quintavalle, and C. Manotti. "ANTICOAGULANT AND ANTIGENIC LEVELS OF PROTEIN C AND PROTEIN S IN PATIENTS ON STABILIZED ORAL ANTICOAGULANT TREATMENT." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644286.

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Isolated deficiencies of protein C and protein S, two vitamin K-dependent plasma proteins, constitute about 70% of the congenital abnormalities of blood coagulation observed in patients with recurrent venous thrombosis beLow the age of 40. The laboratory diagnosis of congenital deficiency of these proteins represents a major problem since a large proportion of patients are on oral anticoagulation (OA) at the time the deficiencies are suspected.Under these circumstances the availability of a reference interval obtained in patients on stabilized OA has proven useful.Functional (C) and antigenic levels (Ag) of protein C, protein S, factor IX and II were estimated in 136 patients on stabilized OA, subdivided according to the degree of anticoagulation (Internatio nal Normalized Ratio, INR).The results indicate that with increasing anticoagulation the activity levels of all the vitamin K-dependent factors decrease to a greater extent than the corresponding antigenic levels. At variance with the other factors, total protein S antigen levels are only moderately reduced by OA with protein S anticoagulant activi ty comparing well to factor IX clotting activity. These data suggest the possibility of identifying both quantitative and qualita tive deficiencies of protein C and protein S in patients on oral anticoagulant treatment.

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Basciano, Christopher A., Julie H. Y. Ng, Ender A. Finol, and Clement Kleinstreuer. "A Relation Between Particle Hemodynamics and Intraluminal Thrombus Formation in Abdominal Aortic Aneurysms." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-204721.

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Abdominal aortic aneurysms (AAAs) are local dilations of the aorta below the renal arteries where the lumen diameter is ≥ 1.5 times the normal diameter of the healthy blood vessel. Ruptured aneurysms are the 13th leading cause of death in the US [1]. In approximately 75% of all AAAs, a particle-deposition layer forms adjacent to the arterial wall within the lumen called the intra-luminal thrombus (ILT). The thrombus composition has been shown to be a fibrin structure composed of blood cells, platelets, blood proteins, and other cellular debris [2]. Additionally, Yamazumi et al. [3] have presented data that suggest AAA morphology is associated with an elevated state of blood coagulation and fibrinolysis within the aneurysm.

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10

Hach-Wunderle, V., R. Walter-Fincke, H. K. Beck, and I. Scharrer. "FAMILY STUDIES OF PATIENTS WITH RECURRENT VENOUS THROMBOSES AND INHERITED DISORDERS OF BLOOD COAGULATION OR FIBRINOLYSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643045.

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Several defects of the coagulation and/or fibrinolytic system have been found to be associated with venous thromboembolism. In young patients with recurrent thromboses or a positive family history, an inherited disorder should be excluded535 young patients with venous thromboses, phlebitis and/or pulmonary embolism were investigated from 1980 until 1986. The first thrombotic event had occurred at an age of less than 45 years.An inborn disorder of the blood coagulation or fibrinolytic system was found in 18 families. Most of them (n=13/18) had a positive family history. In all families either thromboses had occurred in at least one member (n=12/18) and/or the defect could be detected in one of them (n=12/18)Most often we found a deficiency of antithfombin III (n=6). A deficiency of protein C (type I) was detected in 3 and a deficiency of protein S in 5 families. In one patient a combined deficiency of anti thrombin III, protein C and protein S was found. Extensive family studies revealed a deficiency of antithrombin III in the grandmother of the patient, who suffered from arterial thrombosis. A deficiency of plasminogen and an abnormal plasminogen molecule were detected in 2 other families. Defective release of t-PA could be demonstrated in 3 members of one investigated family up to nowSeme family members with either defects of protein C, protein S or plasminogen as well as a defective release of t-PA lack thrombotic events. Furthermore thromboses of mesenteric veins occurred in 2 of 6 patients with anti thrombin III deficiency and in 1 of 5 patients with protein S deficiency. Superficial vein thromboses were mainly found in patients with protein C- or protein S-deficiency

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Reports on the topic "Proteins in blood coagulation"

1

Viksna, Ludmila, Oksana Kolesova, Aleksandrs Kolesovs, Ieva Vanaga, and Seda Arutjunana. Clinical characteristics of COVID-19 patients (Latvia, Spring 2020). Rīga Stradiņš University, December 2020. http://dx.doi.org/10.25143/fk2/hnmlhh.

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Data include following variables: Demographics, epidemiological history, comorbidities, diagnosis, complications, and symptoms on admission to the hospital. Also, body’s temperature and SpO2. Blood cells: white cells count (WBC), neutrophils (Neu), lymphocytes (Ly), eosinophils (Eo) and monocytes (Mo), percentages of segmented and banded neutrophils, erythrocytes (RBC), platelet count (PLT), hemoglobin (Hb), and hematocrit (HCT); Inflammatory indicators: erythrocyte sedimentation rate (ESR) and C-reactive protein (CRP); Tissue damage indicators: alanine aminotransferase (ALT), lactate dehydrogenase (LDH), and troponin T (TnT); Electrolytes: potassium and sodium concentration; Renal function indicators: creatinine and glomerular filtration rate (GFR); Coagulation tests: D-dimer, prothrombin time, and prothrombin index on admission to the hospital.

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Crandall, Craig G., Victor Convertino, and Andre Cap. Effects of Thermal Status on Markers of Blood Coagulation During Simulated Hemorrhage. Fort Belvoir, VA: Defense Technical Information Center, April 2013. http://dx.doi.org/10.21236/ada577217.

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Crandall, Craig G., Victor Convertino, and Andre Cap. Effects of Thermal Status on Markers of Blood Coagulation During Simulated Hemorrhage. Fort Belvoir, VA: Defense Technical Information Center, April 2014. http://dx.doi.org/10.21236/ada600964.

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Crandall, Craig G., Victor Convertino, and Andre Cap. Effects of Thermal Status on Markers of Blood Coagulation During Simulated Hemorrhage. Fort Belvoir, VA: Defense Technical Information Center, April 2015. http://dx.doi.org/10.21236/ada616416.

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Koder, Ronald L. Designed Proteins as Optimized Oxygen Carriers for Artificial Blood. Fort Belvoir, VA: Defense Technical Information Center, February 2014. http://dx.doi.org/10.21236/ada622324.

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Koder, Ronald L. Designed Proteins as Optimized Oxygen Carriers for Artificial Blood. Fort Belvoir, VA: Defense Technical Information Center, February 2013. http://dx.doi.org/10.21236/ada574241.

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7

Gay, Carol V. Unique Proteins Expressed by Blood Vessels in Skeletal Sites Colonized by Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, August 2005. http://dx.doi.org/10.21236/ada446316.

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Gay, Carol V. Unique Proteins Expressed by Blood Vessels in Skeletal Sites Colonized by Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, August 2004. http://dx.doi.org/10.21236/ada429149.

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Gay, Carol V. Unique Proteins Expressed by Blood Vessels in Skeletal Sites Colonized by Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, August 2006. http://dx.doi.org/10.21236/ada461608.

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Arnett, Clint, Justin Lange, Ashley Boyd, Martin Page, and Donald Cropek. Expression and secretion of active Moringa oleifera coagulant protein in Bacillus subtilis. Engineer Research and Development Center (U.S.), August 2021. http://dx.doi.org/10.21079/11681/41546.

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Cationic polypeptide proteins found in the seeds of the tropical plant Moringa oleifera have coagulation efficiencies similar to aluminum and ferric sulfates without their recalcitrant nature. Although these proteins possess great potential to augment or replace traditional coagulants in water treatment, harvesting active protein from seeds is laborious and not cost-effective. Here, we describe an alternative method to express and secrete active M. oleifera coagulant protein (MO) in Bacillus subtilis. A plasmid library containing the MO gene and 173 different types of secretory signal peptides was created and cloned into B. subtilis strain RIK1285. Fourteen of 440 clones screened were capable of secreting MO with yields ranging from 55 to 122 mg/L of growth medium. The coagulant activity of the highest MO secreting clone was evaluated when grown on Luria broth, and cell-free medium from the culture was shown to reduce turbidity in a buffered kaolin suspension by approximately 90% compared with controls without the MO gene. The clone was also capable of secreting active MO when grown on a defined synthetic wastewater supplemented with 0.5% tryptone. Cell-free medium from the strain harboring the MO gene demonstrated more than a 2-fold reduction in turbidity compared with controls. Additionally, no significant amount of MO was observed without the addition of the synthetic wastewater, suggesting that it served as a source of nutrients for the effective expression and translocation of MO into the medium.

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