Academic literature on the topic 'Beta 2-glycoprotein I'
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Journal articles on the topic "Beta 2-glycoprotein I"
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Inanc, M. "beta 2-Glycoprotein I and anti-beta 2-glycoprotein I antibodies: where are we now?" Rheumatology 36, no. 12 (December 1, 1997): 1247–57. http://dx.doi.org/10.1093/rheumatology/36.12.1247.
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Schousboe, I. "beta 2-Glycoprotein I: a plasma inhibitor of the contact activation of the intrinsic blood coagulation pathway." Blood 66, no. 5 (November 1, 1985): 1086–91. http://dx.doi.org/10.1182/blood.v66.5.1086.1086.
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Abstract The general hypothesis for the biological function of beta 2- glycoprotein I is that it neutralizes all negatively charged macromolecules that might enter the bloodstream and diminishes unwanted activation of the blood coagulation. In the present study we report that beta 2-glycoprotein I inhibits the activation of the contact phase system of the intrinsic pathway of blood coagulation. Activation was accomplished by an ellagic acid-phospholipid suspension (Cephotest) and measured by the appearance of amidolytic activity using the chromogenic substrate H-D-Pro-Phe-Arg-p-nitroanilide (S-2302). This inhibitory effect of beta 2-glycoprotein I was observed both when Cephotest was preincubated with beta 2-glycoprotein I and when the amount of beta 2- glycoprotein I in plasma was increased by addition of beta 2- glycoprotein I to either normal or beta 2-glycoprotein I-deficient plasma. The inhibitory effect of beta 2-glycoprotein I on the contact phase activation could be one of the physiological functions of this protein.
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Schousboe, I. "beta 2-Glycoprotein I: a plasma inhibitor of the contact activation of the intrinsic blood coagulation pathway." Blood 66, no. 5 (November 1, 1985): 1086–91. http://dx.doi.org/10.1182/blood.v66.5.1086.bloodjournal6651086.
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The general hypothesis for the biological function of beta 2- glycoprotein I is that it neutralizes all negatively charged macromolecules that might enter the bloodstream and diminishes unwanted activation of the blood coagulation. In the present study we report that beta 2-glycoprotein I inhibits the activation of the contact phase system of the intrinsic pathway of blood coagulation. Activation was accomplished by an ellagic acid-phospholipid suspension (Cephotest) and measured by the appearance of amidolytic activity using the chromogenic substrate H-D-Pro-Phe-Arg-p-nitroanilide (S-2302). This inhibitory effect of beta 2-glycoprotein I was observed both when Cephotest was preincubated with beta 2-glycoprotein I and when the amount of beta 2- glycoprotein I in plasma was increased by addition of beta 2- glycoprotein I to either normal or beta 2-glycoprotein I-deficient plasma. The inhibitory effect of beta 2-glycoprotein I on the contact phase activation could be one of the physiological functions of this protein.
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Arad, Ariela, Richard A. Furie, Barbara C. Furie, and Bruce Furie. "Affinity-Purified Anti-Beta-2 Glycoprotein-1 Antibodies from a Patient with Lupus Anticoagulant-Associated Thrombosis Amplify Thrombus Formation in the Living Mouse." Blood 114, no. 22 (November 20, 2009): 146. http://dx.doi.org/10.1182/blood.v114.22.146.146.
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Abstract Abstract 146 Antiphospholipid syndrome (APS) is characterized by thrombosis, recurrent fetal loss and the presence of the lupus anticoagulant, anticardiolipin antibodies or anti-beta-2 glycoprotein 1 antibodies. Sera from patients with APS contain polyclonal antibodies that bind to various plasma proteins including beta-2 glycoprotein 1. Although beta-2 glycoprotein 1 antibodies have been well-documented as a biomarker for the diagnosis of APS, their direct role in the pathogenesis of thrombosis is unknown. Here, we have demonstrated using intravital microscopy that purified anti-beta-2 glycoprotein 1 antibodies isolated from the serum of a patient with APS greatly amplify thrombus size following laser-induced vessel wall injury in live mice. A patient with systemic lupus and APS complicated by pulmonary embolism was studied. IgG was isolated from serum by affinity chromatography using a Protein A/G column. Anti-beta-2 glycoprotein 1 antibodies in the IgG fraction were affinity-purified using homogeneous beta-2 glycoprotein 1 covalently bound to CNBr-activated agarose beads. Purified anti-beta-2 glycoprotein 1 antibodies were eluted at low pH. Patient IgG depleted of anti-beta-2 glycoprotein 1 antibodies was obtained by repeated chromatography over the beta-2 glycoprotein 1 column. The effects of (a) purified anti-beta-2 glycoprotein 1 antibodies, (b) anti-beta-2 glycoprotein 1 antibody-depleted patient IgG, and (c) IgG from normal human sera on thrombus formation were studied quantitatively in the live mouse. Intravital microscopy was performed using the cremaster muscle as a vascular window, and thrombus formation was initiated by laser injury to the arteriolar wall. Five minutes prior to vessel wall injury, purified anti-beta-2 glycoprotein 1 antibodies, anti-beta-2 glycoprotein 1 antibody-depleted patient IgG, or normal human IgG were infused via a jugular catheter. Platelet thrombus size was determined by widefield microscopy and Alexa 647-conjugated Fab fragments of an anti-CD 41 monoclonal antibody. Up to 10 thrombi were generated per mouse, and the median integrated fluorescence for 25-30 thrombi determined. Infusion of anti-beta-2 glycoprotein 1 antibodies increased thrombus size in a dose-dependent manner. Infusion of purified anti-beta-2 glycoprotein 1 antibodies at 0.12 μg/g mouse and 0.40 μg/g mouse increased thrombus size by about 18-fold and 122-fold respectively over thrombi formed in untreated mice. However, anti-beta-2 glycoprotein 1 antibody-depleted patient IgG and normal human IgG did not affect platelet thrombus size. These results indicate that the anti-beta-2 glycoprotein 1 antibodies isolated from APS patient serum are responsible for markedly increased thrombus size in this thrombosis model. The target cellular antigen of the anti-beta-2 glycoprotein 1 antibodies and the mechanism of enhanced thrombus formation remain unknown. However, these results provide evidence that anti-beta-2 glycoprotein 1 antibodies are not only a marker but are directly involved in the pathogenesis of thrombosis. This in vivo animal model offers an approach to identifying inhibitors of anti-beta-2 glycoprotein 1-mediated thrombosis. Disclosures: No relevant conflicts of interest to declare.
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Kertesz, Z., B. B. Yu, A. Steinkasserer, H. Haupt, A. Benham, and R. B. Sim. "Characterization of binding of human β2-glycoprotein I to cardiolipin." Biochemical Journal 310, no. 1 (August 15, 1995): 315–21. http://dx.doi.org/10.1042/bj3100315.
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beta 2-Glycoprotein I-cardiolipin complexes are reported to be a target antigen for the binding of a subset of anti-phospholipid antibodies. The characteristics of binding of beta 2-glycoprotein I to cardiolipin are reported in this paper. Binding at neutral pH is specific, saturable, dependent on ionic strength and independent of bivalent cation. Binding at low pH is qualitatively different from that at neutral pH, and is not dependent on ionic strength. Denaturation of beta 2-glycoprotein I by heat inactivation and reduction/alkylation indicates that beta 2-glycoprotein I-cardiolipin interaction does not require the native three-dimensional structure of beta 2-glycoprotein I, implying that a linear sequence motif may be responsible. Modification of amino acid residues by KCNO treatment completely destroys binding capacity, indicating crucial involvement of lysine residues in binding of beta 2-glycoprotein I to cardiolipin. Complement factor H, which has some similar highly charged linear sequence motifs to beta 2-glycoprotein I and is composed of the same type of protein module, was found to bind to cardiolipin and inhibit the binding of beta 2-glycoprotein I to cardiolipin. Three different lysine-rich segments of the fifth domain of beta 2-glycoprotein I may be involved in binding to cardiolipin.
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Wittevrongel, C., M. Vanrusselt, M. Hoylaerts, J. Vermylen, and J. Arnout. "Beta-2-glycoprotein I Dependent Lupus Anticoagulants Form Stable Bivalent Antibody Beta-2-Glycoprotein I Complexes on Phospholipid Surfaces." Thrombosis and Haemostasis 79, no. 01 (1998): 79–86. http://dx.doi.org/10.1055/s-0037-1614224.
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SummaryThe precise mechanism by which Beta-2-glycoprotein I (β2GPI-) dependent lupus anticoagulants lengthen phospholipid-dependent clotting reactions is still poorly understood. In order to study this, murine monoclonal antibodies (moabs) against human β2GPI were raised. Eight of the 21 anti-β2GPI moabs, obtained from 2 fusions, fulfilled the criteria for lupus anticoagulant (LA) activity as tested with a variety of sensitive screening assays and confirmatory tests. Seven moabs did not influence any clotting test. The LA positive moabs were found to compete for similar or closely spaced epitopes on immobilized β2GPI. Two moabs with potent LA activity (moabs 22 F 6 and 22 B 3) and 1 moab without LA activity (moab 16 B 3) were selected to study the interaction between antibody, β2GPI and phospholipid. Interactions were investigated by real-time biospecific interaction analysis (BIA) based on plasmon surface resonance technology on a BIA-core instrument using a sensor chip coated with phospholipid. When 22 F 6, the moab with the most pronounced LA activity, was allowed to interact with the phospholipid surface at concentrations between 0 and 400 nmol/l, no appreciable binding could be detected. Likewise, no binding could be measured when β2GPI at concentrations between 0 and 400 nmol/l was passed over the phospholipid coated sensor chip. Combinations of β2GPI and 22 F 6 resulted in significant binding. Similar results were obtained with 22 B 3, another moab with LA activity. A LA negative Moab, 16 B 3, did not cause binding of antibody-β2GPI complexes. Fab’ fragments, derived from moab 22 F 6, inhibited the binding of β2GPI-22 F 6 and β2GPI-22 B 3 in a concentration dependent way, indicating that only bivalent β2GPI-antibody complexes bind with high affinity to phospholipids. Fab’ fragments, derived from moab 22 F 6, also inhibited the LA effect of moabs 22 F 6 and 22 B 3 in diluted plasma. In summary, these experiments indicate that the β2GPI-dependent LA effect depends on the formation of bivalent β2GPI-antibody complexes on phospholipid surfaces.
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Marai, Ibrahim, Angela Tincani, Genesio Balestrieri, and Yehuda Shoenfeld. "Anticardiolipin and anti-beta-2-glycoprotein I antibodies." Autoimmunity 38, no. 1 (February 2005): 33–38. http://dx.doi.org/10.1080/08916930400022608.
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Božič, B., S. Čučnik, T. Kveder, and B. Rozman. "Avidity of anti-beta-2-glycoprotein I antibodies." Autoimmunity Reviews 4, no. 5 (June 2005): 303–8. http://dx.doi.org/10.1016/j.autrev.2005.01.001.
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Meroni, P. L., D. Mari, D. Monti, R. Coppola, M. Capri, S. Salvioli, A. Tincani, R. Gerli, and C. Franceschi. "Anti-beta 2 glycoprotein I antibodies in centenarians." Experimental Gerontology 39, no. 10 (October 2004): 1459–65. http://dx.doi.org/10.1016/j.exger.2004.08.003.
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Matsuda, J., N. Saitoh, M. Gotoh, K. Gohchi, and M. Tsukamoto. "Prevalence of beta 2-glycoprotein I antibody in systemic lupus erythematosus patients with beta 2-glycoprotein I dependent antiphospholipid antibodies." Annals of the Rheumatic Diseases 54, no. 1 (January 1, 1995): 73–75. http://dx.doi.org/10.1136/ard.54.1.73.
Full textDissertations / Theses on the topic "Beta 2-glycoprotein I"
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Giannakopoulos, Bill Clinical School St George Hospital Faculty of Medicine UNSW. "Investigations on beta 2-glycoprotein I and antiphospholipid antibodies." Publisher:University of New South Wales. Clinical School - St George Hospital, 2008. http://handle.unsw.edu.au/1959.4/41440.
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An outline of the work contained in this thesis is presented. The first chapter is a critical review of the literature pertaining to the pathophysiological mechanisms operational with regards to the antiphospholipid syndrome (APS). The syndrome is characterised by venous and arterial thrombosis, and recurrent fetal loss, in association with the persistent presence of antibodies targeting the main autoantigen beta 2-glycoprotein I (β2GPI). The second chapter reviews the literature delineating the diverse physiological functions of β2GPI, and then relates them to its role in our current understanding of the pathophysiology of APS. The third chapter presents a critical review of the evidence base for the diagnosis and management of APS. The fourth chapter describes the interaction between β2GPI and the glycoprotein Ib alpha (GPIbα) subunit of the platelet receptor GPIb-IX-V. GPIbα is an important platelet adhesion receptor, which mediates multiple additional functions on the platelet surface, including binding coagulation factor XI (FXI). The implication of the interaction between β2GPI and GPIbα on platelet activation and the release of thromboxane in the presence of anti-β2GPI antibodies is explored, as well as the intracellular pathways via which this activation occurs. The relevance of these findings to understanding APS pathogenesis, in particular thrombosis, is discussed. The fifth chapter delineates the interaction between the fifth domain of β2GPI and FXI and its activated form factor XIa (FXIa). The ability of FXIa to cleave β2GPI between lysine (Lys) 317 and threonine (Thr) 318, and modulate its function is reported. The sixth chapter describes the ability of β2GPI to inhibit FXIa autoproteolytic hydrolysis at the specific FXIa residues arginine (Arg) 507, Arg532 and Lys539. This interaction with β2GPI stabilizes FXIa activity over time, and leads to enhanced FXIa mediated fibrin formation. This is a novel physiological function of β2GPI with important implications. Recent epidemiological studies by others have emphasized the critical role of FXIa in pathological thrombus propagation. The seventh chapter defines the relevance of the FXIa residues Arg507, Arg532 and Lys539 to FXIa mediated inactivation by the main FXIa inhibitor Protease Nexin 2 (PN2), and by Antithrombin III (ATIII). Insights into future directions for research are presented and discussed within each individual chapter.
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Rahgozar, Soheila Clinical School St George Hospital Faculty of Medicine UNSW. "Studies on beta 2 glycoprotein I and antiphospholipid antibodies." Publisher:University of New South Wales. Clinical School - St George Hospital, 2008. http://handle.unsw.edu.au/1959.4/41475.
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Beta 2 glycoprotein I (β2GPI) is a major antigenic target in antiphospholipid syndrome (APS). In vitro studies suggest that it may have multifaceted physiological functions, as it displays both anticoagulant and procoagulant properties. Beta 2GPI may bind to FXI and serve as a regulator of FXI activation by thrombin. The possible interaction of β2GPI with thrombin is investigated using enzyme linked immunosorbent assays and surface plasmon resonance based studies. It is demonstrated for the first time that domain V of β2GPI is involved in direct binding to thrombin, and exosites I and II on thrombin take part in this interaction. It is also shown that cleavage of β2GPI at Lys317-Thr318 does not interrupt this binding. A quaternary complex is proposed on the surface of activated platelets in which β2GPI may colocalise with FXI and thrombin to regulate FXIa generation. The effect of anti-β2GPI monoclonal antibodies (mAbs) were investigated on this system using 8 anti-β2GPI mAbs directed against domain I. Anti-β2GPI Abs potentiate the suppressing activity of β2GPI on FXI activation by thrombin. Moreover, they restore the inhibitory effect of clipped β2GPI on this system. The current study demonstrates for the first time a novel biological consequence of thrombin interaction with β2GPI. The effect of β2GPI on thrombin inactivation by the serine protease inhibitor heparin cofactor II (HCII) is investigated using chromogenic assays, platelet aggregation studies, and the platelet release response. The current work shows that β2GPI protects thrombin from inactivation by HCII/Heparin. This ability is modulated by the cleavage of β2GPI. A ternary structure is proposed between β2GPI, thrombin and heparin which may limit the N-terminus of HCII to exosite I therefore inhibit thrombin inactivation by HCII. The effect of anti-β2GPI Abs is examined in this system using patient polyclonal IgGs and a murine anti-β2GPI mAb. Anti-β2GPI Abs potentiate the protective effect of β2GPI on thrombin inhibition by HCII/Heparin. In view of the importance of HCII in regulating thrombin activity within the arterial wall, disruption of this function by β2GPI/anti-β2GPI Ab complexes may be particularly relevant in arterial thrombosis in APS. Beta 2 glycoprotein I (β2GPI) is a major antigenic target in antiphospholipid syndrome (APS). In vitro studies suggest that it may have multifaceted physiological functions, as it displays both anticoagulant and procoagulant properties. Beta 2GPI may bind to FXI and serve as a regulator of FXI activation by thrombin. The possible interaction of β2GPI with thrombin is investigated using enzyme linked immunosorbent assays and surface plasmon resonance based studies. It is demonstrated for the first time that domain V of β2GPI is involved in direct binding to thrombin, and exosites I and II on thrombin take part in this interaction. It is also shown that cleavage of β2GPI at Lys317-Thr318 does not interrupt this binding. A quaternary complex is proposed on the surface of activated platelets in which β2GPI may colocalise with FXI and thrombin to regulate FXIa generation. The effect of anti-β2GPI monoclonal antibodies (mAbs) were investigated on this system using 8 anti-β2GPI mAbs directed against domain I. Anti-β2GPI Abs potentiate the suppressing activity of β2GPI on FXI activation by thrombin. Moreover, they restore the inhibitory effect of clipped β2GPI on this system. The current study demonstrates for the first time a novel biological consequence of thrombin interaction with β2GPI. The effect of β2GPI on thrombin inactivation by the serine protease inhibitor heparin cofactor II (HCII) is investigated using chromogenic assays, platelet aggregation studies, and the platelet release response. The current work shows that β2GPI protects thrombin from inactivation by HCII/Heparin. This ability is modulated by the cleavage of β2GPI. A ternary structure is proposed between β2GPI, thrombin and heparin which may limit the N-terminus of HCII to exosite I therefore inhibit thrombin inactivation by HCII. The effect of anti-β2GPI Abs is examined in this system using patient polyclonal IgGs and a murine anti-β2GPI mAb. Anti-β2GPI Abs potentiate the protective effect of β2GPI on thrombin inhibition by HCII/Heparin. In view of the importance of HCII in regulating thrombin activity within the arterial wall, disruption of this function by β2GPI/anti-β2GPI Ab complexes may be particularly relevant in arterial thrombosis in APS.
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Olsson, Ola. "Affinity capillary electrophoresis of Beta-2-glycoprotein I and Anionic phospholipids." Thesis, Karlstad University, Faculty of Technology and Science, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:kau:diva-6113.
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McNally, Tracy Jane. "An investigation of the role of antiphospholipid antibodies and #beta#2 glycoprotein-I in the modulation of haemostasis." Thesis, University College London (University of London), 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.339151.
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Baldavira, Camila Machado. "Estudo do efeito da beta 2-glicoproteína I no desenvolvimento da rede vascular de membrana corioalantóica de embriões de galinha." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/5/5160/tde-28072017-134103/.
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Angiogênese é a formação de novos capilares a partir de vasos pré-existentes, mediada por eventos de sinalização bioquímica que determinam proliferação, migração, diferenciação e morte celular e controlam crescimento e remodelação tecidual. A beta2-glicoproteína I (beta2GPI) é uma proteína plasmática com ação sobre a função vascular e a aterogênese. Monomêros de beta2GPI apresentam efeito anti-inflamatório e anticoagulante; a clivagem enzimática favorece sua dimerização e induz o aparecimento de efeitos opostos. Resultados anteriores mostraram que monômeros e dímeros de beta2GPI têm efeitos diferentes sobre a proliferação e a diferenciação de células endoteliais em culturas bidimensionais utilizadas como modelo de angiogênese. Os monômeros e dímeros de beta2GPI foram obtidos por purificação fracionada e caracterizada por SDS-PAGE e ELISA, como descrito. Neste trabalho, foram utilizadas culturas tridimensionais de células humanas vasculares de cordão umbilical (HUVEC) sobre Matrigel foram utilizadas para identificar efeitos de monômeros e dímeros da beta2GPI sobre a proliferação, migração e formação de estruturas de interação celular in vitro. O monômero de ?2GPI atuou como um fator de diferenciação endotelial dependente da densidade de plaqueamento, induzindo nas culturas tridimensionais de HUVECs a formação de fenótipos alongados, prolongamentos e estruturas de interação célula-célula. A fração dimérica modulou negativamente a proliferação de HUVECs. A membrana corioalantóide (CAM) de embriões de galinha foi empregada para estudar efeitos da beta2GPI sobre a angiogênese. In ovo, o dímero de beta2GPI impediu a angiogênese e induziu a morte embrionária 48h após a exposição, enquanto o monômero permitiu o desenvolvimento do embrião até o 10º dia, apesar de induzir mudanças precoces no desenvolvimento dos vasos da membrana corioalantóide. As estruturas da microvasculatura foram analisadas através de uma abordagem morfológica quantitativa, baseada na classificação de padrões binários locais (LBP). Alvos moleculares de beta2GPI relatados anteriormente foram considerados como fonte dos efeitos observados in vitro e in ovo. Os resultados obtidos suportam dados anteriores sobre a inibição da via de sinalização de anexina-2/Akt pela beta2GPI. Adicionalmente, sugere-se a via de sinalização Notch como um alvo do efeito antiangiogênico de da beta2GPIAngiogenesis is the formation of new capillaries from pre-existing vessels, mediated by biochemical signaling events that determine proliferation, migration, differentiation and cell death, and control of tissue growth and remodeling. beta2-glycoprotein I (beta2GPI) is a plasma protein active on vascular function and atherogenesis. ?2GPI monomers present anti-inflammatory and anticoagulant effects. Enzymatic cleavage favors beta2GPI dimerization and induces the appearance of opposing effects. Previous results have shown that beta2GPI monomers and dimers induce different effects upon the proliferation and differentiation of endothelial cells in two-dimensional cultures used as an angiogenesis model. beta2GPI monomers and dimers were obtained by fractioned purification and characterized by SDS-PAGE and ELISA, as described. In this work, three-dimensional Human Umbilical Vein Endothelial Cells (HUVEC) cultures on Matrigel were used to investigate the effects of beta2GPI monomers and dimers upon proliferation, migration and in vitro formation of cellular interaction structures. The beta2GPI monomer performed as a density-dependent endothelial differentiation factor, inducing the formation of elongated phenotypes, membrane extensions and cell-cell interaction structures in three-dimensional HUVEC cultures; the dimeric fraction negatively modulated the proliferation and differentiation of HUVECs. The chorioallantoic membrane (CAM) of chicken embryos was employed to study the effects of beta2GPI upon angiogenesis. In ovo, the beta2GPI dimer prevented angiogenesis and induced embryonic death after 48h exposure, while the monomer allowed embryo development up to the 10th day, despite it induced early changes in the development of chorioallantoic membrane vessels. Microvasculature structures were evaluated through a quantitative morphology approach, based on local binary pattern classification. Previously reported molecular beta2GPI targets were then considered as the source of the observed effects in vitro and in ovo. The obtained results support previous data on the inhibition of the annexin-2/Akt signaling pathway by beta2GPI. Additionally, the Notch signaling pathway is suggested as a target of the antiangiogenic effect of beta2GPI
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Wagner, Alison F. Lysle Donald T. "Interactions between intracerebral human immunodeficiency virus-1 glycoprotein 120 and systemic heroin on expression of messenger ribonucleic acid mRNA of inducible nitric oxide synthase, interleukin-1[beta], tumor necrosis factor-[alpha], and cyclooxygenase-2 in hippocampus and cortex brain tissue of the Lewis rat." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2008. http://dc.lib.unc.edu/u?/etd,1893.
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Thesis (M.A.)--University of North Carolina at Chapel Hill, 2008.Title from electronic title page (viewed Dec. 11, 2008). "... in partial fulfillment of the requirements for the degree of Master of Arts in the Department of Psychology Behavioral Neuroscience." Discipline: Psychology; Department/School: Psychology. On t.p. and in abstract, [alpha] and [beta] are the Greek letters.
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Bordron, Anne. "Effets pathogènes des auto-anticorps anti-cellules endothéliales à l'encontre de leurs cellules cibles." Brest, 2000. http://www.theses.fr/2000BRES3105.
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WU, TING-YUAN, and 吳庭遠. "Analysis of the interactions of Tafazzin and Beta-2 Glycoprotein I with lipid membrane by hydrogen/deuterium exchange mass spectrometry." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/uqu7b2.
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碩士東海大學
化學系
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Hydrogen/deuterium exchange (HDX) coupled with mass spectrometry (ESI-MS) has been widely used to study the mechanisms of protein dynamics, domain structure, protein-ligand interactions and protein conformational changes. Beta 2 Glycoprotein I (β2GPI) is a membrane protein and it was discovered to be the major antigen for the antiphospholipid antibodies(aPL Abs) in the antiphospholipid syndrome. The β2GPI complex binds with antibody will interact with some receptors, such as annexin A2, TLR family, glycoprotein Ibα, LRP8 to induce inflammation and prothrombotic. Many studies have suggested that β2GPI is not recognized by aPL Abs in the blood circulation. When negatively charged protein surface become exposed, the domain V of β2GPI will bind to the surface and change conformation. Then the aPL Abs are able to recognize the epitope in domain I of β2GPI. Here, we prepared 1,2-dioleoyl-sn-glycero-3-phospho-L-serine(18:1DOPS) and cardiolipin (CL) vesicles to simulate anion surface membrane. The interactions of the β2GPI with the anion membrane vesicles were analyzed by hydrogen/deuterium exchange mass spectrometry (HDXMS). The exchange level of sequence 21-27 significantly increased after β2GPI interacted with DOPS for 10 min. This results indicated that the interaction between domain I and domain V decreased, which caused the sequence 21-27 protruding out of the circular shape of the protein structure. β2GPI still maintained the circular conformation while interacting with DOPS. The exchange levels of the highly accessible sequences 1-20, 53-77, 175-188, 259-268 and 294-306 slightly decreased due to the nonspecific adsorption between β2GPI and DOPS by electrostatic force and hydrogen bonds. After β2GPI interacted with CL 10 mins. The exchange amount of sequence 21-27 significantly increased. This result was same with DOPS, suggesting the perturbation of sequence 21-27 is a preliminary behavior caused by the phospholipid binding. After β2GPI interacted with CL for 30 min, the exchange levels in several sequences significantly increased, including 1-20, 21-27, 41-51, 70-86, 153-162, 191-198, 196-205, 273-279, 297-306 and 310-316.The increasing of 1-20, 21-27, 41-51, 297-306 and 310-316 indicated that domain I did not interact with domain V and these sequences have been exposed. The increasing deuteration levels in 70-86, 153-162, 191-198, 196-205 and 273-279 indicated β2GPI conformation changed from ring conformation to chain conformation, leading to the exposure of the inner region. Overall, β2GPI could not change the ring conformation while initial contact with lipid membrane, but sequence 21-27 will be exposed. β2GPI continued to drastically change its conformation from ring to chain conformation while staying on the lipid membrane surface.
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Hoffmann, Christof Herbert Wolfgang [Verfasser]. "Die Rolle der thrombozytären Kollagenrezeptoren Glycoprotein VI und α2β1-Integrin [Alpha-2-Beta-1-Integrin] für die Thrombozytenadhäsion und Thrombusformation an atheromatöser Plaque / Christof Herbert Wolfgang Hoffmann." 2008. http://d-nb.info/99322122X/34.
Full textBooks on the topic "Beta 2-glycoprotein I"
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Alchi, Bassam, and David Jayne. The patient with antiphospholipid syndrome with or without lupus. Edited by Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0164.
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Antiphospholipid syndrome (APS) is an autoimmune disorder characterized by recurrent arterial or venous thrombosis and/or pregnancy loss, accompanied by laboratory evidence of antiphospholipid antibodies (aPL), namely anticardiolipin antibodies (aCL), lupus anticoagulant (LA), and antibodies directed against beta-2 glycoprotein 1 (β2GP1). APS may occur as a ‘primary’ form, ‘antiphospholipid syndrome,’ without any known systemic disease or may occur in the context of systemic lupus erythematosus (SLE), ‘SLE-related APS’. APS may affect any organ system and displays a broad spectrum of thrombotic manifestations, ranging from isolated lower extremity deep vein thrombosis to the ‘thrombotic storm’ observed in catastrophic antiphospholipid syndrome. Less frequently, patients present with non-thrombotic manifestations (e.g. thrombocytopaenia, livedo reticularis, pulmonary hypertension, valvular heart disease, chorea, and recurrent fetal loss).The kidney is a major target organ in both primary and SLE-related APS. Renal involvement is typically caused by thrombosis occurring at any location within the renal vasculature, leading to diverse effects, depending on the size, type, and site of vessel involved. The renal manifestations of APS include renal artery stenosis and/or renovascular hypertension, renal infarction, APS nephropathy (APSN), renal vein thrombosis, allograft vasculopathy and vascular thrombosis, and thrombosis of dialysis access.Typical vascular lesions of APSN may be acute, the so-called thrombotic microangiopathy, and/or chronic, such as arteriosclerosis, fibrous intimal hyperplasia, tubular thyroidization, and focal cortical atrophy. The spectrum of renal lesions includes non-thrombotic conditions, such as glomerulonephritis. Furthermore, renal manifestations of APS may coexist with other pathologies, especially proliferative lupus nephritis.Early diagnosis of APS requires a high degree of clinical suspicion. The diagnosis requires one clinical (vascular thrombosis or pregnancy morbidity) and at least one laboratory (LA, aCL, and/or anti-β2GP1) criterion, positive on repeated testing.The aetiology of APS is not known. Although aPL are diagnostic of, and pathogenic in, APS, a ‘second hit’ (usually an inflammatory event) may trigger thrombosis in APS. The pathogenesis of the thrombotic tendency in APS remains to be elucidated, but may involve a combination of autoantibody-mediated dysregulation of coagulation, platelet activation, and endothelial injury.Treatment of APS remains centred on anticoagulation; however, it has also included the use of corticosteroids and other immunosuppressive therapy. The prognosis of patients with primary APS is variable and unpredictable. The presence of APS increases morbidity (renal and cerebral) and mortality of SLE patients.
Book chapters on the topic "Beta 2-glycoprotein I"
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Raby, Anne, Karen Moffat, and Mark Crowther. "Anticardiolipin Antibody and Anti-beta 2 Glycoprotein I Antibody Assays." In Haemostasis, 387–405. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-339-8_32.
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Mohammed Ali Jassim, Marwa, Majid Mohammed Mahmood, and Murtada Hafedh Hussein. "Human Herpetic Viruses and Immune Profiles." In Innate Immunity in Health and Disease. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96340.
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Herpesviruses are large, spherical, enveloped viral particles with linear double-stranded DNA genome. Herpesvirus virion consists of an icosahedral capsid containing viral DNA, surrounded by a protein layer called tegument, and enclosed by an envelope consisting of a lipid bilayer with various glycoproteins. Herpesviruses persist lifelong in their hosts after primary infection by establishing a latent infection interrupted recurrently by reactivations. The Herpesviridae family is divided into three subfamilies; α-herpesviruses, β-herpesviruses, and γ-herpesviruses based on the genome organization, sequence homology, and biological properties. There are eight human herpes viruses: Herpes simplex virus type 1 and 2 (HSV-1, −2) andVaricella-zoster virus (VZV), which belong to the α-herpesvirus subfamily; Human cytomegalovirus (HCMV), and Human herpesvirus type 6 and 7 (HHV-6,HHV-7), which belong to the β-herpesvirus subfamily; and Epstein–Barr virus (EBV) and Kaposi’s sarcoma-associated herpesvirus (KSHV) or Human herpesvirus 8 (HHV-8), which belong to the γ-herpesvirus subfamily. Within this chapter, we summarize the current knowledge about EBV and CMV, regarding their genome organization, structural characteristics, mehanisms of latency, types of infections, mechanisms of immune escape and prevention. Epstein–Barr Virus (EBV) genome encodes over 100 proteins, of which only (30) proteins are well characterized, including the proteins expressed during latent infection and lytic cycle proteins. Based on major variation in the EBNA-2 gene sequence, two types of EBV are recognized, EBV type 1 and 2. Epstein–Barr virus types occur worldwide and differ in their geographic distribution depending on the type of virus. EBV spreads most commonly through bodily fluids, especially saliva. However, EBV can also spread through blood, blood transfusions, and organ transplantations. The EBV is associated with many malignant diseases such as lymphomas, carcinomas, and also more benign such as infectious mononucleosis, chronic active infection. The EBV has also been suggested as a trigger/cofactor for some autoimmune diseases. Overall, 1–1.5% of the cancer burden worldwide is estimated to be attributable to EBV The latently infected human cancer cells express the most powerful monogenic proteins, LMP-1 and LMP-2(Latent Membrane Protein-1,-2), as well as Epstein–Barr Nuclear Antigens (EBNA) and two small RNAs called Epstein–Barr Encoded Small RNAs (EBERs). The EBV can evade the immune system by its gene products that interfering with both innate and adaptive immunity, these include EBV-encoded proteins as well as small noncoding RNAs with immune-evasive properties. Currently no vaccine is available, although there are few candidates under evaluation. Human cytomegalovirus (HCMV) is a ubiquitous beta herpesvirus type 5 with seroprevalence ranges between 60 to 100% in developing countries. CMV is spread from one person to another, usually by direct and prolonged contact with bodily fluids, mainly saliva, but it can be transmitted by genital secretions, blood transfusion and organ transplantation. In addition, CMV can be transmitted vertically from mother to child. CMV infection can result in severe disease for babies, people who receive solid organ transplants or bone marrow/stem cell transplants and people with severe immune suppression such as advanced human immunodeficiency virus (HIV) infection. The HCMV has several mechanisms of immune system evasion. It interferes with the initiation of adaptive immune responses, as well as prevent CD8+ and CD4+ T cell recognition interfering with the normal cellular MHC Class I and MHC Class II processing and presentation pathways. Challenges in developing a vaccine include adeptness of CMV in evading the immune system. Though several vaccine candidates are under investigation.
Conference papers on the topic "Beta 2-glycoprotein I"
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Mansour, MA, M. Badr, H. El Bebawi, and A. El Ghobarey. "AB0069 Anti beta 2 glycoprotein antibodies and thrombosis in sle patients." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.1223.
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Borodin, AG, EL Nassonov, AA Baranov, and NG Klukvina. "FRI0085 Anti-beta-2- glycoprotein i antibodies in systemic lupus erythematosus patients." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.1227.
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Hoffman, R., B. J. Roth, G. W. Sledge, J. Straneva, and J. Brandt. "ANALYSIS OF PHORBOL ESTER STIMULATED HUMAN MEGAKARYOCYTE DEVELOPMENT." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642951.
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The events that occur during the terminal maturation of human megakaryocytes are poorly characterized. To examine these events, a recently characterized human megakaryocytic cell line (EST-IU, Cancer Res. 46: 2155-2159, 1986) was exposed to 12-0-tetradecanoyl-phorbol-13-acetate (TPA), as well as 2 non-transforming phorbol esters (4 alpha phorbol and 4 beta phorbol 12 alpha, 13 alpha diacetate) at the identical concentrations. Morphologic changes, including cellular attachment to untreated plastic or glass, occurred within 4 hrs of treatment with TPA. Treatment of EST-IU cells with either of the 2 non-transforming phorbols (4-alpha phorbol, or 4-beta phorbol, 12-beta, 13-alpha diacetate) failed to change morphology, DNA content, or expression of surface membrane glycoproteins or alpha-granule constituents when compared to control cells. TPA treatment resulted, however, in j^rofound changes in adherence to plastic by the EST-IU cells, with an obvious dose-response relationship. At a 5 × 10-8 M TPA, cellular attachment was noted as early as 4 hours following treatment, agd was complete by 16 hours, at which time > 95% of treated cells were attached. Following TPA treatment at 5 × 10-8 M, a number of morphologic changes occurred, including marked cellular flattening, the appearance of extensive cytoplasmic budding, and the development of numerous filopodia. Cells treated with either of the non-transforming phorbols as assessed by propidium iodide staining and flow cytometric analysis failed to exhibit a change in ploidy, although TPA reproducibly altered this parameter of megakaryocyte development. Cells treated with 10-9 M TPA have approximately the same proportion of cells in the 4N and 8N peaks as control cells. Following exposure to 10-9 M and 10-8 M TPA, there was an apparent shift of cells out of the 4N peak to 8N and 16N levels, and even the appearance of a small percentage of 32N cells. The DNA content of TPA-treated cells was also assessed by Feulgen staining and microdensitome try. Those cells (5%) which failed to adhere following TPA treatment were analyzed separately, and showed a very different ploidy distribution than the adherent cell population. Over 85% of adherent cells have a ploidy > 16N, with some cells attaining the 128N level. Treatment of cells with either of the 2 non-transforming phorbols failed to affect the expression of Factor V, Factor VIIIrRAg, beta-throraboglobulin, fibrinogen, or platelet glycoproteins. Cells treated with 5 × 10-8 M TPA similarly do not significantly increse the expression of Factor V, fibrinogen, or beta-thromoglobulin over that observed in control cells. The expression of both Factor VIIIrRAg and platelet glycoproteins however, increase in TPA-treated cells. A similar increase in the expression of platelet glycoprotein Ilb/IIIA using the mouse monoclonal C17 was also observed. Those cells that express the highest levels of Factor VIII:RAg and platelet glycoproteins following phorbol treatment also demonstrated the highest ploidy levels and also are the largest cells as measured by forward angle light scatter during flow cytometry.These studies indicate that TPA treatment of EST-IU cells initiates a cascade of events characterized by cellular adherence, increases in cell size and DNA content, and enhanced expression of platelet glycoproteins and Factor VIIIrRAg. These events appear to occur in concert and closely resemble information that is available concerning maturation of normal rodent and human megakaryocytes. Although it is important to emphasize that EST-IU cells are leukemic and thus intrinsically different from normal human megakaryocytes, their availability and dynamic responses to TPA will provide an appropriate cellular model with which to study megakaryocyte maturation.
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Folts, J. D. "A MODEL OF ACUTE PLATELET THROMBUS FORMATION IN STENOSED CORONARY AND CAROTID ARTERIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643712.
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There is currently a great deal of interest in the diagnosis and treatment of unstable angina and silent ischemia.Many feel that these syndromes are due, in part, to periodic accumulation of platelet thrombi which subsequently embolize.In addition, anti-piatelet therapy is also considered necessary for patients after coronary artery bypass grafts (CABG'S), balloon angioplasty, and thrombolysis. Currently the two antiplatelet agents most commonly prescribed for the patient conditions mentioned above are aspirin (ASA), alone or in combination with dipyridamole (Dip). ASA reduces cardiac events in patients with unstable angina, and prolongs CABG graft patency. The addition of Dip to ASA therapy is very confusing since most studies done compared ASA + Dip to placebo. In several studies however,when an ASA group was compared to an ASA + Dip group there was no significant difference.We have developed and will describe ananimal model of coronary artery stenosis in the dog and the pig, or carotid arterystenosis in the monkey and the rabbit, with intimal damage, that simulates some ofthe conditions that exist in patients with coronary or carotid artery disease. The artery to be studied is dissected outand blood flow is continuously measured with an electromagnetic flowmeter probe. As acute platelet thrombus formation (APTF) developes in the stenosed lumen, the blood flow declines to low levels, producing ischemia until the thrombus emobolizesdistally resulting in abrupt restoration of blood flow. These cyclical flow reductions (CFR's), when they occur in the coronaries, produce ECG changes identical to those observed in patients with silent ischemia and unstable angina. They also produce significant transient regional dyskinesis of the ventricular wall, which resolves when blood flow is restored. Histologic examination of myocardial tissue in the bed distal to the stenosis shows focal areas of ischemic change presumably caused by the embolized platelet emboli.We have examined factors which exacerbate the size and frequency of these CFR"ssuch as; IV infusion of epinephrine (E) 0.4 μg/kg/min for 15 min, ventilating the animals with cigarette smoke, infusing nicotine IV, or placing chewing tobacco under the tongue.We have examined four groups of agentswhich prevent APTF in our model.1. Antiplatelet agents including ASA, indomethacin, ibuprofen and several other NSAI agentsas well as several experimental thromboxane synthetase inhibitors. These agents all block the production of TXA2and inhibit APTF in our model. Unfortunately the IV infusion of E reinstates APTtemporarily (by another biochemical pathway) until the E is metabolized. High (2-4 mg/kg) doses of Dip, alone or with sub threshold dose of ASA does nothing to I APTF.However,0.6mg/kg of chi orpromaz i ne abolishes APTF in all four species and protects agents renewal of APTF by E.2. Dietary Substances In our model, caffeine 10 mg/kg, or the extract from two garlic cloves, or enough ethanol to achieve a blood alcohol level of 0.07 mg% all significantly inhibit or abolish APTF in our model.3. Metabolic Inhibitors POCA, an oral hypoglycemic agent, which inhibits mitochondrial beta oxidation of fatty acids also inhibits APTF in our model possibly by reducing ATP production in the platelet.4. We have studied a monoclonal antibody(developed by Dr. Barry Coller) to the platelet I Ib�I I la glycoprotein receptor where fibrinogen binds platelets into aggregates and ultimately leads to APTF. This antibody 0.3 mg/kg/completely inhibits APTF, and also strongly inhibits in vitro platelet aggregation in response to either ADP or collagen given alone or each combined with E. This antibody is the most potent inhibitor of APTF that we have studied.