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Journal articles on the topic 'Beta 2-glycoprotein I'

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Published: 4 June 2021

Last updated: 18 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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.

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11

Brochado, Maria José Franco, José Fernando C. Figueiredo, Celso Teixeira Mendes-Junior, Paulo Louzada-Junior, Olivia Makiyama Kim, and Ana Maria Roselino. "Correlation between beta-2-glycoprotein I gene polymorphism and anti-beta-2 glycoprotein I antibodies in patients with multibacillary leprosy." Archives of Dermatological Research 302, no. 8 (February 7, 2010): 583–91. http://dx.doi.org/10.1007/s00403-010-1032-9.

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12

KABURAKI, Junichi, Masataka KUWANA, Mihoko YAMAMOTO, Shinichi KAWAI, Eiji MATSUURA, and Yasuo IKEDA. "Phospholipid-Dependent Anti-.BETA.2-Glycoprotein I (.BETA.2-GPI) Antibodies and Antiphospholipid Syndrome." Internal Medicine 35, no. 2 (1996): 105–10. http://dx.doi.org/10.2169/internalmedicine.35.105.

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13

Norden, A. G. W., L. M. Fulcher, M. Lapsley, and F. V. Flynn. "Excretion of beta 2-glycoprotein I (apolipoprotein H) in renal tubular disease." Clinical Chemistry 37, no. 1 (January 1, 1991): 74–77. http://dx.doi.org/10.1093/clinchem/37.1.74.

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Abstract beta 2-Glycoprotein I (beta 2GI) was identified as a major urinary protein excreted by patients with several renal tubular diseases, including adult Fanconi syndrome, nephrocalcinosis associated with autoimmune diseases, Lowe's syndrome, and Dent's disease (a familial renal tubular disease). Sixteen patients excreted between 2 and 40 mg of beta 2GI per millimole of creatinine. In contrast, 18 healthy controls had undetectable amounts of beta 2GI in urine. Isoelectric focusing followed by immunoblotting demonstrated multiple forms of beta 2GI with pls between 6.4 and 8.2. These pls are higher than for several other "tubular proteins"; beta 2GI may therefore be less retarded than more-anionic proteins by the glomerular charge-barrier. This could explain why large quantities of beta 2GI are excreted despite its relatively high molecular mass (50 kDa). Excretion of beta 2GI was easily demonstrated by routine electrophoresis of urine proteins. beta 2GI migrates in the beta-gamma region and may be confused with Bence Jones protein. beta 2GI is stable for at least two years in urine frozen at -25 degrees C.

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14

Nakagawa, Hisako, Shinsuke Yasuda, and Tadaaki Miyazaki. "Novel Function of Beta 2 Glycoprotein I in Angiogenesis." Current Angiogenesis 3, no. 3 (March 11, 2015): 132–38. http://dx.doi.org/10.2174/2211552803666141125214938.

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15

Miyakis, Spiros, Bill Giannakopoulos, and Steven A. Krilis. "Beta 2 glycoprotein I-function in health and disease." Thrombosis Research 114, no. 5-6 (January 2004): 335–46. http://dx.doi.org/10.1016/j.thromres.2004.07.017.

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16

EBELING, F., T. PETTERSSON, L. MUUKKONEN, E. VAHTERA, and V. RASI. "Beta‐2‐glycoprotein I antibodies in patients with thrombosis." Scandinavian Journal of Clinical and Laboratory Investigation 63, no. 2 (January 2003): 111–18. http://dx.doi.org/10.1080/00365510310002086.

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17

Blanco, Manuel Serrano, Jose Angel KJA Martinez Flores 2, Dolores Perez, Jose Maria Morales, Javier Gainza, Roberto Marcen, Fernando Escuin, et al. "Pre-transplant antibodies IgA-anti Beta 2 Glycoprotein I." Transplantation 102, Supplement 7 (July 2018): S189. http://dx.doi.org/10.1097/01.tp.0000542834.31485.ac.

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18

Balasubramanian, Krishnakumar, Jerald J. Killion, and Alan J. Schroit. "Estimation of Plasma Beta-2-Glycoprotein Levels by Competitive ELISA." Thrombosis Research 92, no. 2 (October 1998): 91–97. http://dx.doi.org/10.1016/s0049-3848(98)00115-7.

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19

Brusch, Anna M. "Antiphospholipid antibodies: significance of anti-beta-2-glycoprotein i isotypes." Pathology 47 (2015): S40. http://dx.doi.org/10.1097/01.pat.0000461431.82122.d7.

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20

Artusi, C., S. Fumagalli, M. Oggioni, M. O. Borghi, C. Grossi, P. L. Meroni, F. Tedesco, and M. G. De Simoni. "AB0131 Tissue Beta 2 glycoprotein I in Brain Ischemic Injury." Annals of the Rheumatic Diseases 75, Suppl 2 (June 2016): 941.3–941. http://dx.doi.org/10.1136/annrheumdis-2016-eular.5315.

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21

Blank, Miri, and Yehuda Shoenfeld. "Beta-2-glycoprotein-I, infections, antiphospholipid syndrome and therapeutic considerations." Clinical Immunology 112, no. 2 (August 2004): 190–99. http://dx.doi.org/10.1016/j.clim.2004.02.018.

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22

Passam, F. H., J. C. Qi, K. Tanaka, K. I. Matthaei, and S. A. Krilis. "In vivo modulation of angiogenesis by beta 2 glycoprotein I." Journal of Autoimmunity 35, no. 3 (November 2010): 232–40. http://dx.doi.org/10.1016/j.jaut.2010.06.013.

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23

Ebeling, Freja, Jari Pet�j�, Soile Alanko, Aune Hirvasniemi, Tarja Holm, Marja L�hde, Auli Nuutila, Helena Pesonen, Elina Vahtera, and Vesa Rasi. "Infant stroke and beta-2-glycoprotein 1 antibodies: six cases." European Journal of Pediatrics 162, no. 10 (October 1, 2003): 678–81. http://dx.doi.org/10.1007/s00431-003-1285-9.

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24

Passam, Freda H., Soheila Rahgozar, Miao Qi, Mark J. Raftery, Jason W. H. Wong, Kumiko Tanaka, Yiannis Ioannou, et al. "Beta 2 glycoprotein I is a substrate of thiol oxidoreductases." Blood 116, no. 11 (September 16, 2010): 1995–97. http://dx.doi.org/10.1182/blood-2010-02-271494.

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25

Roberts, G. P. "Characterization of the antigens recognized by two monoclonal antibodies reactive with basal-layer keratinocytes of human epidermis." Biochemical Journal 299, no. 3 (May 1, 1994): 659–64. http://dx.doi.org/10.1042/bj2990659.

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Two monoclonal antibodies, GR3 and GR4, reactive with the basal-layer keratinocytes of human epidermis, were derived by immunization of Balb/c mice with glycoproteins isolated from cultured keratinocytes by lectin-affinity chromatography. Immunoprecipitation of Triton X-100 extracts from human keratinocytes metabolically labelled with D-[1-14C]glucosamine revealed that GR3 recognized a major glycoprotein with migration properties identical with those of a glycoprotein (reduced form M(r) 126,000) which was previously shown to be implicated in intercellular adhesion [Roberts and Brunt (1985) Biochem J. 232, 67-70]. In their unreduced forms the antigens recognized by GR3 and GR4 both migrated as two bands with M(r) values of 118,000 and 147,000. Comparison of 125I-labelled glycoproteins immunoprecipitated by GR3, GR4 and integrin antibodies revealed that, under reducing conditions, the major band immunoprecipitated by both GR3 and GR4 co-migrated with the alpha 3 and beta 1 integrin chains. In addition the immunoprecipitate obtained with GR4 contained an additional band co-migrating with the alpha 2 integrin chain. Sequential immunoprecipitation studies with GR3, GR4 and integrin antibodies confirmed that GR3 is directed against the alpha 3 integrin chain, whereas GR4 is directed against the beta 1 chain. These studies also indicate that some of the alpha 2 integrin chains on keratinocytes may be associated with a beta-chain not recognized by the antisera against the beta 1 integrin chain used in this study.

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26

Joneckis, CC, RL Ackley, EP Orringer, EA Wayner, and LV Parise. "Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia." Blood 82, no. 12 (December 15, 1993): 3548–55. http://dx.doi.org/10.1182/blood.v82.12.3548.3548.

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Abstract The abnormal adherence of red blood cells, especially circulating reticulocytes (erythrocyte precursors), to the endothelium is believed to contribute to vascular occlusion observed in patients with sickle cell disease. Although several plasma proteins including von Willebrand factor and fibronectin have been proposed to mediate this adhesion, the mechanism of sickle cell adhesion to the endothelium remains unknown. Using flow cytometry, we screened sickle red blood cells with monoclonal antibodies (MoAbs) against known adhesion receptors and detected integrin subunits alpha 4 and beta 1 and the nonintegrin glycoprotein IV on reticulocytes but not on erythrocytes. No reactivity was detected against integrin subunits alpha 2, alpha 3, alpha 5, alpha 6, alpha v, beta 2, beta 3, integrin alpha IIb beta 3, or the nonintegrin glycoprotein Ib. Immunoprecipitation of reticulocytes with either alpha 4- or beta 1-specific antibodies identified the alpha 4 beta 1 complex (alpha 4(70) and alpha 4(80) forms), a receptor for fibronectin and vascular cell adhesion molecule-1. An antibody against glycoprotein IV, a receptor reported to bind thrombospondin and collagen, immunoprecipitated an 88-kD protein consistent with its reported M(r). MoAbs against alpha 4 and glycoprotein IV bound to an average of 4,600 and 17,500 sites per reticulocyte, respectively. Identification of alpha 4 beta 1 and glycoprotein IV on reticulocytes suggests both plasma-dependent and independent mechanisms of reticulocyte adhesion to endothelium and exposed extracellular matrix.

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27

Joneckis, CC, RL Ackley, EP Orringer, EA Wayner, and LV Parise. "Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia." Blood 82, no. 12 (December 15, 1993): 3548–55. http://dx.doi.org/10.1182/blood.v82.12.3548.bloodjournal82123548.

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The abnormal adherence of red blood cells, especially circulating reticulocytes (erythrocyte precursors), to the endothelium is believed to contribute to vascular occlusion observed in patients with sickle cell disease. Although several plasma proteins including von Willebrand factor and fibronectin have been proposed to mediate this adhesion, the mechanism of sickle cell adhesion to the endothelium remains unknown. Using flow cytometry, we screened sickle red blood cells with monoclonal antibodies (MoAbs) against known adhesion receptors and detected integrin subunits alpha 4 and beta 1 and the nonintegrin glycoprotein IV on reticulocytes but not on erythrocytes. No reactivity was detected against integrin subunits alpha 2, alpha 3, alpha 5, alpha 6, alpha v, beta 2, beta 3, integrin alpha IIb beta 3, or the nonintegrin glycoprotein Ib. Immunoprecipitation of reticulocytes with either alpha 4- or beta 1-specific antibodies identified the alpha 4 beta 1 complex (alpha 4(70) and alpha 4(80) forms), a receptor for fibronectin and vascular cell adhesion molecule-1. An antibody against glycoprotein IV, a receptor reported to bind thrombospondin and collagen, immunoprecipitated an 88-kD protein consistent with its reported M(r). MoAbs against alpha 4 and glycoprotein IV bound to an average of 4,600 and 17,500 sites per reticulocyte, respectively. Identification of alpha 4 beta 1 and glycoprotein IV on reticulocytes suggests both plasma-dependent and independent mechanisms of reticulocyte adhesion to endothelium and exposed extracellular matrix.

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28

Buchholz, Ina, Peter Nestler, Susan Köppen, and Mihaela Delcea. "Lysine residues control the conformational dynamics of beta 2-glycoprotein I." Physical Chemistry Chemical Physics 20, no. 42 (2018): 26819–29. http://dx.doi.org/10.1039/c8cp03234c.

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29

Gao, Pu-Jun. "Studies on specific interaction of beta-2-glycoprotein I with HBsAg." World Journal of Gastroenterology 9, no. 9 (2003): 2114. http://dx.doi.org/10.3748/wjg.v9.i9.2114.

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30

Balestrieri, Genesio, Angela Tincani, Laura Spatola, Flavio Allegri, Enrica Prati, Roberto Cattaneo, Guido Valesini, Nicoletta Del Papa, and Pierluigi Meroni. "Anti-beta 2-glycoprotein I antibodies: a marker of antiphospholipid syndrome?" Lupus 4, no. 2 (April 1995): 122–30. http://dx.doi.org/10.1177/096120339500400208.

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31

Wong, R. C. W., E. J. Favaloro, S. Adelstein, K. Baumgart, R. Bird, T. A. Brighton, M. Empson, et al. "Consensus guidelines on anti-beta 2 glycoprotein I testing and reporting." Pathology 40, no. 1 (January 2008): 58–63. http://dx.doi.org/10.1080/00313020701717720.

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32

Abinader, A., A. J. Hanly, and C. J. Lozada. "Catastrophic antiphospholipid syndrome associated with anti-beta-2- glycoprotein I IgA." Rheumatology 38, no. 1 (January 1, 1999): 84–85. http://dx.doi.org/10.1093/rheumatology/38.1.84.

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33

Fiallo, Paolo, Carlo Tomasina, Andrea Clapasson, and Paolo P. Cardo. "Antibodies to Beta₂-Glycoprotein I in Ischemic Stroke." Cerebrovascular Diseases 10, no. 4 (2000): 293–97. http://dx.doi.org/10.1159/000016073.

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34

Fleming, Sherry D. "Beta 2-glycoprotein I derived-peptides attenuate complement-mediated intestinal damage." Immunobiology 217, no. 11 (November 2012): 1141. http://dx.doi.org/10.1016/j.imbio.2012.08.035.

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35

Antosik, P., B. Kempisty, M. Jackowska, D. Bukowska, M. Lianeri, KP Brussow, and M. Wozna. "The morphology of porcine oocytes is associated with zona pellucida glycoprotein 3 and integrin beta 2 protein levels--." Veterinární Medicína 55, No. 4 (May 19, 2010): 154–62. http://dx.doi.org/10.17221/38/2010-vetmed.

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The morphology and quality of oocytes is set during oo- and folliculo-genesis, and is completed during final maturation. Early embryonic development is associated with the morphology of the cumulus-oocyte-complex (COC). However, current knowledge of the possible relationships between oocyte morphology and the level of proteins within the oocyte, which may reflect fertilization ability, is insufficient. Using western-blot analysis and confocal microscopic observation, we determined the levels of integrin beta-2 (integrin β2) and glycoprotein 3 (pZP3) protein levels in the porcine zona pellucida of four morphologically different types of oocytes, graded according to their cytoplasmic composition and cumulus structure. The level of integrin β2 protein was increased in grade I and II oocytes as compared to other grades (P < 0.05). Moreover, the level of pZP3 protein was 3–4 fold higher in grade I oocytes (P < 0.01). We suggest that COC morphology may be associated with oocyte fertilization ability with respect to its sperm-oocyte interaction gene expression, which is the result of increased accumulation of specific proteins prior to fertilization in higher quality oocytes. Higher quality oocytes may also reflect better fertilization ability.

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36

Gries, A., J. Nimpf, H. Wurm, G. M. Kostner, and T. Kenner. "Characterization of isoelectric subspecies of asialo-β2-glycoprotein I." Biochemical Journal 260, no. 2 (June 1, 1989): 531–34. http://dx.doi.org/10.1042/bj2600531.

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Isoelectric focusing of purified beta 2-glycoprotein I (beta 2-G-I) revealed five major bands with isoelectric points (pI) between 5.1 and 6.1. Neuraminidase treatment decreased the number of bands to two (pI 8.0 and 8.2). The two asialo subfractions of beta 2-G-I were purified by cation-exchange column chromatography. The more basic isoform II was found to have a higher content of lysine. Western-blot analysis of different plasma samples confirmed the heterogeneity of beta 2-G-I in plasma. Plasma treated with neuraminidase showed two bands irrespective of the number of isoforms as well as of the concentration in native plasma. This led us to the conclusion that human plasma beta 2-G-I consists of two isoproteins that are sialylated to different extents.

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37

Donald, A. S. R., and J. Feeney. "Oligosaccharides obtained from a blood-group-Sd(a+) Tamm-Horsfall glycoprotein. An n.m.r. study." Biochemical Journal 236, no. 3 (June 15, 1986): 821–28. http://dx.doi.org/10.1042/bj2360821.

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Treatment of Tamm-Horsfall urinary glycoprotein with Bacteroides fragilis endo-beta-galactosidase over a range of enzyme concentrations, pH and temperature resulted in the release of a small but constant proportion of the terminal sugars, which indicates the presence in the glycoprotein of relatively few enzyme-susceptible -GlcNAc beta 1-3Gal beta 1-4GlcNAc- units. Three oligosaccharides were isolated from the enzyme digest and characterized as Gal beta 1-4GlcNAc beta 1-3Gal, NeuAc alpha 2-3Gal beta 1-4 GlcNAc beta 1-3Gal and GalNAc beta 1-4(NeuAc alpha 2-3)Gal beta 1-4GlcNAc beta 1-3Gal by methylation analysis and exo-glycosidase digestion. The alditols of these oligosaccharides and related structures were examined by 500 MHz 1H-n.m.r. spectroscopy aided by spin-spin decoupling and two-dimensional correlated spectroscopy. An almost complete assignment of proton shifts was possible, and significant differences between the signals of some of the protons in the blood-group-Sda-active oligosaccharide III and literature values for the corresponding signals in the structurally related Cad-blood-group determinant are noted.

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38

TAKAMATSU, Kazunaga, Tadashi SUEHIRO, Masui KAWADA, and Fumitoshi OHNO. "Clinical Studies on Apolipoprotein H (β₂-glycoprotein I) in Patients with Hyperlipoproteinemia." Journal of Japan Atherosclerosis Society 15, no. 6 (1987): 1401–8. http://dx.doi.org/10.5551/jat1973.15.6_1401.

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39

Brusch, Anna. "The Significance of Anti-Beta-2-Glycoprotein I Antibodies in Antiphospholipid Syndrome." Antibodies 5, no. 2 (June 8, 2016): 16. http://dx.doi.org/10.3390/antib5020016.

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40

Gang, Yong, Nobuhiko Kubo, Ikunosuke Sakurabayashi, Yoshihiko Ohtsuka, Jun Suzuki, Yasuhiro Nomata, and Tadashi Kawai. "Structural variety and biological function of apolipoprotein H (.BETA.2-glycoprotein I)." SEIBUTSU BUTSURI KAGAKU 38, no. 1 (1994): 1–5. http://dx.doi.org/10.2198/sbk.38.1.

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41

BRIGHTON, Timothy A., Yan-Ping DAI, Philip J. HOGG, and Colin N. CHESTERMAN. "Microheterogeneity of beta-2 glycoprotein I: implications for binding to anionic phospholipids." Biochemical Journal 340, no. 1 (May 10, 1999): 59–67. http://dx.doi.org/10.1042/bj3400059.

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Considerable interest is currently focused on the interactions of beta-2 glycoprotein I (β2GPI) and anti-phospholipid antibodies with anionic phospholipids in an attempt to understand the association between these antibodies and clinical diseases such as thrombosis. The interactions of β2GPI and anionic phospholipids have only been characterized partially, and the physiological role of this glycoprotein remains uncertain. In this study we have explored in detail the physical and phospholipid-binding characteristics of a number of β2GPI preparations. We have found (i) that perchloric acid-purification methods are damaging to β2GPI during purification, (ii) that the dissociation constants of the various preparations for phosphatidylserine vary between 0.1-2 μM and are considerably weaker than previously reported, (iii) that considerable differences in affinity of the various β2GPI preparations for anionic phospholipids are obtained when comparing anionic phospholipids immobilized to a solid-phase versus phospholipid assembled in unilamellar vesicles, (iv) that the integrity of the fifth domain of β2GPI is important for binding immobilized anionic phospholipid but not especially important in binding vesicular anionic phospholipid, and (v) that β2GPI preparations with differing isoelectric species content bind anionic phospholipids differently, suggesting that varying glycosylation and/or protein polymorphisms impact upon phospholipid binding. These results highlight the importance of assessing the determinants of the interaction of β2GPI with anionic phospholipids assembled in unilamellar vesicles.

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42

Mankaï, A., A. Achour, Y. Thabet, W. Manoubia, W. Sakly, and I. Ghedira. "Anti-cardiolipin and anti-beta 2-glycoprotein I antibodies in celiac disease." Pathologie Biologie 60, no. 5 (October 2012): 291–95. http://dx.doi.org/10.1016/j.patbio.2011.07.003.

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43

Alarcon, Marcelo, Eduardo Fuentes, Ximena Maldonado, Claudia Mardones, and Iván Palomo. "Methodology of generation and purification of anti-beta 2 glycoprotein I antibodies." MethodsX 6 (2019): 986–92. http://dx.doi.org/10.1016/j.mex.2019.04.023.

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44

Terashi, Hiromi, Shinichiro Uchiyama, Shiori Hashimoto, and Makoto Iwata. ".BETA.2-glycoprotein I polymorphism as a risk factor for cerebral infarction." Nosotchu 27, no. 4 (2005): 608–11. http://dx.doi.org/10.3995/jstroke.27.608.

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45

BRIGHTON, Timothy A., Yan-Ping DAI, Philip J. HOGG, and Colin N. CHESTERMAN. "Microheterogeneity of beta-2 glycoprotein I: implications for binding to anionic phospholipids." Biochemical Journal 340, no. 1 (May 15, 1999): 59. http://dx.doi.org/10.1042/0264-6021:3400059.

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46

Cabral, A. R., and D. Alarcon-Segovia. "Anti-beta 2-glycoprotein I antibody testing in patients with antiphospholipid syndrome." Rheumatology 36, no. 11 (November 1, 1997): 1235. http://dx.doi.org/10.1093/rheumatology/36.11.1235.

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47

Hasdemir, Hale S., and Emad Tajkhorshid. "Characterization of Beta-2-Glycoprotein I Domain V interaction with Plasma Membrane." Biophysical Journal 120, no. 3 (February 2021): 47a—48a. http://dx.doi.org/10.1016/j.bpj.2020.11.530.

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48

Matsuura, E., Y. Igarashi, T. Yasuda, D. A. Triplett, and T. Koike. "Anticardiolipin antibodies recognize beta 2-glycoprotein I structure altered by interacting with an oxygen modified solid phase surface." Journal of Experimental Medicine 179, no. 2 (February 1, 1994): 457–62. http://dx.doi.org/10.1084/jem.179.2.457.

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Anticardiolipin antibodies (aCL) derived from the sera of individuals exhibiting the antiphospholipid syndrome (APS) directly bind to beta 2-glycoprotein I (beta 2-GPI), which is adsorbed to an oxidized polystyrene surface. Oxygen atoms were introduced on a polystyrene surface by irradiation with electron or gamma-ray radiation. X-ray photoelectron spectroscopy revealed the irradiated surfaces were oxidized to generate C-O and C = O moieties. aCL derived from either APS patients or (NZW x BXSB)F1 mice bound to beta 2-GPI coated on the irradiated plates, depending on the radiation dose. Antibody binding to beta 2-GPI on the irradiated plates was competitively inhibited by simultaneous addition of cardiolipin (CL)-coated latex beads mixed together with beta 2-GPI but were unaffected by addition of excess beta 2-GPI, CL micelles, or CL-coated latex beads alone. There was a high correlation between binding values of aCL in sera from 40 APS patients obtained by the anti-beta 2-GPI enzyme-linked immunosorbent assay (ELISA) using the irradiated plates and those by the beta 2-GPI-dependent aCL ELISA. Therefore, aCL have specificity for an epitope on beta 2-GPI. This epitope is expressed by a conformational change occurring when beta 2-GPI interacts with an oxygen-substituted solid phase surface.

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49

Mitchell, E. J., K. Lee, and M. D. O'Connor-McCourt. "Characterization of transforming growth factor-beta (TGF-beta) receptors on BeWo choriocarcinoma cells including the identification of a novel 38-kDa TGF-beta binding glycoprotein." Molecular Biology of the Cell 3, no. 11 (November 1992): 1295–307. http://dx.doi.org/10.1091/mbc.3.11.1295.

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Transforming growth factor-beta (TGF-beta) is a potential mediator of placental trophoblast functions, including differentiation, hormone production, endometrial invasion, and immunosuppression. Equilibrium binding and affinity-labeling assays were used to investigate the binding characteristics of TGF-beta 1 and TGF-beta 2 on an established human choriocarcinoma trophoblastic cell line (BeWo). The equilibrium binding experiments indicated that the BeWo cells exhibited similar average affinities and total number of binding sites for TGF-beta 1 and TGF-beta 2. The Kd values obtained from Scatchard analyses were approximately 65 pM for 125I-TGF-beta 1 and approximately 40 pM for 125I-TGF-beta 2, with 70,000 and 85,000 sites per cell, respectively. Competitive equilibrium binding experiments indicated that TGF-beta 1 and TGF-beta 2 were equipotent (apparent half maximal inhibition [IC50] approximately 70 pM) and that all binding sites were capable of recognizing both isoforms. Affinity-labeling studies with 125I-TGF-beta 1 and 125I-TGF-beta 2 and the chemical cross-linking agent bis(sulfosuccinimidyl)suberate (BS3) revealed a predominant type III/betaglycan receptor, a low level of apparently heterogeneous type I and II receptors and an additional novel 38-kDa TGF-beta binding glycoprotein that was present both under reducing and nonreducing conditions on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Affinity-labeling saturation and competition studies indicated that the type III/betaglycan component appears to have a 7-fold higher capacity for TGF-beta 1 than for -beta 2 yet exhibits a 5- to 10-fold higher affinity for TGF-beta 2 than for -beta 1. The 38-kDa TGF-beta binding component, an N-linked glycoprotein, exhibits a higher affinity for TGF-beta 2 than for -beta 1 that is strikingly similar to that of the type III/betaglycan receptor. This 38-kDa binding protein appears to be upregulated after methotrexate-induced differentiation of the BeWo cells.

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Atsumi, T., M. Khamashta, P. R. J. Ames, K. Ichikawa, T. Koike, and G. R. V. Hughes. "Protein S, C4b-binding protein (C4BP) and beta 2-glycoprotein I (??2-GPI) binding interaction." Blood Coagulation & Fibrinolysis 6, no. 6 (September 1995): 594. http://dx.doi.org/10.1097/00001721-199509000-00027.

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