Journal ArticleDOI
Polymorphisms β2-glycoprotein. I: phospholipid binding and multimeric structure
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TLDR
The normal cardiolipin binding in heterozygous state for mutations at phospholipid-binding domain may be due to the multimeric structure of beta2-glycoprotein I, which is found in plasma at a concentration of approximately 200 microg/ml.About:
This article is published in Thrombosis Research.The article was published on 2002-11-01. It has received 16 citations till now. The article focuses on the topics: Phospholipid Binding & Cardiolipin binding.read more
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Journal ArticleDOI
Current concepts on the pathogenesis of the antiphospholipid syndrome.
TL;DR: This review critically examines the experimental evidence underlying the various propositions made to explain how antiphospholipid antibodies may predispose to disease in humans and examines the evidence relating to the immunologic mechanisms that may contribute to the breakage of peripheral tolerance in this disorder.
Journal ArticleDOI
TLR2 Is One of the Endothelial Receptors for β2-Glycoprotein I
Jean-Eric Alard,Fanny Gaillard,Capucine Daridon,Yehuda Shoenfeld,Christophe Jamin,Pierre Youinou +5 more
TL;DR: The data demonstrate that direct binding of β2- gpI on EC surface occurs through direct interaction with TLR2, and signaling for anti–β2-gpI may be envisioned as a multiprotein complex concentrated in lipid rafts on the EC membrane.
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Plasma Protein β-2-Glycoprotein 1 Mediates Interaction between the Anti-tumor Monoclonal Antibody 3G4 and Anionic Phospholipids on Endothelial Cells
Troy A. Luster,Jin He,Xianming Huang,Sourindra Maiti,Alan J. Schroit,Philip G. de Groot,Philip E. Thorpe +6 more
TL;DR: 3G4 targets tumor EC by increasing the avidity of β2 GP1 for anionic phospholipids through formation of multivalent 3G4-β2GP1 complexes, which indicates that antibody binding to PS is dependent on plasma protein β-2-glycoprotein 1.
Journal ArticleDOI
Phagocytosis of platelet microvesicles and β2– glycoprotein I
TL;DR: It is suggested that the binding of beta2-glycoprotein I to phosphatidylserine-expressing procoagulant platelet microvesicles may promote their clearance by phagocytosis and autoantibodies to beta2 -glycop protein I may inhibit this process to induce a procoAGulant state.
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The effect of phospholipids on the formation of immune complexes between autoantibodies and β2-glycoprotein I or prothrombin
TL;DR: There is now strong evidence that formation of bivalent, trimolecular immune complexes at the lipid membrane essentially contributes to the binding of intrinsically low affinity patient antibodies.
References
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Journal ArticleDOI
Use of resonance energy-transfer to monitor membrane-fusion
TL;DR: An assay for vesicle--vesicle fusion involving resonance energy transfer between N-(7-nitro-2,1,3-benzoxadiazol-4-yl), the energy donor, and rhodamine, the energy acceptor has been developed.
PatentDOI
Target-sensitive immunoliposomes- preparation and characterization
TL;DR: Dioleoylphosphatidylcholine immunoliposomes were not lysed upon contact with infected cells under the same conditions, indicating that PE was essential for the target-specific liposome destabilization.
Journal ArticleDOI
Complete amino acid sequence of human plasma beta 2-glycoprotein I
TL;DR: Computerized analysis of the sequence reveals five consecutive homologous segments in which cysteine, proline, and tryptophan appear to be highly conserved, which suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
Journal ArticleDOI
Complete nucleotide and deduced amino acid sequence of human beta 2-glycoprotein I.
Alexander Steinkasserer,C. Estaller,Elisabeth H. Weiss,Robert B. Sim,Robert B. Sim,Anthony J. Day +5 more
TL;DR: The nucleotide and complete amino acid sequence for the human beta 2-glycoprotein I (beta 2I) was derived by sequencing the cDNA clone pB2I-1 as discussed by the authors.
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Beta 2 glycoprotein I is a major protein associated with very rapidly cleared liposomes in vivo, suggesting a significant role in the immune clearance of "non-self" particles.
TL;DR: It is demonstrated that the amount of β2-glycoprotein I associated with liposomes, as quantitated by an enzyme-linked immunosorbent assay, is correlated with their clearance rates; moreover, the circulation residency time of cardiolipin-containing liposome is extended in mice pretreated with anti-β2- Glycop protein I antibodies.