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Socrates J. Tzartos - One of the best experts on this subject based on the ideXlab platform.
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Extracellular domains of the β, γ and ε subunits of the human acetylcholine receptor as Immunoadsorbents for myasthenic autoantibodies: A combination of Immunoadsorbents results in increased efficiency
Journal of Neuroimmunology, 2007Co-Authors: Kalliopi Kostelidou, Nikolaos Trakas, Socrates J. TzartosAbstract:Abstract Myasthenia gravis (MG) is usually caused by autoantibodies against the human muscle acetylcholine receptor (AChR). Plasmapheresis offers a therapeutic option, but, as well as removing the pathogenic anti-AChR autoantibodies, it non-specifically removes indispensable immunoglobulins. An attractive alternative to plasmapheresis would be the extracorporeal specific removal of the autoantibodies using AChR-based Immunoadsorbents. Previously, we used the N-terminal extracellular domain (ECD) of the AChR α subunit to immunoadsorb anti-α subunit autoantibodies from MG sera. In this study, we immobilised the β -, γ- and e-AChR ECDs on Sepharose and tested them as Immunoadsorbents on 50 MG sera. A given ECD removed a different percentage of autoantibodies from different sera and different ECDs removed different percentages from the same serum; on average, the β-, γ- and e-ECDs removed 22%, 20% and 15.5% of the autoantibodies, respectively. Immunoadsorption was completed in 3 min, 1 μg of ECD removed ∼ 2 pmol of autoantibodies, and the Immunoadsorbent could be recycled ∼ 4 times. The combined use of two (α + γ) or four (α + β + γ + e) ECDs in a single Immunoadsorbent resulted in much higher (often additive) immunoadsorption. These results show that MG sera have autoantibodies against several AChR subunits, and suggest that the combined use of all AChR ECDs could provide the basis for a novel, antigen-specific therapy for MG.
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Extracellular domains of the beta, gamma and epsilon subunits of the human acetylcholine receptor as Immunoadsorbents for myasthenic autoantibodies: a combination of Immunoadsorbents results in increased efficiency.
Journal of neuroimmunology, 2007Co-Authors: Kalliopi Kostelidou, Nikolaos Trakas, Socrates J. TzartosAbstract:Myasthenia gravis (MG) is usually caused by autoantibodies against the human muscle acetylcholine receptor (AChR). Plasmapheresis offers a therapeutic option, but, as well as removing the pathogenic anti-AChR autoantibodies, it non-specifically removes indispensable immunoglobulins. An attractive alternative to plasmapheresis would be the extracorporeal specific removal of the autoantibodies using AChR-based Immunoadsorbents. Previously, we used the N-terminal extracellular domain (ECD) of the AChR alpha subunit to immunoadsorb anti-alpha subunit autoantibodies from MG sera. In this study, we immobilised the beta -, gamma- and epsilon-AChR ECDs on Sepharose and tested them as Immunoadsorbents on 50 MG sera. A given ECD removed a different percentage of autoantibodies from different sera and different ECDs removed different percentages from the same serum; on average, the beta-, gamma- and epsilon-ECDs removed 22%, 20% and 15.5% of the autoantibodies, respectively. Immunoadsorption was completed in 3 min, 1 mug of ECD removed approximately 2 pmol of autoantibodies, and the Immunoadsorbent could be recycled approximately 4 times. The combined use of two (alpha+gamma) or four (alpha+beta+gamma+epsilon) ECDs in a single Immunoadsorbent resulted in much higher (often additive) immunoadsorption. These results show that MG sera have autoantibodies against several AChR subunits, and suggest that the combined use of all AChR ECDs could provide the basis for a novel, antigen-specific therapy for MG.
Kalliopi Kostelidou - One of the best experts on this subject based on the ideXlab platform.
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Extracellular domains of the β, γ and ε subunits of the human acetylcholine receptor as Immunoadsorbents for myasthenic autoantibodies: A combination of Immunoadsorbents results in increased efficiency
Journal of Neuroimmunology, 2007Co-Authors: Kalliopi Kostelidou, Nikolaos Trakas, Socrates J. TzartosAbstract:Abstract Myasthenia gravis (MG) is usually caused by autoantibodies against the human muscle acetylcholine receptor (AChR). Plasmapheresis offers a therapeutic option, but, as well as removing the pathogenic anti-AChR autoantibodies, it non-specifically removes indispensable immunoglobulins. An attractive alternative to plasmapheresis would be the extracorporeal specific removal of the autoantibodies using AChR-based Immunoadsorbents. Previously, we used the N-terminal extracellular domain (ECD) of the AChR α subunit to immunoadsorb anti-α subunit autoantibodies from MG sera. In this study, we immobilised the β -, γ- and e-AChR ECDs on Sepharose and tested them as Immunoadsorbents on 50 MG sera. A given ECD removed a different percentage of autoantibodies from different sera and different ECDs removed different percentages from the same serum; on average, the β-, γ- and e-ECDs removed 22%, 20% and 15.5% of the autoantibodies, respectively. Immunoadsorption was completed in 3 min, 1 μg of ECD removed ∼ 2 pmol of autoantibodies, and the Immunoadsorbent could be recycled ∼ 4 times. The combined use of two (α + γ) or four (α + β + γ + e) ECDs in a single Immunoadsorbent resulted in much higher (often additive) immunoadsorption. These results show that MG sera have autoantibodies against several AChR subunits, and suggest that the combined use of all AChR ECDs could provide the basis for a novel, antigen-specific therapy for MG.
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Extracellular domains of the beta, gamma and epsilon subunits of the human acetylcholine receptor as Immunoadsorbents for myasthenic autoantibodies: a combination of Immunoadsorbents results in increased efficiency.
Journal of neuroimmunology, 2007Co-Authors: Kalliopi Kostelidou, Nikolaos Trakas, Socrates J. TzartosAbstract:Myasthenia gravis (MG) is usually caused by autoantibodies against the human muscle acetylcholine receptor (AChR). Plasmapheresis offers a therapeutic option, but, as well as removing the pathogenic anti-AChR autoantibodies, it non-specifically removes indispensable immunoglobulins. An attractive alternative to plasmapheresis would be the extracorporeal specific removal of the autoantibodies using AChR-based Immunoadsorbents. Previously, we used the N-terminal extracellular domain (ECD) of the AChR alpha subunit to immunoadsorb anti-alpha subunit autoantibodies from MG sera. In this study, we immobilised the beta -, gamma- and epsilon-AChR ECDs on Sepharose and tested them as Immunoadsorbents on 50 MG sera. A given ECD removed a different percentage of autoantibodies from different sera and different ECDs removed different percentages from the same serum; on average, the beta-, gamma- and epsilon-ECDs removed 22%, 20% and 15.5% of the autoantibodies, respectively. Immunoadsorption was completed in 3 min, 1 mug of ECD removed approximately 2 pmol of autoantibodies, and the Immunoadsorbent could be recycled approximately 4 times. The combined use of two (alpha+gamma) or four (alpha+beta+gamma+epsilon) ECDs in a single Immunoadsorbent resulted in much higher (often additive) immunoadsorption. These results show that MG sera have autoantibodies against several AChR subunits, and suggest that the combined use of all AChR ECDs could provide the basis for a novel, antigen-specific therapy for MG.
Chang-zhi Chen - One of the best experts on this subject based on the ideXlab platform.
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A novel Immunoadsorbent for rheumatoid arthritis therapy--preparation and efficacy evaluation.
Artificial cells blood substitutes and immobilization biotechnology, 2000Co-Authors: Chang-zhi ChenAbstract:Aim To develop a novel Immunoadsorbent for rheumatoid arthritis (RA) therapy. Methods: A RA Immunoadsorbent was developed by binding heat-aggregated human IgG(HAHIgG) to porous agar gel beads. Its adsorption capacity for rheumatoid factors (RFs), storage stability and blood compatibility were evaluated. Results: The coupling yield of HAHIgG on the carrier was 6.0mg/g wet gel. Saturation adsorption capacity of the adsorbent for IgMRF, IgGRF and IgARF were 3400, 2240 and 2400 IU/g, respectively. The adsorbent can be stored at 4°C for three months without significant variance in its activity. Its fine permeability and hemocompatibility were demonstrated by extracorporeal hemoperfusion on rabbits. Conclusion: HAHIgG/agar gel is a safe and effective Immunoadsorbent for RA therapy, its potential clinical use is promising in the future.
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Clinical trials of type I and in vitro studies of type II Immunoadsorbents for systemic lupus erythematosus therapy.
Artificial organs, 1998Co-Authors: Deling Kong, Chang-zhi Chen, En‐fu LinAbstract:A highly selective Immunoadsorbent was prepared by immobilization of DNA on carbonized resin beads (Type I) for the removal of the pathogenic antibodies of systemic lupus erythematosus (SLE) patients. Thirty cases of clinical trials of this SLE therapy were performed at 12 hospitals in China. The levels of anti-DNA antibodies after whole blood perfusion were decreased 40-70%. Almost all the symptoms were relieved, and some patients were freed from medicine administration. A new Immunoadsorbent was prepared using aminated cellulose beads (Type II) having a higher DNA immobilization capacity of 0.6 mg/ml than the 0.4 mg/ml capacity for Type I. Stationary adsorption tests with the sera of SLE patients showed that the Type II Immunoadsorbent could remove 60% of the pathogenic antibodies, which is much higher than the 30% for the Type I adsorbent.
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Clinical trials of Immunoadsorbent in systemic lupus erythematosus therapy.
Artificial organs, 1995Co-Authors: Chun-li Gao, Chang-zhi Chen, Ping Yuan, Ji-chang SongAbstract:: Five patients with systemic lupus erythematosus (SLE) were perfused through an extracorporeal shunt filled with DNA-Immunoadsorbent (DNA immobilized on carbonized resin beads). High concentrations of anti-DNA antibodies (36.4–67.0%) (binding percentage with 125I-DNA) in the serum of SLE patients were reduced to 13.8–53.0%, respectively. The highest removal percentage was 62.1%. Although the decline levels varied, the symptoms of patients, i.e., long-term severe joint pain, severe edema, hydropericardium, and ascites were all relieved considerably. The Immunoadsorbent showed satisfactory blood compatibility.
Hiroshi Mitsumoto - One of the best experts on this subject based on the ideXlab platform.
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Myasthenia gravis therapy: Immunoadsorbent may eliminate need for plasma products
Cleveland Clinic journal of medicine, 1993Co-Authors: Koji Sawada, Paul S. Malchesky, Anna P. Koo, Hiroshi MitsumotoAbstract:This in vitro study assessed the effectiveness of a new Immunoadsorbent (Asahi IM-TR 350) in removing anti-acetylcholine receptor antibody from plasma with minimal loss of albumin. Plasma procured from a myasthenia gravis patient undergoing routine plasma exchange was perfused through the Immunoadsorbent and recirculated in vitro to simulate a clinical treatment. To assess the temperature dependency of sorption, perfusion was performed at various temperatures. Plasma solute concentrations were taken before and after perfusion to calculate solute rejection coefficients. The Immunoadsorbent has a high sorption capacity for anti-acetylcholine receptor antibody, while allowing a minimum loss of albumin. For patients with myasthenia gravis, this Immunoadsorbent can provide an alternative to plasma exchange that does not require the use of plasma products.
Nikolaos Trakas - One of the best experts on this subject based on the ideXlab platform.
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Extracellular domains of the β, γ and ε subunits of the human acetylcholine receptor as Immunoadsorbents for myasthenic autoantibodies: A combination of Immunoadsorbents results in increased efficiency
Journal of Neuroimmunology, 2007Co-Authors: Kalliopi Kostelidou, Nikolaos Trakas, Socrates J. TzartosAbstract:Abstract Myasthenia gravis (MG) is usually caused by autoantibodies against the human muscle acetylcholine receptor (AChR). Plasmapheresis offers a therapeutic option, but, as well as removing the pathogenic anti-AChR autoantibodies, it non-specifically removes indispensable immunoglobulins. An attractive alternative to plasmapheresis would be the extracorporeal specific removal of the autoantibodies using AChR-based Immunoadsorbents. Previously, we used the N-terminal extracellular domain (ECD) of the AChR α subunit to immunoadsorb anti-α subunit autoantibodies from MG sera. In this study, we immobilised the β -, γ- and e-AChR ECDs on Sepharose and tested them as Immunoadsorbents on 50 MG sera. A given ECD removed a different percentage of autoantibodies from different sera and different ECDs removed different percentages from the same serum; on average, the β-, γ- and e-ECDs removed 22%, 20% and 15.5% of the autoantibodies, respectively. Immunoadsorption was completed in 3 min, 1 μg of ECD removed ∼ 2 pmol of autoantibodies, and the Immunoadsorbent could be recycled ∼ 4 times. The combined use of two (α + γ) or four (α + β + γ + e) ECDs in a single Immunoadsorbent resulted in much higher (often additive) immunoadsorption. These results show that MG sera have autoantibodies against several AChR subunits, and suggest that the combined use of all AChR ECDs could provide the basis for a novel, antigen-specific therapy for MG.
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Extracellular domains of the beta, gamma and epsilon subunits of the human acetylcholine receptor as Immunoadsorbents for myasthenic autoantibodies: a combination of Immunoadsorbents results in increased efficiency.
Journal of neuroimmunology, 2007Co-Authors: Kalliopi Kostelidou, Nikolaos Trakas, Socrates J. TzartosAbstract:Myasthenia gravis (MG) is usually caused by autoantibodies against the human muscle acetylcholine receptor (AChR). Plasmapheresis offers a therapeutic option, but, as well as removing the pathogenic anti-AChR autoantibodies, it non-specifically removes indispensable immunoglobulins. An attractive alternative to plasmapheresis would be the extracorporeal specific removal of the autoantibodies using AChR-based Immunoadsorbents. Previously, we used the N-terminal extracellular domain (ECD) of the AChR alpha subunit to immunoadsorb anti-alpha subunit autoantibodies from MG sera. In this study, we immobilised the beta -, gamma- and epsilon-AChR ECDs on Sepharose and tested them as Immunoadsorbents on 50 MG sera. A given ECD removed a different percentage of autoantibodies from different sera and different ECDs removed different percentages from the same serum; on average, the beta-, gamma- and epsilon-ECDs removed 22%, 20% and 15.5% of the autoantibodies, respectively. Immunoadsorption was completed in 3 min, 1 mug of ECD removed approximately 2 pmol of autoantibodies, and the Immunoadsorbent could be recycled approximately 4 times. The combined use of two (alpha+gamma) or four (alpha+beta+gamma+epsilon) ECDs in a single Immunoadsorbent resulted in much higher (often additive) immunoadsorption. These results show that MG sera have autoantibodies against several AChR subunits, and suggest that the combined use of all AChR ECDs could provide the basis for a novel, antigen-specific therapy for MG.