抗アセチルコリン受容体抗体
WordNet
- not in favor of (an action or proposal etc.)
- a person who is opposed (to an action or policy or practice etc.); "the antis smelled victory after a long battle"
- social insect living in organized colonies; characteristically the males and fertile queen have wings during breeding season; wingless sterile females are the workers (同)emmet, pismire
- a neurotransmitter that is a derivative of choline; released at the ends of nerve fibers in the somatic and parasympathetic nervous systems
- any of a large variety of proteins normally present in the body or produced in response to an antigen which it neutralizes, thus producing an immune response
- a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response
PrepTutorEJDIC
- 《話》(特定の慣習・政策・行動などに)反対する人
- 『アリ』
- =ain't
- アセチルコリン(神経を刺激し筋肉運動を起こす化合物)
- 抗体,免疫体,抗毒素
- =sense organ / 受信装置
UpToDate Contents
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English Journal
- Structural characterization of the main immunogenic region of the Torpedo acetylcholine receptor.
- Morell SW1, Trinh VB1, Gudipati E2, Friend A3, Page NA4, Agius MA5, Richman DP6, Fairclough RH7.Author information 1University of California, Davis School of Medicine, Department of Neurology, One Shields Avenue, 1515 Newton Court, Room 510C, Davis, CA 95616, United States; Biochemistry, Molecular, Cellular, and Developmental Biology Graduate Group of UC Davis, United States.2Biochemistry, Siemens Healthcare Diagnostics, 5210 Pacific Concourse Drive, Los Angeles, CA 90045, United States.3University of California, Davis School of Medicine, Department of Neurology, One Shields Avenue, 1515 Newton Court, Room 510C, Davis, CA 95616, United States.4University of California, Davis School of Medicine, Department of Neurology, One Shields Avenue, 1515 Newton Court, Room 510C, Davis, CA 95616, United States; Department of Physics Graduate Program, University of California, Davis, One Shields Avenue, Davis, CA 95616, United States.5University of California, Davis School of Medicine, Department of Neurology, One Shields Avenue, 1515 Newton Court, Room 510C, Davis, CA 95616, United States; VANCHCS, 10535 Hospital Way, Mather, CA 95655, United States.6University of California, Davis School of Medicine, Department of Neurology, One Shields Avenue, 1515 Newton Court, Room 510C, Davis, CA 95616, United States; Neurosciences Graduate Group of UC Davis, United States.7University of California, Davis School of Medicine, Department of Neurology, One Shields Avenue, 1515 Newton Court, Room 510C, Davis, CA 95616, United States; Biochemistry, Molecular, Cellular, and Developmental Biology Graduate Group of UC Davis, United States; Biophysics Graduate Group of UC Davis, United States. Electronic address: rhfairclough@ucdavis.edu.AbstractTo develop antigen-specific immunotherapies for autoimmune diseases, knowledge of the molecular structure of targeted immunological hotspots will guide the production of reagents to inhibit and halt production of antigen specific attack agents. To this end we have identified three noncontiguous segments of the Torpedo nicotinic acetylcholine receptor (AChR) α-subunit that contribute to the conformationally sensitive immunological hotspot on the AChR termed the main immunogenic region (MIR): α(1-12), α(65-79), and α(110-115). This region is the target of greater than 50% of the anti-AChR Abs in serum from patients with myasthenia gravis (MG) and animals with experimental autoimmune myasthenia gravis (EAMG). Many monoclonal antibodies (mAbs) raised in one species against an electric organ AChR cross react with the neuromuscular AChR MIR in several species. Probing the Torpedo AChR α-subunit with mAb 132A, a disease inducing anti-MIR mAb raised against the Torpedo AChR, we have determined that two of the three MIR segments, α(1-12) and α(65-79), form a complex providing the signature components recognized by mAb 132A. These two segments straddle a third, α(110-115), that seems not to contribute specific side chains for 132A recognition, but is necessary for optimum antibody binding. This third segment appears to form a foundation upon which the three-dimensional 132A epitope is anchored.
- Molecular immunology.Mol Immunol.2014 Mar;58(1):116-31. doi: 10.1016/j.molimm.2013.11.005. Epub 2013 Dec 11.
- To develop antigen-specific immunotherapies for autoimmune diseases, knowledge of the molecular structure of targeted immunological hotspots will guide the production of reagents to inhibit and halt production of antigen specific attack agents. To this end we have identified three noncontiguous segm
- PMID 24333757
- Preferential production of IgG1, IL-4 and IL-10 in MuSK-immunized mice.
- Ulusoy C1, Kim E2, Tüzün E3, Huda R2, Yılmaz V4, Poulas K5, Trakas N6, Skriapa L7, Niarchos A5, Strait RT8, Finkelman FD9, Turan S1, Zisimopoulou P6, Tzartos S7, Saruhan-Direskeneli G4, Christadoss P2.Author information 1Department of Neuroscience, Institute for Experimental Medical Research, University of Istanbul, Istanbul, 34393, Turkey.2Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, 77555, USA.3Department of Neuroscience, Institute for Experimental Medical Research, University of Istanbul, Istanbul, 34393, Turkey. Electronic address: drerdem@yahoo.com.4Department of Physiology, Istanbul Faculty of Medicine, University of Istanbul, Istanbul, 34393, Turkey.5Department of Pharmacy, School of Health Sciences, University of Patras, Patras, 26504, Greece.6Hellenic Pasteur Institute, Athens, 115 21, Greece.7Department of Pharmacy, School of Health Sciences, University of Patras, Patras, 26504, Greece; Hellenic Pasteur Institute, Athens, 115 21, Greece.8Department of Pediatrics and Cincinnati Children's Hospital Division of Emergency Medicine, College of Medicine, University of Cincinnati, Cincinnati, Ohio, 45229, USA.9Department of Medicine, Cincinnati Veterans Affairs Medical Center, Cincinnati, OH, 45229, USA, Department of Internal Medicine, College of Medicine, University of Cincinnati, Cincinnati, OH, 45229, USA, Division of Immunobiology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229, USA.AbstractMyasthenia gravis (MG) is an autoimmune disease characterized by muscle weakness associated with acetylcholine receptor (AChR), muscle-specific receptor kinase (MuSK) or low-density lipoprotein receptor-related protein 4 (LRP4)-antibodies. MuSK-antibodies are predominantly of the non-complement fixing IgG4 isotype. The MuSK associated experimental autoimmune myasthenia gravis (EAMG) model was established in mice to investigate immunoglobulin (Ig) and cytokine responses related with MuSK immunity. C57BL/6 (B6) mice immunized with 30μg of recombinant human MuSK in incomplete or complete Freund's adjuvant (CFA) showed significant EAMG susceptibility (>80% incidence). Although mice immunized with 10μg of MuSK had lower EAMG incidence (14.3%), serum MuSK-antibody levels were comparable to mice immunized with 30μg MuSK. While MuSK immunization stimulated production of all antibody isotypes, non-complement fixing IgG1 was the dominant anti-MuSK Ig isotype in both sera and neuromuscular junctions. Moreover, MuSK immunized IgG1 knockout mice showed very low serum MuSK-antibody levels. Sera and MuSK-stimulated lymph node cell supernatants of MuSK immunized mice showed significantly higher levels of IL-4 and IL-10 (but not IFN-γ and IL-12), than those of CFA immunized mice. Our results suggest that through activation of Th2-type cells, anti-MuSK immunity promotes production of IL-4, which in turn activates anti-MuSK IgG1, the mouse analog of human IgG4. These findings might provide clues for the pathogenesis of other IgG4-related diseases as well as development of disease specific treatment methods (e.g. specific IgG4 inhibitors) for MuSK-related MG.
- Clinical immunology (Orlando, Fla.).Clin Immunol.2014 Feb 28. pii: S1521-6616(14)00049-7. doi: 10.1016/j.clim.2014.02.012. [Epub ahead of print]
- Myasthenia gravis (MG) is an autoimmune disease characterized by muscle weakness associated with acetylcholine receptor (AChR), muscle-specific receptor kinase (MuSK) or low-density lipoprotein receptor-related protein 4 (LRP4)-antibodies. MuSK-antibodies are predominantly of the non-complement fixi
- PMID 24589747
- Scale up and safety parameters of antigen specific immunoadsorption of human anti-acetylcholine receptor antibodies.
- Lagoumintzis G1, Zisimopoulou P2, Trakas N2, Grapsa E3, Poulas K1, Tzartos SJ4.Author information 1Department of Pharmacy, University of Patras, GR 26500, Patras, Greece.2Department of Biochemistry, Hellenic Pasteur Institute, 127 Vass. Sofias Avenue, GR 11521, Athens, Greece.3Department of Nephrology, Aretaieion University Hospital, Athens, Greece.4Department of Biochemistry, Hellenic Pasteur Institute, 127 Vass. Sofias Avenue, GR 11521, Athens, Greece. Electronic address: tzartos@pasteur.gr.AbstractMyasthenia gravis is an autoimmune disease usually caused by autoantibodies against the muscle nicotinic acetylcholine receptor (nAChR). Current treatments are not specific, and thus often cause side effects. Here, we elaborate on our previous findings on antigen specific immunoadsorption towards scaling up the method as well as testing whole blood apheresis. The average percent of plasma or whole blood immunoadsorption was up to 79.5%±2.9. Moreover, neither pyrogens were co-administered nor did complement activation occur after immunoadsorption. Thus, antigen-specific apheresis of anti-AChR autoantibodies seems a safe and effective treatment for myasthenia gravis that can be scaled up for clinical testing.
- Journal of neuroimmunology.J Neuroimmunol.2014 Feb 15;267(1-2):1-6. doi: 10.1016/j.jneuroim.2013.11.001. Epub 2013 Nov 10.
- Myasthenia gravis is an autoimmune disease usually caused by autoantibodies against the muscle nicotinic acetylcholine receptor (nAChR). Current treatments are not specific, and thus often cause side effects. Here, we elaborate on our previous findings on antigen specific immunoadsorption towards sc
- PMID 24412396
Japanese Journal
- SCC抗原の異常高値を示した重症筋無力症合併，浸潤性胸腺腫の一手術症例
- 山浦 匠,大杉 純,星野 実加,樋口 光徳,吉野 泰啓,鈴木 弘行
- 日本呼吸器外科学会雑誌 28(2), 215-220, 2014
- 症例は30歳代女性．眼瞼下垂と嚥下困難を自覚し近医で前縦隔腫瘍と重症筋無力症を指摘された．神経症状に対する内科的治療を先行した後，前縦隔腫瘍の切除を考慮し当科紹介となった．血液学的検査では血清抗アセチルコリン受容体抗体，血清SCC抗原（SCCA）が高値を示し，CT検査で前縦隔腫瘍と胸膜播種が疑われた．生検の結果WHO type B2胸腺腫，正岡IVa期と診断し拡大胸腺胸腺腫摘出，壁側胸膜全摘術と肺 …
- NAID 130003394019
- 自己免疫性自律神経節障害(AAG)の病態と免疫療法
- 中根 俊成,樋口 理,松尾 秀徳
- 日本アフェレシス学会雑誌 32(3), 198-203, 2013-10-31
- … Autoimmune autonomic ganglionopathy (AAG) is a disorder of isolated autonomic failure associated with antibodies to the nitotinic acetylcholine receptor of the autonomic ganglia resulting in severe orthostatic intolerance, syncope, constipation, gastroparesis, urinary retention, dry mouth, dry eyes, blurred vision and anhidrosis. … We interpreted the improvement in clinical symptoms correlated with the decrease in the levels of anti gAChR antibodies in each case. …
- NAID 110009661554
- Thymus histology and concomitant autoimmune diseases in Japanese patients with muscle-specific receptor tyrosine kinase-antibody-positive myasthenia gravis
- Nakata Ruka,Motomura Masakatsu,Masuda Tomoko,Shiraishi Hirokazu,Tokuda Masahiro,Fukuda Taku,Ando Takao,Yoshimura Toshiro,Tsujihata Mitsuhiro,Kawakami Atsushi
- European Journal of Neurology 20(9), 1272-1276, 2013-09
- … Background and purpose: The differences in the characteristics of thymus histology, coexisting autoimmune diseases and related autoantibodies between anti-muscle-specific receptor tyrosine kinase (MuSK)-antibody (Ab)-positive myasthenia gravis (MG) patients, and anti-acetylcholine receptor (AChR)-Ab-positive MG patients are not clearly defined. …
- NAID 120005328277
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★リンクテーブル★
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- 英
- anti acetylcholine receptor antibody, anti-acetylcholine receptor antibody, antibody of acetylcholine receptor
- 同
- アセチルコリン受容体抗体 acetylcholine receptor antibody、抗AChR抗体 anti-AChR antibody、AChR抗体 AChR antibody
- blocking抗体とbinding抗体が存在しているう
- 診断のために一般的に測定しているのはbinding抗体である。
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抗アセチルコリン受容体抗体
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- 同
- ants, stinging
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アセチルコリン ACh
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アセチルコリン受容体