- 古典的経路：C3からC4b2aのもつC3 convatase活性により生成し、C4b2a3bはC5 convertase活性を持つ (2008前期免疫学プリント 68)
- 別経路：C3からC3bBbPのもつC3 convertase活性により生成し、n(C3bBb)はC5 convertase活性を持つ (2008前期免疫学プリント 68)
- the 3rd letter of the Roman alphabet (同)c
- (music) the keynote of the scale of C major
- a general-purpose programing language closely associated with the UNIX operating system
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- Mechanisms of enhanced neutralization of botulinum neurotoxin by monoclonal antibodies conjugated to antibodies specific for the erythrocyte complement receptor.
- Sharma R, Zhao H, Al-Saleem FH, Ubaid AS, Puligedda RD, Segan AT, Lindorfer MA, Bermudez R, Elias M, Adekar SP, Simpson LL, Taylor RP, Dessain SK.Author information Lankenau Institute for Medical Research, Wynnewood, PA 19096, USA.AbstractImmune complexes formed between monoclonal antibodies (mAbs) and toxins can neutralize toxicity in vivo by multiple mechanisms. Toxin sequestration and clearance by mAbs may be improved by enhancing their ability to bind to red blood cells (RBCs) through immune adherence. This can be achieved by converting the mAbs to heteropolymers (HPs), which are antigen-specific mAbs cross-linked to mAbs targeting the complement receptor (CR1), a protein that is expressed on the surface of RBCs in primates and mediates delivery of complement C3b-containing immune complexes to tissue macrophages. Conversion of mAbs to HPs has been shown to enhance clearance of multivalent antigens from the blood circulation, but the interaction of HPs with monovalent toxins has not been examined. Using botulinum neurotoxin (BoNT) as a model system, we studied the effect of conversion of a pair of BoNT-specific mAbs into HPs on toxin neutralization and handling in vivo. Two HPs given in combination had 166-fold greater potency than un-modified mAbs, neutralizing 5000 LD50 BoNT, when tested in transgenic mice expressing human CR1 on RBC membranes. Improvement required adherence of BoNT to the RBC in vivo and 2 HPs, rather than an HP+mAb pair. The HP pair bound BoNT to RBCs in the circulation for 2h, in comparison to BoNT-neutralizing anti-serum, which induced no detectable RBC binding. HP pairs exhibited enhanced uptake by peritoneal macrophages in vitro, compared to pairs of mAbs or mAb+HP pairs. In a post-exposure therapeutic model, HPs gave complete protection from a lethal BoNT dose up to 3h after toxin exposure. In a pre-exposure prophylaxis model, mice given HP up to 5 days prior to BoNT administration were fully protected from a lethal BoNT dose. These studies elucidate general mechanisms for the neutralization of toxins by HP pairs and demonstrate the potential utility of HPs as BoNT therapeutics.
- Molecular immunology.Mol Immunol.2014 Feb;57(2):247-54. doi: 10.1016/j.molimm.2013.09.005. Epub 2013 Nov 1.
- Immune complexes formed between monoclonal antibodies (mAbs) and toxins can neutralize toxicity in vivo by multiple mechanisms. Toxin sequestration and clearance by mAbs may be improved by enhancing their ability to bind to red blood cells (RBCs) through immune adherence. This can be achieved by con
- PMID 24184879
- Versatile Roles of CspA Orthologs in Complement Inactivation of Serum-Resistant Lyme Disease Spirochetes.
- Hammerschmidt C, Koenigs A, Siegel C, Hallström T, Skerka C, Wallich R, Zipfel PF, Kraiczy P.Author information Institute of Medical Microbiology and Infection Control, University Hospital of Frankfurt, Frankfurt, Germany.AbstractCspA of the Lyme disease spirochete Borrelia burgdorferi represents a key molecule in immune evasion, protecting borrelial cells from complement-mediated killing. As previous studies focused almost exclusively on CspA of B. burgdorferi, here we investigate the different binding capacities of CspA orthologs of Borrelia burgdorferi, B. afzelii, and B. spielmanii for complement regulator factor H and plasminogen and their ability to inhibit complement activation by either binding these host-derived plasma proteins or independently by direct interaction with components involved in formation of the lethal, pore-like terminal complement complex. To further examine their function in serum resistance in vivo, a serum-sensitive B. garinii strain was used to generate spirochetes, ectopically producing functional CspA orthologs. Irrespective of their species origin, all three CspA orthologs impart resistance to complement-mediated killing when produced in a serum-sensitive B. garinii surrogate strain. To analyze the inhibitory effect on complement activation and to assess the potential to inactivate C3b by binding of factor H and plasminogen, recombinant CspA orthologs were also investigated. All three CspA orthologs simultaneously bound factor H and plasminogen but differed in regard to their capacity to inactivate C3b via bound plasmin(ogen) and inhibit formation of the terminal complement complex. CspA of B. afzelii binds plasmin(ogen) and inhibits the terminal complement complex more efficiently than CspA of B. burgdorferi and B. spielmanii. Taken together, CspA orthologs of serum-resistant Lyme disease spirochetes act as multifunctional evasion molecules that inhibit complement on two central activation levels, C3b generation and assembly of the terminal complement complex.
- Infection and immunity.Infect Immun.2014 Jan;82(1):380-92. doi: 10.1128/IAI.01094-13. Epub 2013 Nov 4.
- CspA of the Lyme disease spirochete Borrelia burgdorferi represents a key molecule in immune evasion, protecting borrelial cells from complement-mediated killing. As previous studies focused almost exclusively on CspA of B. burgdorferi, here we investigate the different binding capacities of CspA or
- PMID 24191298
- Detection of cell membrane-bound CD46 using flow cytometry.
- Kolev M, Kemper C.Author information Division of Transplantation Immunology and Mucosal Biology, MRC Centre for Transplantation, King's College London, Guy's Hospital, London, UK.AbstractCD46 is an important regulator of the complement system by preventing unwanted deposition of the complement activation products and opsonins C3b/C4b onto self-tissue. Recently, intracellular signals mediated by CD46 activation on several distinct human cell types have demonstrated that CD46 also plays decisive roles in immuneregulation. The growing recognition of CD46 as key regulator in several vital biological processes, led to increased demand in sensitive methods for monitoring CD46 expression and changes thereof on cells and in tissues. Here we describe a method, which allows for studying CD46 expression on the surface of cells using specific antibodies in combination with fluorescence-activated cell sorting (FACS) analysis.
- Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2014;1100:329-39. doi: 10.1007/978-1-62703-724-2_27.
- CD46 is an important regulator of the complement system by preventing unwanted deposition of the complement activation products and opsonins C3b/C4b onto self-tissue. Recently, intracellular signals mediated by CD46 activation on several distinct human cell types have demonstrated that CD46 also pla
- PMID 24218272
- 緑藻 クロレラ Chlorella pyrenoidosa より得られたペプチドヘテロ多糖体の補体 C3 と腹腔マクロファージに及ぼす影響
- Effects of endosulfan on the immune function of erythrocytes, and potential protection by testosterone propionate
- カラオケ部屋有 2時間半-3,000円飲み放題+歌い放題 Bar料金1,000円〜 1970年代のソウルロックポップス昭和歌謡等 アナログレコード レコード4,000枚 リクエストOK
- factor D, D
- 第二経路、C3, C3b, B, C3bBb, C3a
- C3b inactivator, C3b INA
- complement C3b、C3b complement
- 補体第三成分 third component of complement
- 補体、C3a, C3b
- C3 convertaseによってC3aとC3bを生じる
- C3 convertase活性を持つのは２つ
- 1. C4bC2a (古典的経路)
- 2. C3bBbP (別経路)