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- W2045171612 abstract "Naturally occurring anti-band 3 antibodies (anti-band 3 NAbs) are directed against the 55-kDa chymotryptic fragment of the anion transport protein (band 3) of red blood cells (RBCs). They bind to senescent and oxidatively stressed RBCs and induce their selective clearance. These IgG NAbs exist at low concentrations, and have a weak affinity that prevents them from actively recruiting second binding sites. Cellular senescence or oxidative damage induces a cascade of biochemical events that results in the detachment of band 3 from the cytoskeleton and in clustering of band 3 protein by bound hemichromes and Syk kinase. Clustered band 3 proteins allow bivalent binding of anti-band 3 NAbs. Bivalently bound anti-band 3 NAbs have the unique capacity to stimulate C3b deposition by preferentially generating C3b2-IgG complexes, which act as potent C3 convertase precursors of the alternative complement pathway. Antibody binding not only to clustered, but also to oligomerized band 3 protein further increases if the human plasma also contains induced anti-lactoferrin antibodies. These bind to the polylactosaminyl oligosaccharide, a carbohydrate that exists in lactoferrin and in the 38-kDa fragment of band 3 protein. Anti-lactoferrin antibodies are found primarily in plasma of patients with autoimmune diseases and who have anti-neutrophil cytoplasmic antibodies (ANCA).Natürlicherweise vorkommende Anti-Bande-3-Antikörper (Anti-Bande-3-NAbs) sind gegen das chymotrypti-sche 55-kDa-Fragment des Anionenaustauschproteins der roten Blutkörperchen (RBCs) (Bande 3) gerichtet, binden an alte und oxidativ geschädigte RBCs und induzieren deren selektive Phagozytose. Diese NAbs sind IgG-Immunglobuline und haben eine schwache Affinität, welche sie daran hindert, aktiv Zweitbindungsstellen zu rekrutieren. Zelluläre Alterung oder oxidative Schädigungen induzieren eine Kaskade von biochemischen Vorgängen, die in der Ablösung der Bande-3-Proteine vom Zytoskelett resultieren und die Verklumpung von Bande 3 in der Membran durch die Bindung von Hemichromen und Syk-Kinase begünstigen. Verklumpte Bande-3-Proteine erlauben eine bivalente Bindung der Anti-Bande-3-NAbs. Bivalent gebundene Anti-Bande-3-NAbs haben die Fähigkeit, die C3b-Deposition zu stimulieren indem sie präferentiell C3b2-IgG bilden, die als potente Vorläufer von alternativen C3-Konvertasen wirken. Die Antikörper-Bindung nicht nur an verklumpte, sondern bereits an oligomerisierte Bande-3-Proteine steigt weiter an, wenn humanes Plasma auch induzierte Anti-Laktoferrin-Antikörper enthält, die an das Polylactosylaminyl-Kohlehydrat binden, das in Laktoferrin vorkommt aber auch im 38-kDa-Fragment des Bande-3-Proteins. Anti-Laktoferrin-Antikörper treten bevorzugt im Plasma von Patienten mit Autoimmunkrankheiten auf, insbesondere solchen, die sich durch anti-neutrophile zytoplasmatische Antikörper (ANCA) auszeichnen." @default.
- W2045171612 created "2016-06-24" @default.
- W2045171612 creator A5054243093 @default.
- W2045171612 date "2012-01-01" @default.
- W2045171612 modified "2023-09-30" @default.
- W2045171612 title "Naturally Occurring Anti-Band 3 Antibodies in Clearance of Senescent and Oxidatively Stressed Human Red Blood Cells" @default.
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- W2045171612 doi "https://doi.org/10.1159/000342171" @default.
- W2045171612 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3678295" @default.
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