کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9141914 | 1163886 | 2005 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
IgG naturally occurring antibodies stabilize and promote the generation of the alternative complement pathway C3 convertase
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کلمات کلیدی
VBSIVIgnAbsMPGNNaturally occurring antibodiesC3 Nephritic factor - C3 فاکتور خونیantibodies - آنتی بادی هاinflammation - التهاب( توروم) Human - انسانautoimmunity - خودایمنیveronal-buffered saline - فلوئور بافر فلوئورComplement - متممalternative pathway of complement - مسیر جایگزین مکملmembranoproliferative glomerulonephritis - گلومرولونفریت غشایی غشایی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: IgG naturally occurring antibodies stabilize and promote the generation of the alternative complement pathway C3 convertase IgG naturally occurring antibodies stabilize and promote the generation of the alternative complement pathway C3 convertase](/preview/png/9141914.png)
چکیده انگلیسی
Normal human IgG contains naturally occurring anti-C3 antibodies (anti-C3 NAbs) that have been proposed to regulate complement amplification. Here, we report a novel procedure for anti-C3 NAb purification. Pooled human IgG was fractionated on a DEAE column prior to affinity chromatography on IgG and then on C3. Anti-C3 NAbs co-purified with anti-F(abâ²)2 NAbs. In a refined protocol, IgG fractions were absorbed on Fc, F(abâ²)2, and C3, which allowed to isolate the directly accessible NAbs and to remove IgG hinge-region-specific NAbs. Since a substantial fraction of total anti-C3 NAbs in whole IgG pre-existed as complexes, IgG that did not bind to the three affinity columns was treated with urea and the affinity chromatography repeated to collect the dissociated NAbs. The urea-accessible anti-F(abâ²)2 NAbs were rather pure but anti-C3 NAbs yet contained substantial amounts of anti-F(abâ²)2 NAbs. Anti-C3 NAbs showed up to 400-fold and anti-F(abâ²)2 NAbs, up to 30-fold enrichment as compared to pooled normal human IgG. Anti-C3 NAb preparations exhibited nephritic factor activity that was up to 60 times stronger than that of total IgG from a patient with membranoproliferative glomerulonephritis type 2. In addition, anti-C3 NAbs promoted C3 convertase generation, when added to the convertase precursor or during convertase assembly, suggesting a non-nephritic-factor mechanism. Factors H and I reduced the overall level of activity but had no influence on the NAb dose-response curve meaning that NAbs did not interfere with factor H binding. Convertase promoting activity during assembly correlated with the content of anti-C3 NAbs in NAb complexes. In conclusion, anti-C3 NAbs associated with framework-specific anti-idiotypic NAbs stabilize C3 convertase and promote its generation but their activity is compensated for in whole IgG.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular Immunology - Volume 42, Issue 11, July 2005, Pages 1393-1403
Journal: Molecular Immunology - Volume 42, Issue 11, July 2005, Pages 1393-1403
نویسندگان
Emiliana Jelezarova, Hans U. Lutz,