Quantitative determination of anti-dsDNA antibodies and antibody/dsDNA stoichiometries in prepared, soluble complement-fixing antibody/dsDNA immune complexes

Taylor, Ronald P.; Horgan, Carol

doi:10.1016/0161-5890(84)90139-1

Cited by 14 publications

(9 citation statements)

References 21 publications

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“…The IgG anti-dsDNA antibodies isolated from this plasma form soluble, C-fixing IC with dsDNA that bind to CR1 on human E (31,36). The biophysical and immunological properties ofthese IC have been extensively characterized both in vitro and in vivo in a number of animal systems (24,25,27,28,31,(34)(35)(36).…”

Section: Introductionmentioning

confidence: 99%

“…As a model IC system we used Ab/dsDNA IC because this antigen-antibody system is relevant to autoimmune disease (32,33), these model IC fix C efficiently and bind to E CR1 (34)(35)(36), and their slow release from E allows for direct investigation of potential E sequestration during the IC transfer process. In addition to conventional clearance studies, we used anti-Fcy receptor MAb infusions to probe the role of Fcy receptors in the removal of soluble IC from the circulation by the MPS.…”

Section: Introductionmentioning

confidence: 99%

“…These data, demonstrating that the transfer mechanism is much faster than C (Factor I) mediated spontaneous Preparation ofantibodies. The 7S IgG fraction of an SLE plasma (plasma Ma), which contains high titer nonprecipitating anti-dsDNA antibodies, was prepared as previously described (25,35). The IgG anti-dsDNA antibodies isolated from this plasma form soluble, C-fixing IC with dsDNA that bind to CR1 on human E (31,36).…”

Section: Introductionmentioning

confidence: 99%

“…These IC give > 90% binding in the Farr assay (38). To insure that the dsDNA was saturated with anti-DNA antibodies, soluble IC for the in vivo experiments were prepared at a two-to threefold higher Ab/dsDNA ratio (27,35). IC made with dsDNA of 500 bp are typically 50-100 S in size (34).…”

Section: Introductionmentioning

confidence: 99%

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In vivo handling of soluble complement fixing Ab/dsDNA immune complexes in chimpanzees.

Kimberly

Edberg²,

Merriam³

et al. 1989

J. Clin. Invest.

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We used soluble, C-fixing antibody/dsDNA IC to investigate immune complex (IC) handling and erythrocyte (E)-to-phagocyte transfer in chimpanzees. IC bound efficiently to chimpanzee E in vitro and showed minimal release with further in vitro incubation in the presence of serum in EDTA (c 15% within 1 h). These IC also bound rapidly to E in vivo (70-80% binding within 1 min) and did not show detectable release from E in the peripheral circulation after infusion in vivo (< 2% within 1 h). Despite such slow C-mediated release of IC from E, IC were rapidly stripped from E by the mononuclear phagocyte system (T50 for E-IC1500 = 5 min) without sequestration of E.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

In vivo handling of soluble complement fixing Ab/dsDNA immune complexes in chimpanzees.

Kimberly

Edberg²,

Merriam³

et al. 1989

J. Clin. Invest.

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“…In vitro demonstration of immunoglobulins bound to human RBC as components of prepared CF antibody/DNA immune complexes was performed according to our methods (33,341, as follows. Affinity-purified rabbit anti-human IgG (3 1) and goat anti-human IgM (Cappel-Worthington Biochemicals, Freehold, NJ) were '251-labeled with iodogen to a specific activity of -200 counts per minutelng and stored frozen in small aliquots.…”

Section: Simple Precipitation (2230)mentioning

confidence: 99%

The interaction of antibody/dna immune complexes with complement

Taylor

Edberg

Kujala

et al. 1987

Arthritis & Rheumatism

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In 28 serum and plasma samples from patients with systemic lupus erythematosus, we examined the importance of antibody class with respect to complement-mediated binding to human red blood cells (RBC) of antibody/DNA immune complexes (IC) prepared with anti-DNA antibodies. We used both 3H-double-stranded DNA and 3H-single-stranded DNA (ssDNA). Generally, double-stranded DNA IC showed considerably higher binding than did ssDNA IC in the RBC binding assay. Further analysis indicated that although ssDNA IC fix complement, it is necessary that these IC contain IgM anti-DNA antibodies in order for them to bind to RBC. The results suggest that the mechanisms of clearance and pathogenic potential of these IC may depend upon both the DNA conformation and antibody class. In particular, complement-fixing IC which contain IgG anti-DNA antibodies and ssDNA may not be cleared via the erythrocyte clearance mechanism, and therefore, Address reprint requests to Ronald P. Taylor, PhD, Department of Biochemistry, University of Virginia School of Medicine, Charlottesville, VA 22908.Submitted for publication March 19, 1986; accepted in revised form September 10, 1986. could be more likely to deposit in certain tissues and initiate inflammatory reactions.The results of extensive studies from a number of different laboratories indicate that complementfixing (CF) IgG antibody/double-stranded DNA (dsDNA) immune complexes (IC) play a significant role in the pathogenesis of systemic lupus erythematosus (SLE) (1-5). Although it is also believed that IC containing single-stranded DNA (ssDNA) may contribute to the pathogenesis of SLE (6,7), studies of these IC have been less frequent. This is because antibodies to dsDNA are more specific for SLE (3,8,9). In fact, care has often been taken to ensure that the DNA antigen used in SLE studies is not contaminated with ss regions (9-11). However, it has been demonstrated that IC prepared with ssDNA, and SLE sera containing anti-DNA antibodies, do fix complement, as defined by immune hemolysis techniques (12).Recently, Cornacoff and colleagues' findings in baboons (13) have raised considerable interest in the role of red blood cells (RBC) in the clearance of CF IC from the circulation. Their studies indicate that injected CF bovine serum albumin (BSA)/anti-BSA IC rapidly bind to the complement receptors of the baboon RBCs and are then taken to the liver, where the IC (but not the RBC) are removed from the circulation. In vitro studies (14) have shown that C F antibody/dsDNA IC also bind to the C3b receptors of human RBC, so it is likely that a similar clearance mechanism is operative in humans. The recent finding of a reduction in either the number of RBC C3b receptors or in their IC binding capacity, in ICmediated diseases such as SLE and rheumatoid arthri-

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