The erythrocyte–immune complex–glomerulonephritis connection in man

Hebert, Lee A.; Cosio, Fernando G.

doi:10.1038/ki.1987.81

Cited by 88 publications

(38 citation statements)

References 36 publications

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“…These C3b-opsonized ICs can bind to cellular receptors specific for C3b (5) in a process defined by Nelson as the immune adherence reaction (6,7). Binding of these antibody-pathogen ICs to the immune adherence receptor (CR1) on circulating cells (platelets in nonprimates [8,9] and erythrocytes in primates [1][2][3][4][5]10]) may serve to prevent the pathogen from leaving the bloodstream and emigrating to susceptible organs and tissues (4,11). Moreover, it is likely that in primates, the erythrocyte-bound ICs are handled by a mechanism in which they are transferred to and destroyed by phagocytic cells in the liver and spleen, with little damage to the erythrocytes (1)(2)(3)(4)6,7,11,12).…”

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confidence: 99%

“…In the circulation of immunized animals, recognition of complex and multivalent foreign antigens or pathogens can lead to the formation of immune complexes (ICs), which rapidly activate complement and covalently capture C3b (1)(2)(3)(4). These C3b-opsonized ICs can bind to cellular receptors specific for C3b (5) in a process defined by Nelson as the immune adherence reaction (6,7).…”

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confidence: 99%

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Clearance of anti-double-stranded DNA antibodies: The natural immune complex clearance mechanism

Craig

Bankovich

McElhenny

et al. 2000

Arthritis & Rheumatism

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Objective. To develop an in vitro model for investigating the mechanism by which autoantibodies in immune complexes (ICs) that are bound to primate erythrocytes via antigen-based heteropolymers (AHPs) are cleared from the circulation and localized to the liver.Methods. IgG anti-double-stranded DNA (antidsDNA) antibodies in ICs with dsDNA were bound to human erythrocytes via complement receptor 1 (CR1) either by opsonization with normal human serum as a complement source or through the use of an AHP, which consists of an anti-CR1 monoclonal antibody (mAb) that is chemically crosslinked with dsDNA. We performed parallel investigations of the mechanism of transfer of both types of erythrocyte-bound ICs to a monocytic cell line (U937). Erythrocytes with CR1-bound ICs were incubated with U937 cells under a variety of conditions, and subsequently, the levels of IgG anti-dsDNA, CR1, AHP, or C3b on both erythrocytes and U937 cells were measured by flow cytometry with appropriate fluorescently labeled probes.Results. In the presence of U937 cells, both the AHP-anti-dsDNA and C3b-opsonized ICs were rapidly removed from the erythrocytes; at 37°C, more than half of the complexes were removed in 2 minutes. Monomeric mouse IgG2a mAb blocked the transfer of both types of complexes by 75%, suggesting that Fc␥ receptor type I (Fc␥RI) is the main phagocyte receptor responsible for the removal of ICs from erythrocytes. Levels of CR1 on the erythrocyte surface were reduced during transfer of the AHP-anti-dsDNA ICs, suggesting that transfer involves a concomitant removal of CR1, presumably by proteolysis.Conclusion. Transfer of AHP-anti-dsDNA ICs from erythrocyte CR1 to model phagocytes occurs by a mechanism that is similar to the natural mechanism of IC clearance, involving recognition by Fc␥RI and removal of erythrocyte CR1 as key steps.

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confidence: 99%

mentioning

confidence: 99%

Clearance of anti-double-stranded DNA antibodies: The natural immune complex clearance mechanism

Craig

Bankovich

McElhenny

et al. 2000

Arthritis & Rheumatism

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“…The primate erythrocyte is thought to play an important role in the clearance of circulating immune complexes (IC) (reviewed in [1]). IC, incorporating complement component C3b, bind to CR1 on erythrocytes (E-CR1) [2][3][4] and are then transported to the liver and/or spleen where IC may be removed and degraded by cells of the fixed tissue macrophage system [5].…”

Section: Introductionmentioning

confidence: 99%

Complement coating of erythrocytes is reduced following their interaction with neutrophils in vitro without loss of complement receptor 1 (CR1)

Imrie

Jones

1997

Clinical and Experimental Immunology

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SUMMARYWe have investigated the interaction of complement-coated erythrocytes (E) with neutrophils, in vitro, to determine the effects of erythrocyte CR1. Complement-coating in vitro, to mimic immune complex uptake, caused a reduction in E-CR1, but subsequent interaction with neutrophils effected a removal of E-C3b and a return of E-CR1 to levels approximating that of uncoated erythrocytes. These data indicate that C3b, associated with immune complexes, may bind to E-CR1 in a reversible manner and that subsequent interaction with phagocytes need not necessarily result in cleavage (and loss of ) E-CR1. Further, we conclude that E-CR1 can apparently be reduced by epitope masking.

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“…mAbs to CR1 (12,16,17), human IgG (14), and the dinitrophenyl (DNP) group (6) were purified from ascites fluid by treatment with octanoic acid and precipitation with 50%6 saturated ammonium sulfate (14) or by affinity chromatography on Sepharose-linked protein G (Pharmacia LKB). Cross-linked heteropolymers were prepared using N-succinimidyl-3-(2-pyridyldithio)propionate (SPDP) (18)(19)(20).…”

Section: Methodsmentioning

confidence: 99%

“…He provided intriguing evidence that this reaction plays an important role in the body's defense against microorganisms by facilitating their phagocytosis after adherence and immobilization on RBCs. Recent studies in the nonhuman primate by Hebert and coworkers (5,6) as well as reports from other laboratories (7)(8)(9) indicate that immune adherence of soluble complement-opsonized IC to RBCs via CR1 provides a vehicle for safe and rapid clearance of potentially pathogenic IC from the circulation. Defects in this RBC-based clearance reaction have been shown in a number ofdiseases (10)(11)(12) and are believed to presage disease activity, such as enhanced deposition of inflammatory IC in susceptible tissues and organs (13).…”

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confidence: 99%

Use of heteropolymeric monoclonal antibodies to attach antigens to the C3b receptor of human erythrocytes: a potential therapeutic treatment.

Taylor

Sutherland

Reist

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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The erythrocyte–immune complex–glomerulonephritis connection in man

Cited by 88 publications

References 36 publications

Clearance of anti-double-stranded DNA antibodies: The natural immune complex clearance mechanism

Clearance of anti-double-stranded DNA antibodies: The natural immune complex clearance mechanism

Complement coating of erythrocytes is reduced following their interaction with neutrophils in vitro without loss of complement receptor 1 (CR1)

Use of heteropolymeric monoclonal antibodies to attach antigens to the C3b receptor of human erythrocytes: a potential therapeutic treatment.

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