Immune complex binding efficiency of erythrocyte complement receptor 1 (CR1)

Madi, Nada; Paccaud, Jean‐Pierre; Steiger, G; Ja, Schifferli

doi:10.1111/j.1365-2249.1991.tb08116.x

Cited by 36 publications

(6 citation statements)

References 19 publications

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“…Mouse anti‐human CR1 MoAb 3D9 was a gift from Professor J. Atkinson (University of Washington, St Louis, MO, USA). This blocks the binding of C3b to CR1 on erythrocytes [22]. The MoAb 3.9 against CR4 (CD11c) was a gift from Dr N. Hogg (Cancer Research UK, London) while the mouse anti‐human CR3 MoAb 2LPM19c (IgG 1 kappa) was obtained from Dako [23].…”

Section: Methodsmentioning

confidence: 99%

Both Fcγ and complement receptors mediate transfer of immune complexes from erythrocytes to human macrophages under physiological flow conditionsin vitro

Hepburn

Mason

Wang

et al. 2006

Clinical and Experimental Immunology

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SummaryAbnormal clearance by the mononuclear phagocytic system of immune complexes (IC) is important in the pathogenesis of systemic lupus erythematosus (SLE). We have developed an in vitro model to investigate the cellular mechanisms involved in the transfer of soluble IC from erythrocytes to human macrophages under physiological flow conditions. In this assay, erythrocytes bearing fluorescently labelled IC are perfused over monolayers of human monocytes or monocyte-derived macrophages in a parallel-plate flow chamber, and transfer quantified using confocal microscopy and flow cytometry.

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Section: Methodsmentioning

confidence: 99%

Both Fcγ and complement receptors mediate transfer of immune complexes from erythrocytes to human macrophages under physiological flow conditionsin vitro

Hepburn

Mason

Wang

et al. 2006

Clinical and Experimental Immunology

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“…[6][7][8] Previous studies have shown that CR1 on human erythrocytes is constitutively expressed in large clusters, which were thought to be important for promoting multivalent ligand binding. 9,10 These results were based on indirect immunofluorescence methods or binding studies. [9][10][11] In addition, 2 different electron microscopy methods that used a 2-step erythrocyte staining with anti-CR1 Ab and immunogold-labeled secondary Ab reported either 2-15 or 30-75 immunogold particles per CR1 cluster.…”

Section: Introductionmentioning

confidence: 99%

“…9,10 These results were based on indirect immunofluorescence methods or binding studies. [9][10][11] In addition, 2 different electron microscopy methods that used a 2-step erythrocyte staining with anti-CR1 Ab and immunogold-labeled secondary Ab reported either 2-15 or 30-75 immunogold particles per CR1 cluster. 9,12 We demonstrated previously that storage and ex vivo manipulation of erythrocytes induced CR1 clustering as well as an apparent decrease in the total number of CR1 molecules on erythrocytes.…”

Section: Introductionmentioning

confidence: 99%

Ligation of erythrocyte CR1 induces its clustering in complex with scaffolding protein FAP-1

Ghiran

Glodek

Weaver

et al. 2008

Blood

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The primary identified function of complement receptor 1 (CR1/CD35) on primate erythrocytes is to bind complementtagged inflammatory particles including microbes and immune complexes. When erythrocytes circulate through liver and spleen, sinusoidal phagocytes remove CR1-adherent particles and erythrocytes return to the circulation. This process of immune adherence clearance is important for host defense and prevention of autoimmunity. CR1 was previously described as clustered in the human erythrocyte membrane, which was thought to be necessary for binding complementopsonized particles. In contrast, we demonstrate that on erythrocytes CR1 is not clustered, but dispersed, and able to bind complement-tagged particles. When fresh erythrocytes are solubilized by nonionic detergent, CR1 partitions to the cytoskeleton fraction. Using a PDZ-peptide array, CR1's cytoplasmic tail, which contains 2 PDZ-motifs, binds PDZ domains 2, 3, and 5 of Fas-associated phosphatase 1 (FAP-1), a scaffolding protein. We show that FAP-1, not previously recognized as an erythroid protein, is expressed on circulating erythrocytes. CR1 and FAP-1 coimmunoprecipitate, which confirms their molecular association. Disperse CR1 on erythrocytes may be advantageous for capturing immune-complexes, while ligation-induced CR1 clustering may prevent ingestion of the erythrocyte during the immune-complex transfer to the macrophages by keeping the opsonic stimulus localized thus preventing phagocyosis. (Blood. 2008;112:3465-3473) IntroductionEvolution of a closed circulatory system necessitated an efficient means of clearing the intravascular space of inflammatory particles, for example, microbes and immune complexes. To accomplish this task, vertebrates first tag the particles with complement opsonins, predominately C3b, then immobilize the particles by ligation to a cell expressing a complement receptor: process known as immune adherence. 1 Nonprimate vertebrates use platelets and adherent factor H as the complement receptor to capture circulating opsonized particles. 2,3 Once platelets bearing their cargo reach the liver or spleen, resident phagocytes remove the entire platelet-particle complex. 2,3 In contrast, primates use erythrocytes and complement receptor 1 (CR1 or CD35) to ligate complement-tagged inflammatory particles to their membranes. 4,5 When primate erythrocytes with immune-adherent particles move through the liver and spleen, sinusoidal macrophages remove only the immune-adherent particles and allow erythrocytes to return to the circulation. [6][7][8] Previous studies have shown that CR1 on human erythrocytes is constitutively expressed in large clusters, which were thought to be important for promoting multivalent ligand binding. 9,10 These results were based on indirect immunofluorescence methods or binding studies. [9][10][11] In addition, 2 different electron microscopy methods that used a 2-step erythrocyte staining with anti-CR1 Ab and immunogold-labeled secondary Ab reported either 2-15 or 30-75 immunogold particles per CR1 cluste...

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“…Plasmodium falciparum exploits CR1 as an adhesion-ligand in the process of rosetting, the pathogenic clumping of erythrocytes [6]. Destruction of erythrocytes, however, cannot be solely explained by the direct effect of the parasite [7][8], or by deposition of parasite-derived antigen nor by its surface damage through IgG and complement-regulatory proteins or complementfixation [9][10] or alternatively C3b-bearing ICs via CR1 reticulo-endothelial system [11][12].…”

Section: Introductionmentioning

confidence: 99%

Unraveling the C-reactive Protein Complement-Cascade in Destruction of Red Blood Cells: Potential Pathological Implications in <i>Plasmodium Falciparum</i> Malaria

Ansar

Habib²,

Roy³

et al. 2009

Cell Physiol Biochem

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Background: Deficiencies of the complementregulatory proteins on RBC (RBC Mal ) of patients with Plasmodium falciparum were reported. Here, we sought to determine the role of affinity-purified Creactive protein from patients (CRP Mal ), in modulating the complement-regulatory proteins and downstream effect on complement-cascade. Methods: CRP Mal was characterized by analytical ultracentrifuge and electrophoretic analysis. Surface plasmon resonance, Western blotting, co-immuno-precipitation, flowcytometry and ELISA determined the binding of CRP Mal with RBC Mal . Modifications of membranes for RBC Mal -CRP Mal binding were explored by scanning electron microscopy, osmotic and turbulence fragility, hydrophobicity and oxyhemoglobin release. Flowcytometry, ELISA, Western blotting and Scatchard analysis monitored the status of complementregulatory proteins on RBC Mal . Complement-activation via CRP Mal was quantified by C3-deposition and hemolysis. Results: CRP Mal binds specifically to RBC Mal through distinct molecules. Such binding altered the normal discoid-shape of RBC Mal with increased membrane fluidity and hydrophobicity. In the presence of CRP, RBC Mal showed reduced complementregulatory proteins (CR1 or CD35, CD55 and CD59) with decreased affinity. These changes caused enhanced C3-deposition and complement-mediated hemolysis. Conclusion: Taken together, we have established the contributory effect of CRP Mal causing decreased complement-regulatory proteins, possibly providing a new mechanism of complement-fueled RBC Mal destruction refractory to erythrophagocytosis and may account for pathogenesis of anemia.

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Immune complex binding efficiency of erythrocyte complement receptor 1 (CR1)

Cited by 36 publications

References 19 publications

Both Fcγ and complement receptors mediate transfer of immune complexes from erythrocytes to human macrophages under physiological flow conditionsin vitro

Both Fcγ and complement receptors mediate transfer of immune complexes from erythrocytes to human macrophages under physiological flow conditionsin vitro

Ligation of erythrocyte CR1 induces its clustering in complex with scaffolding protein FAP-1

Unraveling the C-reactive Protein Complement-Cascade in Destruction of Red Blood Cells: Potential Pathological Implications in <i>Plasmodium Falciparum</i> Malaria

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