A novel membrane glycoprotein capable of inhibiting membrane attack by homologous complement

Okada, Noriko; Harada, Ryuhei; Fujita, Teizo; Okada, Hidechika

doi:10.1093/intimm/1.2.205

Cited by 183 publications

(113 citation statements)

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“…This covered all the Thr (10,13,29) and Ser (20,21) residues, which are potential O-glycosylation sites, in the first half of the CD59 molecule. The data that were obtained were identical to the published amino acid sequence (45,46). The repetitive yields for the five residues at potential sites for O-glycosylation were close to the predicted value (data not included).…”

Section: Characterization Of the O-glycans Attached To Humansupporting

confidence: 69%

The Glycosylation of the Complement Regulatory Protein, Human Erythrocyte CD59

Rudd

Morgan

Wormald

et al. 1997

Journal of Biological Chemistry

164

103

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Section: Characterization Of the O-glycans Attached To Humansupporting

confidence: 69%

The Glycosylation of the Complement Regulatory Protein, Human Erythrocyte CD59

Rudd

Morgan

Wormald

et al. 1997

Journal of Biological Chemistry

164

103

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“…Three cell-associated regulators function intrinsically on the surface membranes of self cells for this purpose. In humans, these intrinsic regulators consist of DAF (Medof et al, 1984), membrane cofactor protein (CD46) (Seya et al, 1986), and CD59 (Davies et al, 1989;Holguin et al, 1989;Okada et al, 1989), all three of which are ubiquitously expressed on almost all cell types. In the mouse, DAF and CD59 are widely distributed on virtually all cells as in humans, whereas membrane cofactor protein is expressed significantly only in the testis.…”

Section: Discussionmentioning

confidence: 99%

Decay-Accelerating Factor Confers Protection Against Complement-Mediated Podocyte Injury in Acute Nephrotoxic Nephritis

Lin

Emancipator

Salant

et al. 2002

Laboratory Investigation

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SUMMARY:Decay-accelerating factor (DAF or CD55) is one of a set of regulators that function to protect self cells from deposition of autologous C3b on their surfaces. Its relative importance in vivo, however, is incompletely understood. As one approach to address this issue, we induced nephrotoxic serum (NTS) nephritis in wild-type mice and Daf1 gene-floxed mice devoid of renal DAF expression. For these experiments NTS IgG was administered at a dose (0.5 mg iv) that requires complement for glomerular injury. After 18 hours, renal injury was assessed by proteinuria and by histologic, immunohistochemical, and electron microscopic analyses of kidneys. Fifteen normal and 15 DAF-deficient mice were studied. Baseline albuminuria in the Daf1 Ϫ/Ϫ mice was 115.9 Ϯ 41.4 g/mg creatinine as compared with 85.7 Ϯ 32.3 g/mg creatinine in their Daf1 ϩ/ϩ littermates (p ϭ 0.075). After administration of NTS IgG, albuminuria increased to 2001.7 Ϯ 688.7 g/mg creatinine as compared with 799.7 Ϯ 340.5 g/mg creatinine in the controls (p ϭ 0.0003). Glomerular histology was similar in Daf1 Ϫ/Ϫ and Daf1 ϩ/ϩ mice, with essentially no infiltrating leukocytes. In contrast, electron microscopy revealed severe podocyte fusion in the Daf1 Ϫ/Ϫ mice but only mild focal changes in the controls. Immunohistochemical staining showed equivalent deposition of the administered (sheep) NTS IgG in the Daf1 Ϫ/Ϫ and Daf1 ϩ/ϩ animals. This contrasted with marked deposition of autologous murine C3 in the former and minimal deposition in the latter. The results show that DAF is essential physiologically for protecting glomeruli against autologous complement attack initiated by the classical pathway. (Lab Invest 2002, 82:563-569).D ifferent forms of nephrotoxic serum (NTS)-induced nephritis in rats and mice have been widely utilized as animal models for human antibodyinduced renal diseases (reviewed in Salant and Cybulsky, 1988). The mechanism of glomerular damage differs, depending on the source and dose of the antibody and the time after antibody administration (Boyce and Holdsworth, 1985;Salant and Cybulsky, 1988). When a low dosage of sheep NTS is given to mice, complement plays a significant role in the early heterologous phase of nephritis (Hebert et al, 1998;Quigg et al, 1998aQuigg et al, , 1998bSchrijver et al, 1988). This has been verified either by depleting serum complement proteins with cobra venom factor (Quigg et al, 1998b) or using C3 or C4 knock-out mice (Hebert et al, 1998). When the dosage of NTS is increased, the disease is in large part antibody mediated, and dependence on complement is diminished (Hebert et al, 1998). During the later autologous phase, especially if accelerated by preimmunization with heterologous IgG, a more fulminant, leukocyte-rich inflammatory lesion is induced (Lloyd et al, 1997).The sheep NTS used in these studies is specific for several podocyte cell surface proteins, including some that are known to be nephritogenic (Chugh et al, 2001). In addition, the proteinuria that develops in the early heterologous phase of g...

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“…Their and our experiments on CDC were performed with animal complement instead of human complement. Since human cells bear membrane proteins which inhibit attack by human complement (Okada et al, 1989), the CDC observed in vitro may not occur in the human body.…”

Section: Discussionmentioning

confidence: 99%

A human monoclonal antibody against varicella-zoster virus glycoprotein III

Sugano

Tomiyama²,

Matsumoto³

et al. 1991

Journal of General Virology

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Hybridomas producing human monoclonal antibodies (HMAbs) against varicella-zoster virus (VZV) were generated by fusing murine myeloma cells with human lymphocytes immunized in vitro. An assay system was developed to select anti-glycoprotein (gp)III HMAbs from the pool of anti-VZV HMAbs. A murine antigplII MAb, 4B7, did not react with a VZV-infected cell homogenate, but did react with a VZV-infected cell monolayer, whereas anti-gpI and anti-gplI MAbs reacted with both antigens. Hybridomas were screened to obtain HMAbs having a reaction profile similar to that of 4B7 and one such clone, V3, stably produces human IgG1 (x). HMAb V3 immunoprecipitated a VZV antigen of l15K to 120K, which was not immunoabsorbed by an anti-gplI HMAb, implying that V3 recognizes gpIII. V3 neutralized VZV independently of complement, unlike anti-gpI and anti-gplI HMAbs. All five strains of VZV tested were completely neutralized by V3, and the dose of V3 required to reduce the number of virus plaques by 50% ranged from 0-027 to 0.15 ~tg/ml. V3 was also able to inhibit the spread of virus infection from infected to uninfected cells, whereas anti-gpI and anti-gplI HMAbs could not. In addition, V3 mediated antibody-dependent cellular cytotoxicity but not complement-dependent cytotoxicity of VZV-infected cells. The results suggest that an anti-gplII HMAb may provide a new means of passive immunoprophylaxis and also help to identify an antigenic epitope appropriate for a subunit vaccine.

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A novel membrane glycoprotein capable of inhibiting membrane attack by homologous complement

Cited by 183 publications

References 0 publications

The Glycosylation of the Complement Regulatory Protein, Human Erythrocyte CD59

The Glycosylation of the Complement Regulatory Protein, Human Erythrocyte CD59

Decay-Accelerating Factor Confers Protection Against Complement-Mediated Podocyte Injury in Acute Nephrotoxic Nephritis

A human monoclonal antibody against varicella-zoster virus glycoprotein III

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