Anti-native and recombinant myeloperoxidase monoclonals and human autoantibodies

Audrain, Marie; Baranger, Thierry; Moguilevski, N.; Martin, Stéphane; Devys, Anne; Cm, Lockwood; Muller, Jean‐Yves; Esnault, Vincent

doi:10.1046/j.1365-2249.1997.d01-895.x

Cited by 34 publications

(26 citation statements)

References 19 publications

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“…Since MPO-ANCA did not react with human MPO under either reducing or heating conditions or both, it seems likely that MPO-ANCA recognize a critical region that contributes to the conformational epitope of MPO. The results support previous findings that MPO-ANCA recognize the native MPO, 28,29 although the MW of the target molecule is slightly different from the findings reported by others. This difference may be attributable to the methodology employed in Western blot analysis.…”

Section: Discussionsupporting

confidence: 83%

Antineutrophil cytoplasmic antibodies in patients with Graves? disease: association of antimyeloperoxidase autoantibodies with propylthiouracil therapy

Honda¹,

Shibata²,

Hara³

et al. 2003

Modern Rheumatology

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Section: Discussionsupporting

confidence: 83%

Antineutrophil cytoplasmic antibodies in patients with Graves? disease: association of antimyeloperoxidase autoantibodies with propylthiouracil therapy

Honda¹,

Shibata²,

Hara³

et al. 2003

Modern Rheumatology

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“…The mAb appears to recognize both heavy and light chain. This has been observed previously (Audrain et al, 1997). Sequence similarity suggests there may be common epitope(s), e.g., EPLAR (heavy chain) and EPAAR (light chain).…”

Section: Identification Of Mpo As a Binding Molecule For Sp-a And Sp-dsupporting

confidence: 79%

Surface-bound myeloperoxidase is a ligand for recognition of late apoptotic neutrophils by human lung surfactant proteins A and D

et al. 2010

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Surfactant proteins A (SP-A) and D (SP-D), both members of the collectin family, play a well established role in apoptotic cell recognition and clearance. Recent in vitro data show that SP-A and SP-D interact with apoptotic neutrophils in a distinct manner. SP-A and SP-D bind in a Ca 2+ -dependent manner to viable and early apoptotic neutrophils whereas the much greater interaction with late apoptotic neutrophils is Ca 2+ -independent. Cell surface molecules on the apoptotic target cells responsible for these interactions had not been identified and this study was done to find candidate target molecules. Myeloperoxidase (MPO), a specific intracellular defense molecule of neutrophils that becomes exposed on the outside of the cell upon apoptosis, was identified by affinity purification, mass-spectrometry and western blotting as a novel binding molecule for SP-A and SP-D. To confirm its role in recognition, it was shown that purified immobilised MPO binds SP-A and SP-D, and that MPO is surface-exposed on late apoptotic neutrophils. SP-A and SP-D inhibit binding of an anti-MPO monoclonal Ab to late apoptotic cells. Fluorescence microscopy confirmed that anti-MPO mAb and SP-A/SP-D colocalise on late apoptotic neutrophils. Desmoplakin was identified as a further potential ligand for SP-A, and neutrophil defensin as a target for both proteins.

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“…155 Audrain et al have shown that autoantibodies to human MPO are directed against at least four different epitopes. 156 Fujii et al have reported that the most common antigenic sites are regions on the upstream side of Met341 and Met409 near the N-terminus of the MPO heavy chain as well as on a domain on the downstream side of Gly598 near the C-terminus. 157…”

Section: Figure 21mentioning

confidence: 99%

Autoantibodies to intracellular autoantigens and their B-cell epitopes: Molecular Probes to Study the Autoimmune Response

Routsias

Vlachoyiannopoulos

Tzioufas

2006

Critical Reviews in Clinical Laboratory Sciences

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A common laboratory finding in systemic autoimmune diseases is the presence of autoantibodies against intracellular autoantigens. Although their pathogenesis is not fully understood, autoantibodies are important tools for establishing diagnosis, classification, and prognosis of autoimmune diseases. Autoantibodies mainly target multicomponent complexes containing both protein antigens and (ribo)-nucleic acid(s), such as the spliceosome or Ro/La RNPs. In this review, we address the main characteristics and the clinical value of the main autoantibody types with respect to their disease association, and we describe the corresponding autoantigens, their biologic function, and their B-cell antigenic determinants (epitopes). The structural characteristics and clinical associations of these epitopes, and their utility as tools to investigate the autoimmune response, are discussed in detail. New insights into the pathogenetic role of epitopes in systemic autoimmunity are also examined. In this regard, using the defined structures of the B-cell antigenic epitopes, complementary epitopes can be designed according to the "molecular recognition" theory. These complementary epitopes can be used as probes to study pathogenetic and immunoregulatory aspects of the anti-idiotypic response. The origin of humoral autoimmunity and the spreading of the epitopes in systemic lupus erythematosus are also discussed. Finally, the ability of post-translational modifications to induce autoreactive immune attack via the generation of neo-epitopes is summarized.

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Anti-native and recombinant myeloperoxidase monoclonals and human autoantibodies

Cited by 34 publications

References 19 publications

Antineutrophil cytoplasmic antibodies in patients with Graves? disease: association of antimyeloperoxidase autoantibodies with propylthiouracil therapy

Antineutrophil cytoplasmic antibodies in patients with Graves? disease: association of antimyeloperoxidase autoantibodies with propylthiouracil therapy

Surface-bound myeloperoxidase is a ligand for recognition of late apoptotic neutrophils by human lung surfactant proteins A and D

Autoantibodies to intracellular autoantigens and their B-cell epitopes: Molecular Probes to Study the Autoimmune Response

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