Epitope recognized by anti-glomerular basement membrane (GBM) antibody in a patient with repeated relapse of anti-GBM disease
| Autor: | Sakiko Masuda, Xiao-yu Jia, Ming-Hui Zhao, Daigo Nakazawa, Utano Tomaru, Zhao Cui, Satoshi Tanaka, Akihiro Ishizu, Yuka Nishibata, Mandkhai Nergui, Kimimasa Nakabayashi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
medicine.drug_class Anti-Glomerular Basement Membrane Disease Clinical Biochemistry Monoclonal antibody Autoantigens Epitope Pathology and Forensic Medicine 03 medical and health sciences Type IV collagen Young Adult 0302 clinical medicine Recurrence Glomerular Basement Membrane medicine Humans Molecular Biology anti-GBM disease Autoantibodies Basement membrane relapse epitope biology business.industry Glomerular basement membrane type IV collagen protease Primary and secondary antibodies Molecular biology 030104 developmental biology medicine.anatomical_structure 030220 oncology & carcinogenesis biology.protein Immunohistochemistry Epitopes B-Lymphocyte Female Antibody business |
| Zdroj: | Experimental and Molecular Pathology. 107:165-170 |
| ISSN: | 0014-4800 |
| Popis: | The major epitopes recognized by autoantibodies in anti-glomerular basement membrane (GBM) disease are found in the α3-subunit non-collagenous domain of type IV collagen [α3(IV)NC1], which is present in the glomerular and alveolar basement membranes. These epitopes are structurally cryptic, owing to the hexamer formation of the non-collagenous domain of α3, α4, and α5 subunits and are expressed by the dissociation of the hexamer. Anti-GBM disease usually manifests as a single attack (SA), and we rarely see patients who repeatedly relapse. We recently treated a patient with anti-GBM disease who exhibited repeated relapse (RR). Here, we conducted immunohistochemistry of formalin-fixed paraffin-embedded normal kidney sections and immunoblotting using recombinant human α3(IV)NC1 to compare the epitopes recognized by anti-GBM antibodies in the RR patient and SA patients. Although a clear staining of GBM especially in the connecting basement membrane of Bowman's capsule was observed when IgGs of SA patients were used as primary antibodies, such staining was not obtained when IgG of the RR patient was employed. In immunoblotting of α3(IV)NC1 using the IgG of the RR patient as a primary antibody, an 18-kDa band was detected besides the 56.8-kDa band corresponding to the whole-size α3(IV)NC1. Whereas the 56.8-kDa band disappeared after digestion of the recombinant α3(IV)NC1 by protease, the 18-kDa band remained. Furthermore, the 18-kDa band was not detected by a commercially available anti-α3(IV)NC1 monoclonal antibody. These findings suggest that the IgG of the RR patient recognizes the epitope distinct from that recognized by the anti-α3(IV)NC1 monoclonal antibody. |
| Databáze: | OpenAIRE |
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