IgM natural autoantibodies against bromelain-treated mouse red blood cells recognise carbonic anhydrase
| Autor: | Steele Ej, Cox Ko, Jonusys Am |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Erythrocytes
Immunology Immunoblotting Enzyme-Linked Immunosorbent Assay Mice Inbred Strains Immunoglobulin E Binding Competitive Epitopes Mice Carbonic anhydrase medicine Immunology and Allergy Glycophorin Animals Autoantibodies Carbonic Anhydrases chemistry.chemical_classification biology Molecular biology Bromelains Blot Red blood cell Enzyme medicine.anatomical_structure chemistry Biochemistry Immunoglobulin M biology.protein Female Antibody Glycoprotein |
| Zdroj: | Autoimmunity. 9(3) |
| ISSN: | 0891-6934 |
| Popis: | Carbonic anhydrase (CA) from mouse erythrocyte membranes is recognised as an autoantigen in Western blotting experiments with FUB 1, a murine IgM monoclonal antibody that binds both phosphatidylcholine and bromelain-treated mouse red blood cells (BrMRBC). Serum from mice stimulated with lipopolysaccharide (LPS-serum) also recognises CA. From SDS-PAGE, and blotting experiments with whole mouse erythrocytes, we found two closely spaced glycoprotein bands in the 30 kD region that reacted with both FUB 1 and LPS-serum. One of the molecular weight markers, bovine carbonic anhydrase which is of a molecular weight of about 30 kD, electrophoresed in the same 30 kD region also reacted with these antibodies. Carbonic anhydrases from a range of mammalian species were found to be crossreactive with FUB 1 and LPS-serum by Western blotting, whereas human glycophorin A and human asialoglycophorin were not recognised by the antibodies. FUB 1 specifically recognises both native and denatured bovine carbonic anhydrase in ELISA assays. The serological identity of the determinants of CA and BrMRBC was confirmed by specific absorption of both FUB 1 and LPS-serum with BrMRBC and normal mouse erythrocytes. We propose that a native autoantigenic epitope on erythrocytes may be revealed by the proteolytic action of bromelain and that this determinant is associated, at least in part, with carbonic anhydrase. |
| Databáze: | OpenAIRE |
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