201. High antibody levels against mouse laminin with specificity for galactosyl-(alpha 1-3)galactose in patients with inner ear diseases
- Author
-
Dietrich Plester, Reinhild Klein, Rupert Timpl, Fortunato R. Zanetti, and Peter A. Berg
- Subjects
Adult ,Male ,Immunoblotting ,Labyrinth Diseases ,Radioimmunoassay ,Fluorescent Antibody Technique ,Enzyme-Linked Immunosorbent Assay ,Immunofluorescence ,Disaccharides ,Epitope ,03 medical and health sciences ,Epitopes ,Mice ,0302 clinical medicine ,Laminin ,Antibody Specificity ,medicine ,Animals ,Humans ,030223 otorhinolaryngology ,Laminin binding ,medicine.diagnostic_test ,biology ,business.industry ,General Medicine ,medicine.disease ,Titer ,Otorhinolaryngology ,030220 oncology & carcinogenesis ,Immunology ,biology.protein ,Sensorineural hearing loss ,Female ,Antibody ,business - Abstract
Sera of 413 patients with inner ear diseases were examined for ELISA binding to mouse laminin and compared to a normal group. Strongly enhanced antilaminin antibody reactions were observed in a large number of patients with sensorineural hearing loss (68%), tinnitus (60%), and sudden deafness (46%), but not in those with Meniere's disease (14%) or normal individuals (8%). Absorption experiments demonstrated that these antibodies are also responsible for the antisarcolemmal antibody pattern in the immunofluorescence test and for the reaction with pig kidney microsomes in the ELISA. Immunochemical studies showed that laminin binding of high or low titer in sera from patients and normal individuals is due to the Galα1-3Gal epitope present in N-linked oligosaccharides of mouse laminin. No reactions were observed with human laminin, which lacks this epitope. The findings suggest that high levels of antibodies against carbohydrate structures are triggered by persistent infections, providing some new insights about the possible cause of these diseases.
- Published
- 1989