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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 252 (1995), S. 249-254 
    ISSN: 1434-4726
    Keywords: Middle ear ; Glycoconjugate ; Wheat germ agglutinin ; Electron microscopy ; Guinea pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To evaluate the protective function of the mucous blanket (MB) against lectin substances, we examined at the ultrastructural level whether intraluminal colloidal gold-labelled wheat germ agglutinin (WGA) could enter the MB-covered epithelial cell surface of the guinea pig tubotympanic mucosa. Post-embedding staining with WGA/gold on thin tissue sections was done in parallel for comparison. The cell surface glycoconjugate of the eustachian tubal and transitional epithelium had a typical bilayered structure: the outer MB and the microvilli-associated glycocalyx (MAG), which were interposed by the interciliary fluid zone. In squamous epithelium of the distal middle ear, the MB adhered to the MAG, thereby forming a monolayered coat of glycoconjugates at the cell surface. In the pre-embedding staining, WGA/gold did not bind with the MB and MAG in the eustachian tube, and exclusively bound with MB in the transitional area. Direct binding was also found with MAG and the apical plasmic membrane in the squamous epithelium. These findings indicate that MAG is occluded by MB lined with the interciliary fluid zone for luminal access of lectin at the proximal lumina of the tubotympanic epithelium. It is also suggested that MB existing at two sites possesses a different WGA-binding capacity: shielding as a “dust cover” in the eustachian tube and entrapping as a “flypaper” against lectin in the transitional area of the middle ear.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 254 (1997), S. 145-149 
    ISSN: 1434-4726
    Keywords: Eighth nerve compound action potential ; Aging effects ; Guinea pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The eighth nerve compound action potential (CAP) in 95 guinea pigs was measured using click stimuli to investigate age-related changes in their neural auditory thresholds. The animals were separated into three groups: group A (n = 43, 86 ears; 2–4 months old); group B (n = 29; 58 ears, 13–15 months old); and group C (n = 23; 46 ears, 23–25 months old). With increasing age, a gradual elevation of CAP thresholds was clearly seen among the three groups. The negative peak (N1) latencies of the CAP were prolonged, and the N1 amplitudes of the CAP decreased. There were significant differences in N1 latencies among the three groups and in N1 amplitudes between groups A and B, and between groups A and C. However, the rate of decline of the thresholds as well as the input-output function curves of the CAP varied in some of the oldest animals, suggesting that there were some individual differences in degenerative aging processes of the auditory system.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 250 (1993), S. 412-417 
    ISSN: 1434-4726
    Keywords: Sugar-binding site ; Guinea pig ; Middle ear ; Lipopolysaccharide ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Glucosamine-binding sites were detected in Lowicryl K4M-embedded guinea pig middle ear mucosa by electron microscopy, using glucosaminyl bovine serum albumin. Incubation of ultrathin tissue sections with gold-labeled glucosaminyl bovine serum albumin (GlcN/BSA/gold) resulted in binding mainly on cilia, microvilli, rough endoplasmic reticulum and nuclei. The sugar binding was not inhibited after ultrathin sections had been digested with trypsin or neuraminidase. Various carbohydrates and glycoconjugates were tested as competitive inhibitors of G1cN/BSA/gold labeling on the tissue sections. The sugar specificity range detected by the glucosamine-binding sites included glucosamine, N-acetylglucosamine, mannose and fucose, whereas N-acetylgalactosamine, galactose and glucose were not detectable. A series of endotoxic substances such as Salmonella minnesota Re595 lipid A complex with BSA and lipopolysaccharides (LPS) derived from Escherichia coli 055: B5 or S. minnesota Re595 also competed with GlcN/BSA/gold binding. This indicates that the lipid A backbone glucosamine or other carbohydrate portions of LPS is a part of the structure recognized by glucosamine binding sites.
    Type of Medium: Electronic Resource
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