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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 252 (1995), S. 153-158 
    ISSN: 1434-4726
    Keywords: Superoxide dismutase ; Otitis media Inflammation ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cu, Zn superoxide dismutase (SOD) is a metalloprotein that catalyzes the dismutation of the superoxide anion into O2 − and H202, and therefore functions to maintain a low intracellular concentration of an otherwise toxic metabolite of oxygen. SOD protects living tissue from the destructive effects of free radicals. Increasing evidence implicates free radicals, including the superoxide radical (O2 −), in the pathogenesis of disease, including otitis media. In an effort to elucidate the role free radicals play in the pathogenesis of otitis media, SOD was localized immunocytochemically to determine its cellular distribution in specimens of guinea pig middle ear. In normal ears, SOD was found concentrated in the epithelium of the middle ear mucosa. Low quantities were characteristic of connective tissue, bone, and cartilage. In streptococcus-infected ears, SOD localized similarly, concentrating in the epithelium. The infected ears had extensive submucosal edema which stained poorly and appeared to have less SOD than did normal ears. This was confirmed by an assay using laser densitometry of Western blots to quantify the amount of SOD in the mucosa of normal versus infected middle ears. This demonstrated a value of SOD in normal mucosa of 1.77 ± 0.48 μg/mg of protein compared with 1.02 ± 0.28 μg/mg in the infected mucosa. The two groups were significantly different at P 〈 0.05. These findings are discussed, and suggestions for future experimentation addressed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 245 (1988), S. 160-165 
    ISSN: 1434-4726
    Keywords: Fibronectin ; Basal cell ; Cholesteatoma ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Fibronectin was localized in human cholesteatoma tissues by immunohistochemical methods. The avidin-biotin-peroxidase complex staining method was used with specific fibronectin antibody. Fibronectin appeared to be localized in the matrix of the cholesteatoma studied, particularly on the surface of the cell membranes and the nuclei of the basal cells and in connective tissue. Fibronectin was not seen in the granular layer or in the keratin area. Fibronectin was found on the surface of granulation tissue, mononuclear cells, fibroblasts and endothelial cells of blood vessels. These findings were confirmed by the immunofluorescent staining method. Our previous study showed that fibronectin induced a migration of keratinocytes, macrophages and fibroblasts demonstrated by the Boyden's chamber chemotaxis assay. Macrophages and fibroblasts were shown to produce collagenase, a bone resorption factor, in cholesteatomatous tissue. The present study showed the presence of fibronectin in the matrix of cholesteatoma and granulation tissue, suggesting that fibronectin might play an important role in the clinical development and invasive behavior of cholesteatoma.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 36 (1998), S. 357-366 
    ISSN: 0887-624X
    Keywords: surface graft copolymerization ; adhesive-free adhesion ; polycarbonate ; XPS ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The surfaces of ozone-pretreated polycarbonate films were subjected to further modification by thermally induced graft copolymerization with acrylic acid (AAc), sodium salt of styrene sulfonic acid (NaSS), N,N-dimethylacrylamide (DMAA), N,N-(dimethylamino)ethyl methacrylate (DMAEMA) and 3-dimethyl(methacryloyl ethyl)-ammonium propanesulfonate (DMAPS) monomers. The structure and composition at the copolymer interface were studied by angle-resolved X-ray photoelectron spectroscopy (XPS). For polycarbonate films with a substantial amount of grafted polymer, the hydrophilic graft penetrates or becomes partially submerged beneath a thin surface layer of dense substrate chains. This microstructure was further supported by the water contact angle measurements. Adhesive-free adhesion studies revealed that the AAc, DMAA or DMAPS graft copolymerized polycarbonate film surface adhered strongly to another similarly modified surface (homo-interface) when brought into direct contact in the presence of water and subsequently dried. The development of the lap shear strength is dependent on the concentration of the surface graft, the microstructure of the grafted surface, the adhesion (drying) time, and the nature of the interfacial interaction. The simultaneous presence of chain entanglement and electrostatic interaction readily results in substantially enhanced adhesion strengths between two DMAPS graft copolymerized surfaces or between an AAc and a DMAA graft copolymerized surface (hetero-interface). XPS analyses of the delaminated surfaces suggest that failure occurred cohesively below the graft-substrate interface. © 1998 John Wiley & Sons, Inc. J Polym Sci A: Polym Chem 36: 357-366, 1998
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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