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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Archives of dermatological research 279 (1987), S. 530-535 
    ISSN: 1432-069X
    Schlagwort(e): Adenylate cyclase ; Cell culture ; Trichilemmoma
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The adenylate cyclase system of an established human trichilemmoma cell line was investigated. Stimulators of human epidermal adenylate cyclase system, epinephrine, histamine, adenosine, and prostaglandin E increased cyclic AMP levels of the trichilemmoma cells. The effects of epinephrine, histamine, and adenosine were inhibited by the addition of propranolol (a beta-adrenergic antagonist), cimetidine (histamine H2-antagonist), and theophylline (adenosinereceptor antagonist), respectively. The epinephrine, histamine, and protaglandin E effects were augmented by the addition of cyclic AMP (cAMP) phosphodiesterase inhibitor, isobutylmethylxanthine (IBMX); the adenosine effect was augmented by another phosphodiesterase inhibitor, papaverine. Without the addition of these phosphodiesterase inhibitors, the maximal accumulations were observed at 3 min incubation. Following this, the cAMP content returned to the basal level, and the cells did not respond to repeated stimulations with the same initial stimulator. This fact indicates receptor-specific refractoriness. For example, epinephrine-pretreated cells did not respond to epinephrine, but retained their sensitivity to histamine. It has been known that normal epidermal keratinocytes are regulated in vitro by glucocorticoids, colchicine, and retinoids, resulting in the augmentation of their beta-adrenergic response. Only hydrocortisone treatment on the trichilemmoma cells resulted in the augmentation of the beta-adrenergic response. Although the established human trichilemmoma cell line has similar adenylate cyclase systems as normal epidermis, it apparently has lost some of the regulatory mechanism of the beta-adrenergic response.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Virchows Archiv 436 (2000), S. 36-42 
    ISSN: 1432-2307
    Schlagwort(e): Key words Fabry disease ; Lysosomal deposit ; Glycosphingolipid ; Lectin histochemistry ; Enzyme digestion
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract  Fabry disease is an X-linked inborn error of glycosphingolipid catabolism resulting from a deficiency of lysosomal α-galactosidase activity. Globotriaosylceramide accumulates predominantly in lysosomes of various tissues. Former studies have clarified the nature of this disease, and the accumulated materials in the lysosomes have been analyzed using biochemical techniques. In the present study, transmission electron microscopy was used to reveal the fine structure of these lysosomal deposits, and sugar residues in the lysosomal deposits in Fabry disease were examined by lectin histochemistry combined with enzyme digestion. This is the first report to describe the lysosomal sugar residues in Fabry disease analyzed using lectin histochemistry at the ultrastructural level. With these techniques, we were able to detect α-galactosyl, β-galactosyl and glucosyl sugar residues in the lysosomal deposits. The experimental procedures used in this study have considerable potential for use in investigations of glycolipid and glycoprotein storage diseases without the need for complex methodology and expensive materials.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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