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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 279 (1986), S. 95-99 
    ISSN: 1432-069X
    Keywords: Protein kinase C ; Pig epidermis ; Protein phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Endogenous calcium-activated, phospholipid-dependent protein kinase phosphorylates pig epidermal protein. Pig epidermis was homogenized and centrifuged at 30,000xg for 30 min. The supernatant was incubated with or without calcium and phospholipid. A 97 kD soluble protein from pig epidermis was phosphorylated in the presence of calcium and phosphatidylserine. The phosphorylation reaction occurred immediately. With the use of two-dimensional polyacrylamide gel electrophoresis, it was shown that the 97 kD fragment was a basic protein, and that several small proteins were also phosphorylated. The characterization of these proteins is yet to be undertaken.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 61 (1987), S. 440-442 
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The junction down mounting attached to a Si-submount with Au-Si solder has been shown to be very reliable for lasers by aging tests of 5 mW at 80° C. The thermal resistance of this junction down mounting is 30 K/W smaller than that of a junction up mounting. Output powers as high as cw 80 mW/stripe, corresponding to 400 mW, was realized without saturation with a five-stripe phase-locked laser array with an inner-stripe configuration assembled on this mounting.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    British journal of dermatology 115 (1986), S. 0 
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We studied the effect of Ionophore A23187 (A23187) on phospholipid degradation and the accumulation of cyclic GMP in pig epidermis. A23187 stimulated the release of AA, probably partially through the activation of phospholipase A. A23187 also stimulated the accumulation of epidermal cyclic GMP, but the activity of cyclic GMP-dependent phosphodiesterases was not altered. Mepacrine, an inhibitor of phospholipase A*, inhibited the A23i87-stimulated accumulation of cyclic GMP. The results suggest that A23i87 stimulates the accumulation of epidermal cyclic GMP by a calcium-dependent process which also requires products of phospholipid degradation.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 83 (1985), S. 189-193 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Normal human gastric mucosal cells were examined by light and electron microscopy using lectins as a probe. The ABC method was used with biotinylated lectins for light microscopy and HRP-labeled lectins for electron microscopy. The human gastric mucosal cells revealed specific binding patterns for each lectin by light microscopy. Among the lectins tested, in particular, DBA gave a characteristic pattern. It specifically stained the supranuclear region of surface epithelial cells and the perinuclear region of parietal cells. By electron microscopy, the stacked cisternae and the vesicles of the Golgi apparatus of the surface epithelial cells were positive for the DBA staining. These results show that the DBA-positive supranuclear region observed by light microscopy corresponds to the Golgi apparatus. In the parietal cells, DBA, RCA and ConA bound to the intracellular secretory canaliculi which are invaginations of the cell membrane running around the nucleus in the cytoplasm. Therefore, the tubular perinuclear positive region observed by light microscopy corresponds to the membranes of the intracellular secretory canaliculi. In addition, the ConA reagent stained the endoplasmic reticulum, Golgi apparatus, nuclear envelope, and cell membrane of the parietal cell, which explains the diffuse cytoplasmic staining observed at the light microscopic level with this lectin. Lectins have proved to be very useful for the evaluation of in situ cytochemical aspects of the glycoconjugates characteristic to human gastric mucosal cells.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-069X
    Keywords: TPA ; Protein kinase C ; E5166 ; Retinoids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 12-o-Tetradecanoylphorbol-13-acetate (TPA) activates calcium-activated, phospholipid-dependent protein kinase (protein kinase C) partially purified in an ion exchange column from pig epidermis. Protein kinase C was activated by TPA in a concentration-dependent manner with simultaneous addition of Ca2+ and phospholipid. Polyprenoic acid derivative (E5166) which is a newly synthesized retinoic acid derivative, inhibited the TPA activation of protein kinase C. This inhibition may explain the mechanisms by which retinoids inhibit TPA-induced tumor promotion.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-069X
    Keywords: Polyprenoic acid derivative ; Ornithine decarboxylase ; Epidermis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Irradiation of skin with ultraviolet B (UVB) stimulates epidermal activity of ornithine decarboxylase (ODC), a rate limiting polyamine biosynthesing enzyme. The maximum stimulation of ODC activity by UVB was found at 24 after irradiation. Systemic administration of a polyprenoic acid derivative (E-5166) significantly inhibited the UVB-stimulated ODC activity in a dose-dependent manner. The inhibitory effect of E-5166 on the UVB-stimulated ODC activity was found to begin at 5 mg/kg body weight. These results indicate that because it inhibits ODC activity E-5166 can be utilized for the treatment of hyperproliferative skin diseases.
    Type of Medium: Electronic Resource
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