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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
    Springer
    Archives of dermatological research 279 (1987), S. 402-405 
    ISSN: 1432-069X
    Keywords: Hexadecane ; Protein kinase C ; Epidermal cell kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The application of hexadecane on animals skin induces hyperkeratinization and hyperplasia of the epidermis, however, the initial mechanisms of the epidermal cell proliferation and keratinization by hexadecane stimulation remains unknown. Protein kinase C is reported to be one of the critical enzymes involved in proliferation and differentiation of various cells and tissues. Therefore we investigated the effects of hexadecane on protein kinase C in pig epidermis. Protein kinase C activity of the pig skin increased 10 min after topical application of hexadecane to the back of the pig, normalized at 30 min, and subsequently kept falling for 24 h. In studying hexadecane dropped on floating sliced pig skin in Krebs buffer, similar results were obtained for the short term. Immediately after the hexadecane treatment, protein kinase C activity was not altered as compared with that of the untreated skin. Thus, the alteration of the protein kinase C activity after the hexadecane treatment is not due to the direct effect of hexadecane on the enzyme, but is due to other as yet unknown mechanisms of epidermal cell kinetics in response to hexadecane stimulation. We discuss the mechanisms of protein kinase C activity alteration upon treatment with hexadecane.
    Type of Medium: Electronic Resource
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  • 3
    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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