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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of cosmetic science 8 (1986), S. 0 
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Lipids found in the skin are derived both from the keratinized epidermis and from the sebaceous glands. The composition of human sebum and epidermal lipids has only been fully elucidated during the past few years, and the role of these lipids is still being evaluated. This presentation reviews sebaceous gland structure and function composition of human sebum, the effects of aging and hormones on sebum secretion and the role of sebum in acne and in dry skin. In addition, a review of the role of epidermal lipids in the properties of skin includes consideration of the structure and function of the epidermis, the composition of the epidermal lipids, and the function of lipids in epidermal differentia-tion and water barrier properties. Le rǒle du sébum et des lipides de I'épiderme dans les propriétes cosmétiques de la peau
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 39 (1967), S. 218-221 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 40 (1968), S. 827-828 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 272 (1982), S. 343-349 
    ISSN: 1432-069X
    Keywords: Sebum ; Sebaceous glands ; Physiology of sebaceous glands ; Transit time of sebum ; Talg ; Talgdrüsen ; Physiologie der Talgdrüsen ; Transitzeit der Talgdrüsen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Aufgrund der Arbeiten von Kligman nehmen die meisten Untersucher an, daß eine kontinuierliche Funktion der Talgdrüsen den Talg zur Hautoberfläche befördert. Sowohl in den peripheren Zellen der Talgdrüsenlobuli wie auch in Ansammlungen von undifferenzierten Zellen, die sich durch das Drüsenparenchym ziehen, werden differenzierende Zellpopulationen durch mitotische Aktivität aufrechterhalten. Nach Ausbildung eines Drüsenläppchens bildet dieser, solange er durch zirkulierende Hormone unterhalten wird, fortwährend einen Strom von differenzierenden Zellen. Während sie sich gegen den Talgdrüsengang bewegen, akkumulieren die Zellen Talg und platzen schließlich, um ihren Inhalt in den Ausführungsgang zu entleeren. Nach intradermaler Markierung mit 3H-Thymidin während der DNS-Replikation der germinativen Zellen dauert es 28 Tage bis alle markierten Zellen aus den Drüsen verschwinden. Werden differenzierende Zellen mit 3H-Aminosäuren markiert, verliert sich die Markierung überwiegend innerhalb 7 Tagen. Auch wenn Lipide mit 14C-Acetat markiert werden, beträgt die durchschnittliche Sekretionsdauer des markierten Talgs 8 Tage. Hierzu kann die Erneuerungszeit undifferenzierter Zellen addiert werden, so daß sich eine durchschnittliche Transitzeit der Talgdrüsenzellen von 14 Tagen ergibt. Aus der Zeit zwischen Synthese und Sekretion des Talgs wurde anhand des Talggehalts von Stanzbiopsien die Produktionsrate des Talgs errechnet. Die Durchgangszeit des Talgs im Follikelkanal wurde auf etwa 14 h geschätzt. Die so bestimmten Produktionsraten stimmen gut mit den Werten überein, die durch Langzeitabsorption des Talgs an der Hautoberfläche gemessen wurden.
    Notes: Summary Following the studies of Kligman, most investigators now believe that sebaceous glands function continuously in excreting sebum to the skin surface [7, 8]. Populations of differentiating cells are maintained by mitotic activity both in the peripheral cells of the sebaceous lobules and in aggregations of undifferentiated cells which extend through the body of the lobules. Once formed, and as long as maintained by circulating hormones, each lobule continues to produce a stream of differentiating cells which accumulate sebum as they move towards the sebaceous duct and finally disrupt to release their contents into the pilosebaceous canal. After intradermal injections of 3H-thymidine to label germinative cells during DNA replication, up to 28 days elapse before all labeled cells disappear from the glands. When differentiating cells are labeled with 3H-amino acids, much of the label is lost in 7 days. Likewise, when lipids are labeled with 14C-acetate, the average excretion time for the labeled sebum is 8 days. To this time may be added the renewal time of undifferentiated cells to give an average sebaceous cell transition time of 14 days [15]. From knowledge of the time between synthesis and excretion of sebum, sebum production rates were calculated from the sebum content of punch biopsies. The transit time of sebum in the follicular canals was estimated to be 14 h. Production rates determined in this way agree with those measured by long-term absorption of sebum at the skin surface.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 23 (1995), S. 204-217 
    ISSN: 0887-3585
    Keywords: α-helix ; β-helix ; β-strand ; oligomerization ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Mammalian epidermal keratin molecules adopt rod-shaped conformations that aggregate to form cytoplasmic intermediate filaments. To investigate these keratin conformations and the basis for their patterns of molecular association, graphical methods were developed to relate known amino acid sequences to probable spacial configurations. The results support the predominantly α-helical conformation of keratin chains, interrupted by short non-α-helical linkages. However, it was found that many of the linkages have amino acid sequences typical of β-strand conformations. Space-filling atomic models revealed that the β-strand sequences would permit the formation of 2-chain and 4-chain cylindrical β-helices, fully shielding the hydrophobic amino acid chains that alternate with hydrophilic residues in these sequences. Because of the locations of the β-helical regions in human and mouse stratum corneum keratin chains, only homodimers of the keratins could interact efficiently to form 2-chain and 4-chain β-helices. Tetramers having the directions and degrees of overlap of constituent dimers that have been identified by previous investigators are also predicted from the interactions of β-helical motifs. Heterotetramers formed from dissimilar homodimers could combine, through additional β-helical structures, to form higher oligomers having the dimensions seen in electron microscopic studies. Previous results from chemical crosslinking studies can be interpreted to support the concept of homodimers rather than heterodimers as the basis for keratin filament assembly. © 1995 Wiley-Liss, Inc.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Pharmaceutical research 9 (1992), S. 1415-1421 
    ISSN: 1573-904X
    Keywords: stratum corneum ; ceramides ; 2H nuclear magnetic resonance (NMR) ; bilayer ; hexagonal phase ; hydrogen bonding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Hydrated lipid mixtures consisting of stratum corneum ceramides, cholesterol, specifically deuterated palmitic acid, and cholesteryl sulfate were investigated by solid-state 2H NMR spectroscopy at different temperatures. The mole ratio of cholesterol to ceramides was varied from 1 to 0. 2H NMR spectra from these mixtures showed powder patterns with quadrupolar splittings smaller than those obtained from control mixtures containing dipalmitoylphosphatidylcholine (DPPC) instead of the ceramides. This result is attributed to the rigid amide group of the ceramides, with a planar configuration, which could prevent close packing of the α-methylenes of the acyl chains. There was a gradual loss of symmetry in the powder pattern as the amount of cholesterol was decreased and the amount of ceramides (or DPPC) was increased concomitantly. The loss was more pronounced in the ceramide-containing samples. This phenomenon is interpreted as a decrease in the axial reorientation rate of the α-deuterated palmitic acid in the bilayers, presumably caused by the increased hydrogen bonding resulting from the high amount of hydroxyl-bearing ceramides. Spectra obtained at temperatures above 60°C indicated the formation of a hexagonal phase (HII) by the ceramide-containing mixtures. Spectra of the ω-deuterated palmitic acid in the mixture containing 76 mol% ceramides and no cholesterol indicated phase separation into a more rigid phase and a more mobile phase in the temperature range of 25 to 60°C. The bilayer configuration of lipids at 25°C was confirmed by thin-section electron microscopy.
    Type of Medium: Electronic Resource
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