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  • 1985-1989  (2)
  • Electron microscopy  (1)
  • Hair fibrous proteins  (1)
  • Inhibition
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 281 (1989), S. 254-259 
    ISSN: 1432-069X
    Keywords: Innermost cell layer ; Tonofilaments ; Huxley's cells ; Henle's cells ; Anagen hair follicles ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To elucidate the biologic roles and further cytologic characteristics of the innermost cell (IMC) layer of the outer root sheath (ORS), human anagen hair follicles were ultrastructurally examined. In the lower follicle, the transeversely running tonofilaments in the inner side of the cytoplasm of the IMCs showed a massive accumulation, facing the keratinized part of a Huxley's cell protruding through a Henle's pore. In a rare instance, a spindle-shaped cell was seen between the IMC layer and the keratinized Henle's layer. At the lower isthmus portion, some of the IMCs containing a large number of tonofilaments showed a partial degeneration of the inner side of the cytoplasm. More distally, intercellular spaces between the keratinized IMCs and keratinized Henle's cells were partly dilated and contained amorphous substances. It is suggested that the IMCs in the lower follicle may play a role to support and cover the inner hair structures, tightly as hoops of a barrel. In the isthmus portion, the IMCs may loosely support and guide the keratinized Henle's cells undergoing degeneration.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 281 (1989), S. 495-501 
    ISSN: 1432-069X
    Keywords: Keratins ; Hair fibrous proteins ; Hair matrix proteins ; S-Carbamoylmethylation ; 2D-PAGE
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Human hair keratins are composed of hair fibrous proteins (HFP) forming 10-nm filaments and nonfilamentous cysteine-rich hair matrix proteins (HMP); these proteins are highly cross-linked by disulfide bonds. In order to obtain high-resultional separation of HFP and HMP by two-dimensional polyacrylamide gel electrophoresis according to isoelectric point (IP) in the first dimension and molecular weight (MW) in the second dimension, these proteins were converted to S-carbamoylmethylated (SCam) derivatives with nonionizable iodoacetamide; this treatment hardly modified the electrophoretic mobility. SCam-HFP were separated into polypeptides with MW 41.5–59 kD (IP pH 5.1-6.8). SCam-HMP were subdivided into two groups; 14 polypeptides of acidic HMP with MW 15-28 kD (IP pH 5.0-7.0) and 12 polypeptides of basic HMP with MW 18.5-28 kD (IP pH 7.8-8.8). Variation in electrophoretic patterns among hair samples obtained from 15 persons in four Japanese families was found in acidic HMP, but not in HFP in basic HMP. The present method appears to be very suitable for the biochemical analysis of human hair keratins, especially HMP of nonfilamentous proteins.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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