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  • 1985-1989  (2)
  • Hair matrix proteins  (1)
  • Deiters neurones
  • Keratinization
  • PKC; protein kinase C
  • Rabbit
  • Vestibular
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 279 (1986), S. 112-119 
    ISSN: 1432-069X
    Keywords: Innermost cell layer ; Outer root sheath ; Anagen hair follicle ; Keratinization ; Light and electron microscopes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To investigate cell differentiation in the outer root sheath (ORS) of the human anagen hair follicle, scalp skin specimens from individuals with normal hair were examined using light and electron microscopes. In the bulbar portion, the ORS was composed of two cell layers. The cells in the outer layer gradually increased in number upwards and finally underwent so-called trichilemmal keratinization, which proceeded toward the hair canal. On the other hand, the inner cells in the bulb formed a single cell layer along the outside of Henle's layer during cell differentiation; this unique layer was referred to as the innermost cell (IMC) layer of the ORS. With the use of hematoxylin and eosin stain, at the suprabulbar portion, where Henle's cells were keratinizing, an eosinophilic substance was deposited in the inner (Henle's) side of the IMC cytoplasm. The IMCs gradually became entirely eosinophilic and often produced keratohyaline granules. Ultrastructurally, the IMCs of the ORS showed an oblong shape forming a regularly arranged single-cell layer along the keratinizing Henle's layer and accumulated tonofilaments in the cytoplasm. They produced a few small electron-dense keratohyaline granules and were keratinized at the level at which Henle's layer still preserved its cell structure. From these findings, it is suggested that there are two types of keratinization of the ORS: trichilemmal keratinization and IMC keratinization.
    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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