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  • Articles: DFG German National Licenses  (2)
  • 1985-1989  (2)
  • 1955-1959
  • Antikeratin autoantibodies  (1)
  • Hair cortex  (1)
Source
  • Articles: DFG German National Licenses  (2)
Material
Years
  • 1985-1989  (2)
  • 1955-1959
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 280 (1988), S. 308-318 
    ISSN: 1432-069X
    Keywords: Pili annulati ; Ultrastructure ; DACM staining ; Hair cortex ; Protein metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Plucked scalp hairs and hair roots of pili annulati were examined to understand their pathogenesis. Stereoscopic examinations of hairs in transmitted light and/or reflected light and light microscopic surveys of the cross-sections of hairs confirmed that the cortical empty spaces appeared to be responsible to the unique dotted shiny appearance of the hairs seen by the unaided eyes under a refracted light. By transmission electron microscope, small vacuoles and dense bodies were observed in the cytoplasm of the differentiating cortical cells; subsequently, with increasing number of tonofilaments, an uneven distribution of free ribosomes occurred and abnormal spaces containing fine granular substances were formed in the cytoplasm of the cortical cells. Occasionally, extremely large cortical trichohyaline granules were found. In the keratinized hair, irregular empty spaces were present in the cortex of the abnormal hair segments. Histochemically, the keratinized cortex of the affected hairs always had more residual SH groups than the controls. Pili annulati may be a disorder of protein metabolism involving a partial dysfunction of cytoplasmic ribosomes, resulting in a lack of cortical keratin formation.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 281 (1989), S. 377-382 
    ISSN: 1432-069X
    Keywords: Lichen amyloidosus ; Macular amyloidosis ; Antikeratin autoantibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In order to characterize immunoglobulins found on amyloid deposits of lichen amyloidosus and macular amyloidosis, an elution from cryostat sections was performed with citrate buffer, glycine buffer, NaCl, and PBS. Resulting eluates (mainly IgG) were examined with dot immunoblotting and SDS-PAGE immunoblotting and were found to react with the human epidermal keratin of 50 and 67 kD. Antikeratin autoantibody activities in normal murine and human sera were examined using a dot immunoblotting assay. In murine sera, titers of IgG and IgM autoantibodies were higher in older mice. The human cord blood showed significantly lower IgM autoantibody titers, whereas IgG antibody titers showed no significant differences from adults' sera, probably due to the permeability of IgG through the placental barrier. A stronger antibody activity in older individuals was thought to be due to the repeated exposures to keratin proteins derived from apoptotic keratinocytes. Sera from lichen amyloidosus and macular amyloidosis patients did not show any difference from normal controls in their antikeratin titers. It was concluded that the patients with lichenoid or macular amyloidosis are capable of producing a normal level of antikeratin autoantibodies. However, the removal of opsonized keratin-type amyloid from the skin is slow or deficient due to as yet unknown factors.
    Type of Medium: Electronic Resource
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