Journal of the Japan Organization of Clinical Dermatologists
Online ISSN : 1882-272X
Print ISSN : 1349-7758
ISSN-L : 1349-7758
Volume 24, Issue 4
Displaying 1-5 of 5 articles from this issue
  • Yasumasa Ishibashi
    2007 Volume 24 Issue 4 Pages 292-297
    Published: July 15, 2007
    Released on J-STAGE: March 13, 2009
    JOURNAL FREE ACCESS
    Amyloidosis is characterized by remarkable deposition of homogenous insoluble material, amyloid, in the intra- or extra-cellular space of various tissues or organs. Amyloid is a generic term, which derives from certain diverse, approximately 20, sequentially unrelated proteins. This substance is little produced in normal individual, and characterized by showing a peculiar conformational change, named as the cross-β-sheet structure. Protein chains, newly synthesized from ribosome must be folded to compact three-dimensional structures in endoplasmic reticulum(ER), if they may be functionally active. As the protein folding, however, is not always done correctly, such proteins must be degraded or scavenged by ubiquitin-proteasome pathways and/or molecular chaperone systems, because they are prone to aggregate in the tissue.. The neurodegenerative disorders, such as Alzheimer's disease, are directly associated with the aggregation of abnormal protein. The aggregates in such disorders all exhibit, more or less, certain characteristics to be identical to amyloid, which is recently proposed to emerge through the process of protein degradation by proteasomes. In the field of dermatology, a familiar type of primary localized cutaneous amyloidosis(FPLCA) seems to be the most suitable research targets for understanding amyloidgenesis. In this paper, I reviewed the histogenesis of amyloid in FPLCA under the novel concept of protein folding and misfolding, and discussed on the possibility of functional failures of ubiquitin-proteosome pathways and/or molecular chaperone systems, and finally prospected how we can prevent the merging of this substance in comparison with that in Alzheimer's disease. (Online only)
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  • [in Japanese], [in Japanese], [in Japanese], [in Japanese]
    2007 Volume 24 Issue 4 Pages 310-313
    Published: July 15, 2007
    Released on J-STAGE: March 13, 2009
    JOURNAL FREE ACCESS
  • Yukio Sasagawa
    2007 Volume 24 Issue 4 Pages 314-318
    Published: July 15, 2007
    Released on J-STAGE: March 13, 2009
    JOURNAL FREE ACCESS
    We encountered a 10-month-old girl who developed refractory black-dot ringworm of the head caused by Trichophyton tonsurans. The source of infection was her mother, who had played judo until 3 years before marriage. The present case raised the following issues: the oral administration of antimicrobial agents to infants aged 10 months was limited; we hesitated to administer oral therapy, considering the risk of a side effect-related lawsuit; her mother had been an asymptomatic carrier over 3 years; her father was also infected, and all 3 family members developed this disorder; and the reliability of fungus identification by the clinical laboratory was low. Trichophyton tonsurans infection spreads not only among judo practitioners but also to their families via vertical infection. The important point in Trichophyton tonsurans or Microsporum canis infection control is to pursue the source of infection and prevent its transfer to a new population. An education program to improve dermatologists'; ability to identify fungus must be developed as soon as possible. It is important to promote the role of dermatologists in society via preventive medicine-based activities. In patients with alopecia of the head, black-dot ringworm should always be considered. On consultations, it must be recognized that judo practitioners consist of both males and females. (Online only)
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