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  • Electronic Resource  (3)
  • 1995-1999  (3)
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  • Electronic Resource  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    British journal of dermatology 137 (1997), S. 0 
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We present an unusual case of linear focal elastosis occurring exclusively on the legs of a 13-year-old girl. An increase of elastic fibres (EF) was demonstrated histologically, and the number of EF in lesional and normal skin was quantified using a video measuring system. EF were found to be increased by about 100% in lesional skin compared with unaffected skin. EF were elongated, thinned and split at their ends with a paintbrush formation. Dedicated to Eva Jurkowitsch, MD, on the occasion of her birthday.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1600-0625
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The 72-kD heat shock protein (hsp72) belongs to a family of stress inducible proteins (heat shock proteins, hsp) and its expression is associated with increased survival of cells in culture following exposure to ultraviolet radiation (UV). Hsp72 can be induced by a number of stresses, including heat, cold, and toxic chemicals. The purpose of this study was to evaluate whether UV is able to activate transcription of hsp72. The human fibrosarcoma cell line HT1080 was used for these experiments because hsp72 is not detectable in these cells under normal culture conditions. Cells were exposed to UVA and UVB using a solar simulating source and hsp72 was determined in whole cell extracts by immunoblotting. For inhibition of mRNA and protein synthesis cordycepin (20 μg/ml) and cycloheximide (10 μg/ml) were added to the cultures, respectively. UVA-induced lipid peroxidation was inhibited by α-tocopherol and butylated hydroxytoluene (BHT). UVA but not UVB induced hsp72 with maximal expression at 40 J/cm2, 8–12 h after exposure. Induction was blocked by cordycepin as well as by cycloheximide indicating that both, mRNA and protein synthesis, are required for UVA-induction of hsp72. Inhibition of cell lipid peroxidation with α-tocopherol and BHT had no effect on hsp72 expression. These results suggest that induction of hsp72 is part of an adaptive response mechanism in human cells to UV-related stress.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    British journal of dermatology 133 (1995), S. 0 
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The 27-kDa heat shock protein (HSP27) is a member of the small heat shock protein (HSP) family. In addition to its putative function in thermotolerance, this protein may play a part in the regulation of cell growth and differentiation. This study was conducted to assess the significance of the expression of HSP27 in human epidermis and in cutaneous neoplasms. Sixty-two biopsy samples from normal human skin and from inflammatory and neoplastic skin diseases were investigated by immuno-histochemistry on formalin-fixed paraffin-embedded tissue sections, using a monoclonal antibody specific for HSP27.In normal human epidermis, HSP2 7 is expressed in the upper epidermal layers with a cytoplasmic staining pattern. The basal cell layer does not express detectable amounts of HSP27. In hair follicles, staining is mainly confined to the outer root sheath and to the infundibular epithelium. Melanocytes, dermal fibroblasts and endothelial cells do not express detectable amounts of HSP27. HSP27 could not be detected in fetal skin until the 20th week of gestation. Tumour cells in basal and squamous cell carcinomas do not express significant amounts of HSP27. In solar keratoses, seborrhoeic keratoses, human papillomavirus (HPV)-induced hyperproliferative lesions and inflammatory skin conditions, HSP27 expression largely resembles the pattern observed in normal human skin.HSP27 is expressed in a differentiation-related pattern in normal human epidermis and hyperproliferative disorders of the epidermis. We conclude that HSP27 may be regarded as a marker of differentiation in epidermal keratinocytes. Absence of HSP27 in the upper epidermal layers may be a marker for epidermal malignancy.
    Type of Medium: Electronic Resource
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