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  • 1
    Electronic Resource
    Electronic Resource
    Production of Immunosuppressing Melanotropins By Human Keratinocytes (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 680 (1993), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1993.tb19741.x
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  • 2
    Electronic Resource
    Electronic Resource
    Release of Oxygen-Free Radicals by Neutrophils Is Reduced by Photopheresis (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 636 (1991), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1991.tb33473.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Expression of the 72-kD heat shock protein is induced by ultraviolet A radiation in a human fibrosarcoma cell line (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Experimental dermatology 8 (1999), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1600-0625.1999.tb00369.x
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  • 4
    Electronic Resource
    Electronic Resource
    Linear focal elastosis (elastotic striae): increased number of elastic fibres determined by a video measuring system (1997)
    Oxford, UK : Blackwell Publishing Ltd
    British journal of dermatology 137 (1997), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1046/j.1365-2133.1997.19922073.x
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  • 5
    Electronic Resource
    Electronic Resource
    Expression of the 27-kDa heat shock protein in human epidermis and in epidermal neoplasms: an immunohistological study (1995)
    Oxford, UK : Blackwell Publishing Ltd
    British journal of dermatology 133 (1995), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1365-2133.1995.tb02615.x
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  • 6
    Electronic Resource
    Electronic Resource
    Mechanisms of photodamage of the skin and its functional consequences for skin ageing (2001)
    Oxford, UK : Blackwell Science Ltd
    Clinical and experimental dermatology 26 (2001), S. 0 
    Details
    ISSN: 1365-2230
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Chronic photodamage of the skin manifests itself as extrinsic skin ageing (photoageing) and photocarcinogenesis. DNA photodamage and UV-generated reactive oxygen species are the initial molecular events that lead to most of the typical histological and clinical manifestations of chronic photodamage of the skin. Knowledge of the UV-absorbing chromophores in the skin and of the molecular mechanisms leading to the unwanted effects of sun exposure provide a basis for the development of novel strategies for the prevention and repair of photoageing. This review provides an overview of the photochemistry of the major skin chromophores and their relationship to chronic photodamage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2230.2001.00893.x
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  • 7
    Electronic Resource
    Electronic Resource
    Subcorneal colocalization of the small heat shock protein, hsp27, with keratins and proteins of the cornified cell envelope (2002)
    Oxford, UK : Blackwell Science Ltd
    British journal of dermatology 147 (2002), S. 0 
    Details
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background hsp27 is a member of the small heat shock protein family. Its expression in epidermal keratinocytes in situ and in tissue culture correlates with differentiation. Experimental evidence points to the fact that hsp27 is a molecular chaperone and is involved in the regulation of cell growth and differentiation. Objectives To investigate whether epidermal hsp27 through its chaperone function plays a role in the assembly of keratin filaments and the cornified cell envelope. Methods We performed double staining immunofluorescence and immunogold microscopy on normal human skin (n = 15). We analysed the colocalization of hsp27 with actin, keratins and proteins of the cornified cell envelope (loricrin, filaggrin, transglutaminase 1). Results Actin staining did not reveal detectable colocalization with hsp27. For keratins, transglutaminase, loricrin and filaggrin colocalization was found in more than 60% of the samples. Colocalization was confined to a narrow subcorneal layer with varying patterns of expression. Electron microscopy revealed that loricrin and filaggrin colocalize with hsp27 indirectly through binding to intermediate filaments. Conclusions These results provide morphological evidence that in normal human skin hsp27 might act as a chaperone of cornification. Investigations of the molecular hsp27 interactions with the proteins of the cornified cell envelope are necessary to gain further insight into terminal keratinocyte differentiation and disorders of keratinization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2133.2002.04667.x
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  • 8
    Electronic Resource
    Electronic Resource
    Antibody formation against human collagen and C1q in response to a bovine collagen implant (1991)
    Springer
    Archives of dermatological research 283 (1991), S. 395-399 
    Details
    ISSN: 1432-069X
    Keywords: Bovine collagen implant ; Immune response ; Autoantibodies ; Human collagen ; C1q
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The humoral immune response to commercially available bovine collagen implants (Zyderm, Zyplast) is characterized in a 45-year-old female patient. Circulating anti-collagen antibodies were detected after eight injections of Zyderm and after two injections of Zyplast given during a period of 3 years. The specificity of these antibodies for bovine and human collagens as well as for the collagen-like region of C1q (a subcomponent of the first component of complement), was investigated by affinity chromatography. Serum levels of anti-collagen and anti-C1q antibodies were measured using ELISA. High levels of antibodies to bovine collagens, showing a strong cross-reactivity with human collagen type III were detected in the patient's serum. Only weak cross-reactivity with human collagen type I and IV and no reactivity with type II were observed. In addition, these antibodies specifically cross-reacted with the collagen-like region of C1q. The antibody levels decreased continuously and disappeared 1 year after cessation of treatment. These results demonstrate for the first time the formation of autoantibodies upon treatment with a bovine collagen implant. Although antibodies to collagens and C1q have been found in various autoimmune diseases, neither adverse reactions to the bovine collagen implant nor any other clinical symptoms were observed in association with the described antibody response.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00371822
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  • 9
    Electronic Resource
    Electronic Resource
    UVA- and UVB-induced changes in hairless mouse skin collagen (1994)
    Springer
    Archives of dermatological research 286 (1994), S. 490-494 
    Details
    ISSN: 1432-069X
    Keywords: Skin collagen ; UV effects ; Hairless mice ; Collagen solubility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract UVA- and UVB-induced alterations in dermal collagen were investigated in a murine animal model. Groups of hairless mice were exposed to UVA and UVB for 28 weeks at a dose of 60 J/cm2 three times weekly and 0.06 J/cm2 three times weekly, respectively. Untreated animals were used as controls. Every 4 weeks dorsal skin was examined for quantitative and qualitative changes in dermal collagen. Neither UVA nor UVB caused a significant alteration in total skin collagen content. However, after UVA treatment the ability of skin collagen to be digested by pepsin decreased dramatically (up to 65% of skin collagen remained insoluble after 4 months), whereas exposure to UVB had no significant effect. Furthermore a shift in the ratio of α1(I,III) chains to α2(I) chains was detected after UVA exposure. The amount of type V collagen in mouse skin, as determined by a sensitive ELISA method, was markedly decreased after UVA treatment, but not after UVB treatment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00371578
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