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  • 1
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of type V collagen in normal human skin (1988)
    Springer
    Archives of dermatological research 280 (1988), S. 145-151 
    Details
    ISSN: 1432-069X
    Keywords: Immunohistochemical localization ; Type V collagen ; Normal human skin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Tissue distribution of type V collagen in normal human skin was studied using an indirect immunofluorescent technique to determine whether type V collagen is present in the interstitium or in the basement membrane. Type V collagen was isolated from the human placenta by pepsin digestion and was purified with fractioning salt precipitations. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that type V collagen contained α1(V) and α2(V) chains, but not the α3(V) chain. Specificity of the rabbit antibodies to type V collagen was assessed using enzyme-linked immunosorbent assay (ELISA) and an immunoblotting method. Antibodies showed no cross-reactivity to other collagens, laminin, and fibronectin. With an indirect immunofluorescent technique, type V collagen was found to be widely distributed throughout the dermis. Intense fluorescent staining was noted in the papillary dermis and adnexal dermis surrounding hair follicles and eccrine glands. The basement membrane of the dermoepidermal junction, skin appendages, and capillaries was not stained. By indirect immunoperoxidase double staining, type V collagen was not found to be deposited on type IV collagen present in the basement membrane. Immunoelectron microscopic studies showed that type V collagen was not located in the basal lamina. These results suggest that type V collagen is distributed in the interstitium, but not in the basement membrane of normal human skin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00456844
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  • 2
    Electronic Resource
    Electronic Resource
    Primary cutaneous adenoid cystic carcinoma: ultrastructural study and immunolocalization of Types I, III, IV, V collagens and laminin (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of cutaneous pathology 17 (1990), S. 0 
    Details
    ISSN: 1600-0560
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A primary adenoid cystic carcinoma of the skin is reported. Light microscopy revealed pseudocysts. PAS-positive basement membrane and true glandular lumen, which in aggregates are specific for adenoid cystic carcinoma. Perineural invasion was also observed. Ultrastructural examinations revealed three types of cystic spaces; pseudocysts, true glandular lumens and intercellular spaces. Enzyme histochemical examinations showed positive reactions for eccrine enzymes, including phosphorylase and succinic dehydrogenase and negative for apocrine enzymes. Immunolocalization of collagens and laminin revealed that basement membranes of the pseudocysts involve Type V collagen as well as Type IV collagen and laminin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0560.1990.tb00115.x
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  • 3
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of lysyl oxidase in normal human skin (1994)
    Oxford, UK : Blackwell Publishing Ltd
    British journal of dermatology 131 (1994), S. 0 
    Details
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Lysyl oxidase (EC 1.4.3.13), a copper-dependent enzyme which catalyses the formation of aldehyde cross-links, and acts primarily on collagen and elastin, is known to be increased during wound healing and in fibrotic disorders including liver cirrhosis and atherosclerosis, and to be decreased in some hereditary connective tissue diseases and in malignant cell lines. A recent study showed that lysyl oxidase might possess tumour suppressor activity as an antioncogene for ras. Little is known about the localization of this enzyme in human skin. In this study, we determined immunohistochemically the localization of lysyl oxidase in normal skin of young and elderly subjects obtained from sun-exposed and unexposed regions of the body. All skin samples tested had similar distributions of lysyl oxidase. The enzyme was present both extracellularly and intracellularly. Extracellularly, a few granular aggregates of immunoreactants were observed along collagen and elastic fibres. These granules were more common in the adventitial portion of the dermis than in the reticular portion. Of all sun-exposed and unexposed regions studied, the skin of the face displayed the greatest amount of extracellular immunoreactants. Immunopositive granules were observed intracellularly in fibroblasts, vascular endothelial cells, sweat glands, sebaceous glands, arrector pili muscles and some keratinocytes. These findings provide evidence that, as suggested in recent reports, lysyl oxidase may have a variety of intracellular functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2133.1994.tb08518.x
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  • 4
    Electronic Resource
    Electronic Resource
    Increased expression of lysyl oxidase in skin with scleroderma (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: Summary Lysyl oxidase initiates cross-linkage of collagen and elastin by catalysing the formation of a lysine-derived aldehyde. In order to study cross-linking in scleroderma, we used monoclonal antibodies to lysyl oxidase to determine the localization of this enzyme in systemic and localized scleroderma, and compared the distributions obtained with that in normal skin. Using an indirect immunofluorescent antibody method and an avidin-biotinylated enzyme complex method. 11 cases of diffuse type of systemic scleroderma and seven cases of localized scleroderma were studied. In the oedematous stage of systemic scleroderma, intracellular and extracellular lysyl oxidase were remarkably increased in the dermis, particularly in groups around blood vessels. In the sclerotic stage of systemic scleroderma, lysyl oxidase was detected intracellularly in fibroblasts and extracellularly among collagen bundles between the lower dermis and the subcutaneous fat tissue. In localized scleroderma, a marked increase in lysyl oxidase was observed in mononudear cells and libroblasts near blood vessels in the lower dermis and in the subcutaneous fat tissue, in addition to the extracellular deposits between collagen bundles. The increase in lysyl oxidase in localized scleroderma was much more common than in the oedematous stage of systemic scleroderma. These findings indicated that intracellular and extracellular expression of lysyl oxidase expression was greater in sclerodermatous skin than in normal skin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2133.1995.tb02743.x
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  • 5
    Electronic Resource
    Electronic Resource
    Farber's lipogranulomatosis in siblings: light and electron microscopic studies (1989)
    Oxford, UK : Blackwell Publishing Ltd
    British journal of dermatology 121 (1989), S. 0 
    Details
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Two cases of Farber's lipogranulomatosis in siblings are reported. The clinical features included contractures of the limbs with swelling of the joints and subcutaneous nodules and erythematous infiltrated plaques. On histology there were many large foam cells in the dermis, and electron microscopy showed numerous large cells with round cytoplasmic lamellar and microtubular bodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2133.1989.tb08222.x
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  • 6
    Electronic Resource
    Electronic Resource
    Alteration of cartilagenous proteoglycan in psoriasis (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental dermatology 16 (1991), S. 0 
    Details
    ISSN: 1365-2230
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Articular tissue was obtained at surgery for a femoral neck fracture in a patient with psoriasis without arthritis. The proteoglycan of the cartilage of the sample was analysed biochemically. Normal cartilage is known to produce two types of proteoglycan monomers (fast- and slow-sedimenting groups), which are distinguishable by density-gradient ultracentrifugation. In the psoriatic cartilage analysed in the present study, it was shown that the former group was absent and only the latter group remained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2230.1991.tb00287.x
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  • 7
    Electronic Resource
    Electronic Resource
    Detection of lysyl oxidase gene expression in rat skin during wound healing (1995)
    Springer
    Archives of dermatological research 288 (1995), S. 7-10 
    Details
    ISSN: 1432-069X
    Keywords: Key words Lysyl oxidase ; Gene expression ; Wound healing ; Type III collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Lysyl oxidase (LOX) initiates the crosslinking of the lysine-derived aldehyde and plays an essential role in maturation of collagen, for example in wound healing. Although the activity of this enzyme has been examined in various disorders, and a further intriguing aspect of the relationship between LOX and tumorigenesis has recently emerged, its gene expression pattern in tissues is still unknown. We examined LOX gene expression during wound healing in rat skin. In addition, type III collagen gene expression was studied to determine the formation of fibrils. The LOX mRNA level reached a peak by day 3 after injury, which was earlier than that of type III collagen, and continued at a high level until day 22. The type III collagen mRNA level began to rise from day 3 and had increased intensely by day 22. In situ hybridization revealed grains corresponding to LOX mRNA in the fibroblasts of the granulomatous tissue. These results suggest that LOX is produced before collagen synthesis in preparation for crosslinking in the early phase of wound healing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004030050014
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