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  • Osteogenesis imperfecta  (3)
  • Procollagen mRNA  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Osteogenesis imperfecta: Biochemical and clinical evaluation of 13 cases (1981)
    Springer
    Journal of molecular medicine 59 (1981), S. 91-93 
    Details
    ISSN: 1432-1440
    Keywords: Collagen synthesis ; Fibroblast cultures ; Osteogenesis imperfecta ; Kollagensynthese ; Fibroblastenkulturen ; Osteogenesis imperfecta
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Hautfibroblasten wurden von 13 Patienten mit Osteogenesis imperfecta gezüchtet und deren Kollagensynthese in vitro untersucht. Dabei fand sich bei 7 Patienten, die durch nur milde Manifestation der Erkrankung charakterisiert waren, eine Störung des Verhältnisses der Kollagentypen I und III. Fibroblasten von solchen Patienten mit einer schweren Form der Osteogenesis imperfecta synthetisierten die Kollagentypen I und III in einem normalen Verhältnis.
    Notes: Summary Skin fibroblasts were cultured from 13 patients with Osteogenesis imperfecta and collagen biosynthesis was investigated in vitro. In those patients characterised by only mild manifestations of the disease, the ratio of collagen types I and III was disturbed. By contrast, fibroblasts obtained from patients with Osteogenesis imperfecta of a more severe type synthesised collagen types I/III in a normal ratio.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01477288
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Presence of type III collagen in bone from a patient with osteogenesis imperfecta (1977)
    Springer
    European journal of pediatrics 125 (1977), S. 29-37 
    Details
    ISSN: 1432-1076
    Keywords: Osteogenesis imperfecta ; Collagen types ; Bone ; In vitro study ; Immunofluorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Samples of bone from a patient with osteogenesis imperfecta were found to synthesize and contain type III collagen as well as type I collagen. Normal bone contains only type I collagen except in the lining cells of the bone marrow cavities. In the patient's tissue, type III collagen was localized in nonfibrillar structures in discrete areas of the bone. These and previous studies indicate that certain types of osteogenesis imperfecta may be caused by a failure of normal bone maturation and the sites in which the type III collagen is found appear to be defects in the bone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00470603
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Defective collagen fibril formation and mineralization in osteogenesis imperfecta with congenital joint contractures (Bruck syndrome) (1993)
    Springer
    European journal of pediatrics 152 (1993), S. 505-508 
    Details
    ISSN: 1432-1076
    Keywords: Osteogenesis imperfecta ; Joint contractures ; Collagen fibrils ; Mineralization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We describe a male patient with osteogenesis imperfecta (OI) who was born with contractures of the knee, elbow and ankle joints. During the first 4 years he suffered from recurrent fractures. He has white sclerae, mild dentinogenesis imperfecta, multiple wormian bones, severe scoliosis and short stature. Morphological analysis of cortical bone revealed typical characteristics of OI including varying width of the osteoid, swollen mitochondria and a dilated endoplasmic reticulum of the osteoblasts. Collagen fibrils of the osteoid had a varying diameter, a feature not found in typical OI patients. Analysis of compact bone showed that the size of apatite crystals and the extractability of collagen with pepsin were markedly elevated compared to controls and other OI type III and IV patients. Lysyl hydroxylation of collagen from the organic bone matrix and the electrophoretic mobility of collagen α1(I)- and α2(I)-chains were normal. Our results provide evidence that this patient belongs to a subtype of OI. The biochemical studies indicate that the underlying defect involves defective fibril-formation of collagen type I leading to an altered mineralization of bone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01955060
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The effect of tissue expansion on the expression of collagen type I and type III mRNA in distinct areas of skin in the dog as an animal model (1998)
    Springer
    European archives of oto-rhino-laryngology and head & neck 255 (1998), S. 473-477 
    Details
    ISSN: 1434-4726
    Keywords: Key words Skin expansion ; Procollagen mRNA ; In ; situ hybridization ; Animal models
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To evaluate the transcriptional response of skin to tissue expansion in the dog, the expression of procollagen α1(I) mRNA and procollagen α1(III) mRNA were analyzed by in situ hybridization. This expression was evaluated in distinct skin areas (subepidermal zone, dermis, capsular zone) after 4–85 days of expansion. Within the first 4 days of expansion expression of procollagen α1(I) and α1(III) mRNA was not affected in the subepidermal and dermal zone. Only a slightly elevated level of type III procollagen mRNA was demonstrated in tissue surrounding the implanted silicone expander. After 7 days of expansion an enhanced level of procollagen α1(III) mRNA was observed in the dermis and capsular zone. A slightly enhanced type I collagen mRNA level occurred in all zones of the dermis that was even stronger in the capsular zone after 9 days of expansion. Concurrently, the number of transcriptionally active cells was significantly higher. Return to the basal level of procollagen α1(I) mRNA was attained after 40 days. At this time a significant expression of procollagenase mRNA was observed. Procollagen III mRNA expression reached its basal level on day 85.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004050050102
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  • 5
    Electronic Resource
    Electronic Resource
    Experimental tissue expansion induces changes in expression of procollagen I and III messenger RNA (1995)
    Springer
    European archives of oto-rhino-laryngology and head & neck 252 (1995), S. 475-477 
    Details
    ISSN: 1434-4726
    Keywords: Tissue expansion ; Skin ; Procollagen mRNA ; Northern blot analysis ; Canine animal model
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Experimental tissue expansion was performed in nine dogs following placement of subcutaneous silicone balloons. The balloon expander was then filled with 300 ml saline immediately after implantation. Duration of expansion varied from 3 days to 124 days. Unaffected skin and skin over an empty expander served as control tissue. Dermal procollagen I and procollagen III gene expression in response to tissue expansion was investigated by dot-blot analysis using digoxigenin-labeled RNA probes complementary to either human procollagen-al (I) mRNA or procollagen-a1 (III) mRNA. Cross-hybridization of human probes with canine procollagen mRNA was demonstrated by Northern blot analysis. In response to the trauma of surgery, procollagen I and III mRNA transcriptions were found to be decreased significantly within the first few days after implantation. After 9 days of expansion, increased levels of procollagen I mRNA were found, while after 16 days increased levels of procollagen III mRNA were evident. The present study is the first to demonstrate changes in dermal collagen gene expression as a reaction to tissue expansion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02114754
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    Paper (German National Licenses)
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