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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 59 (1981), S. 91-93 
    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
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    European journal of pediatrics 125 (1977), S. 29-37 
    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
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    European journal of pediatrics 124 (1977), S. 101-111 
    ISSN: 1432-1076
    Keywords: Hutchinson-Gilford-syndrome ; Familial incidence ; Autosomal-recessive disorder ; Fibroblast cultures ; Collagen types ; Thymidine incorporation ; Immunofluorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract This report relates the case histories of two sisters who demonstrated the typical symptoms of progeria at birth. One of these children had died previous to this study. The familial occurrence underlines the thesis that progeria is an autosomal-recessive disorder. The examination of the cultured skin fibroblasts from the younger child showed a clear decrease in cell growth. On the other hand, the immunfluorescent examination of skin biopsies and cultured skin fibroblasts revealed no atypical distribution of collagen types.
    Type of Medium: Electronic Resource
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  • 4
    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
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