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  • Immunofluorescence  (3)
  • Bone  (2)
  • Fibroblastenkulturen  (2)
  • 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: 1432-1440
    Keywords: Constitutional connective tissue disorder ; fibroblast cultures ; collagen biosynthesis ; Konstitutionelle Bindegewebserkrankung ; Fibroblastenkulturen ; Kollagenbiosynthese
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Es wird über eine konstitutionelle Bindegewebserkrankung bei dem 10 Jahre alten Sohn blutsverwandter Eltern berichtet. Das klinische und röntgenologische Befundmuster unterscheidet sich von bisher bekannten Syndromen, insbesondere der Osteogenesis imperfecta und dem Marfan-Syndrom, mit denen gewisse Ähnlichkeiten bestehen. In Fibroblastenkulturen aus Hautbiopsien wurde die Kollagenbiosynthese untersucht. Dabei zeigte sich, daß die Fibroblasten unterschiedliche Typen von α1-Ketten synthetisieren, während α2-Ketten weder im Kulturmedium noch in Zellextrakten nachgewiesen werden konnten. Es wird vermutet, daß die Störung der Kollagenbiosynthese mit den klinischen und röntgenologischen Befunden der Erkrankung in Verbindung steht.
    Notes: Summary An apparently “new” connective tissue disorder is described in the 10 year old son of consanguineous parents. The patient showed clinical and radiographic abnormalities reminiscent of both osteogenesis imperfecta and Marfan syndrome. Collagen biosynthesis was analysed in fibroblast cultures from skin biopsies. Fibroblasts of the patient synthesized different types ofα1 chains. No α2 chains could be detected in cell extracts or in culture media suggesting a defect in the synthesis of these compounds. The peculiar pattern of clinical abnormalities may be causally related to the apparent defect in collagen synthesis.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-1440
    Keywords: Knorpel-Knochenumwandlung ; Osteoarthrose ; Chondrocyten ; Kollagensynthese ; Immunfluorescenz ; Cartilage-bone metamorphosis ; Osteoarthrosis ; Chondrocytes ; Collagen-synthesis ; Immunofluorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary Synthesis of collagen by chondrocytes was studied by immunofluorescence using antibodies specific for type I, II and III collagen. The following tissues and culture conditions were chosen for this immunohistological study: normal articular cartilage, epiphyseal growth cartilage, cartilage undergoing osteoarthrotic degeneration, suspension culture and monolayer culture. While type II collagen is the unique collagen all over hyaline cartilage, type I collagen is produced by hypertrophic chondrocytes in the growth plate. In addition, chondrocytes in osteoarthrotic areas of articular cartilage synthesize type I collagen. Under in vitro culture conditions, chondrocytes initially produce type II collagen and synthesize later on type I collagen. The change of synthesis from type II to type I collagen is more rapid in monolayer than in suspension culture. It is concluded that the presence of matrix compounds and the cellmatrix interaction as well are necessary to maintain synthesis of type II collagen in chondrocytes. Alterations in the cell-matrix interactions are shown to occur in the hypertrophic zone of the epiphyseal growth plate, in cartilage undergoing osteoarthrotic degeneration as well as in chondrocytes grown in culture. Thus, change in the control of gene activity may subsequently lead to change in collagen synthesis. It is possible that the synthesis of type I collagen, which cannot fulfil the physiological function of a structural element in cartilageneous tissue, is a crucial factor in the process of osteoarthrosis.
    Notes: Zusammenfassung Unter Verwendung von spezifischen Antikörpern ist es möglich, mit Hilfe immunhistologischer Methoden die Verteilung der verschiedenen Kollagentypen und auch die Kollagensynthese einzelner Zellen zu verfolgen. Diese Methode wurde angewendet, um die Kollagensynthese von Chondrocyten im normalen Gelenkknorpel, Epiphysenknorpel der Wachstumsplatte, osteoarthrotischen Gelenkknorpel, sowie unter in vitro Kulturbedingungen zu verfolgen. Während im normalen Knorpel nur Typ II Kollagen synthetisiert wird, wurde festgestellt, daß die hypertrophierenden großen Chondrocyten an der Basis des Säulenknorpels auf die Synthese des Typ I Kollagens umschalten. Ähnliches gilt auch für die arthrotischen Zellen des Gelenkknorpels. Hier führt die Degeneration zu einer Umschaltung der Kollagensynthese von Typ II auf Typ I Kollagen. Dieses Phänomen kann auch in vitro nachvollzogen werden. In Suspensionskulturen, in denen Chondrocyten in Aggregaten eine knorpelähnliche Matrix aufzubauen vermögen, vollzieht sich der Umschaltungsprozeß langsamer als in Monolayerkulturen. Diese Beobachtungen zeigen, daß Chondrocyten zur Aufrechterhaltung ihrer Typ II Kollagensynthese eine spezielle Zell-Matrix-Wechselwirkung benötigen. Wird durch eine Veränderung der Knorpelmatrix (z.B. bei dem Degenerationsprozeß der Osteoarthrose) diese Wechselbeziehung gestört, kommt es zu einer Neuorientierung der Kollagensynthese und — in deren Folge — zur Umschaltung auf Typ I Kollagen.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 273 (1993), S. 381-389 
    ISSN: 1432-0878
    Keywords: Vigilin ; Cartilage ; Bone ; Differentiation ; In-situ hybridization ; Chicken
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The expression of vigilin was followed during chick embryonal development by in situ hybridization. Vigilin mRNA is abundantly expressed in tissues of mesenchymal and ectomesenchymal origin. The mesenchymal primordial cells of cartilage and bone did not show any significant, expression of vigilin. As tissue differentiation proceeded, vigilin mRNA levels increased in hyaline cartilage and in both endochondral as well as intramembranous bone. The results suggest that the expression of vigilin mRNA in cartilage- and bone-forming cells chondrocytes and osteobalsts, is dependent on the stage of development and cellular differentiation, although not a unique process of bone formation. Most striking is the correlation of the maximum vigilin mRNA expression in osteoblasts and hypertrophic chondrocytes to periods when cell-specific genes were highly transcribed and substantially translated, e.g., synthesis of procollagen and formation of extracellular matrix in bone and cartilage.
    Type of Medium: Electronic Resource
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