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  • Immunofluorescence histochemistry collagen crosslinking  (1)
  • Tibial dyschondroplasia lesion  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Chicken tibial dyschondroplasia: A limb mutant with two growth plates and possible defects of collagen crosslinking (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 196 (1993), S. 54-61 
    Details
    ISSN: 1058-8388
    Keywords: Type II collagen ; Type X collagen ; Tibial dyschondroplasia lesion ; Crosslink formation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In the cartilaginous epiphyseal growth plate, extracellular matrix molecules such as collagens are believed to play important roles during both normal and abnormal development. One defect of the epiphyseal plate occurs in chickens with a condition termed tibial dyschondroplasia (TD). This abnormality occurs in certain strains of juvenile chickens and other rapidly developing animals. It is characterized by the presence of a mass of avascular, uncalcified cartilage which is retained in the proximal metaphysis of the tibiotarsus. To elucidate the developmental events which may be involved in this lesion, we have performed both immunohistochemistry and in situ hybridizations for collagen types II and X, known components of the extracellular matrix of the growth plate. By immunohistochemical analyses, the TD lesion contains both of these collagen types; therefore, the presence of these molecules per se is not sufficient for calcification of vascularization to occur. Since type X collagen is expressed exclusively in hypertrophic cartilage, the chondrocytes in the lesion must have undergone hypertrophy before their developmental arrest. The matrix of the lesion also reacted with a monoclonal antibody which is directed against an epitope in the NH2-terminal telopeptide of the α1(II) chain. Our previous data suggest that this epitope is rendered unavailable in type II collagen which has undergone crosslink formation; its availability in the lesion suggests that crosslinking may be abnormal. Lastly, analyses by in situ hybridization failed to detect mRNA for either type II or type X collagen within the lesion, but chondrocytes distal to the lesion do contain mRNAs for these collagens in a spatial pattern suggesting the presence of a second growth plate. © 1993 wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1001960107
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Type II collagen during cartilage and corneal development: Immunohistochemical analysis with an anti-telopeptide antibody (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 196 (1993), S. 47-53 
    Details
    ISSN: 1058-8388
    Keywords: II-5B2 epitope ; Type II collagen molecule ; Immunofluorescence histochemistry collagen crosslinking ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: We have examined the pattern of immunoreactivity of a monoclonal antibody, II-5B2, with specificity for an epitope which resides within the NH2-terminal extension peptide (telopeptide) of the avian type II collagen molecule. This epitope is available in regions of matrix where de novo synthesis of the molecule is ongoing, but not where synthesis has ceased and maturation and crosslink formation have occurred. Within the cartilaginous growth plate, the epitope disappears from the matrix soon after the chondrocytes become hypertrophic; within the cornea, the epitope disappears subjacent to the epithelium. The II-5B2 epitope is not made available by a variety of procedures shown to remove potentially masking substances and to disrupt fibrillar organization. It is rendered available, however, when covalent crosslink formation between collagen molecules is blocked through administration of β-aminopropionitrile or penicillamine. In contrast, the epitope of another monoclonal antibody against type II collagen, II-II6B3, which resides in the triple-helical domain of the molecule, in cartilage is present throughout the growth plate including the hypertrophic zone, and in cornea extends for a considerable distance into the stroma. Thus, it is available for antibody binding regardless of fibril maturation and crosslinking. These data suggest that the II-5B2 epitope becomes unavailable when the telopeptide becomes cross-linked. By using these two monoclonal antibodies in serial sections, one can establish the crosslinking pattern of type II collagen in the tissue. This set of antibodies is a potentially useful tool for analyzing normal and abnormal development, remodeling, and repair processes in the skeletal system and in other tissues where type II collagen is involved in organization of the matrix, such as the primary corneal stroma. © 1993 wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1001960106
    Location Call Number Limitation Availability
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    Paper (German National Licenses)
    Fulltext
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