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  • 1
    Electronic Resource
    Electronic Resource
    Immunofluorescent localization of collagen types I, III and IV, fibronectin, laminin, and basement membrane proteoglycan in developing mouse skin (1987)
    Springer
    Development genes and evolution 196 (1987), S. 295-302 
    Details
    ISSN: 1432-041X
    Keywords: Extracellular matrix ; Dermal-epidermal interactions ; Skin ; Hair morphogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The distribution of various extracellular matrix components was studied in frozen sections of embryonic (14–18 days) and early postnatal (birth and 4 days post parturn) dorsal mouse skin using monospecific antibodies and indirect immunofluorescence. Basement membrane zone components — type IV collagen, laminin and heparan sulphate proteoglycan — were found to be uniformly and unchangingly distributed along the dermal-epidermal junction. In contrast, the distribution of interstitial matrix components — types I and III collagen, and fibronectin — was heterogeneous and varied with the stages of hair development. Collagens became sparse and were eventually completely removed from the prospective dermal papilla and from a one-cell-thick sheath of dermal cells around hair buds. They remained absent from the dermal papilla throughout hair organogenesis. Fibronectin was always present around dermal papilla cells and was particularly abundant along the dermal-epidermal junction of hair rudiments, as well as underneath hair buds. In contrast, in interfollicular skin, collagens accumulated in increasing density, while fibronectin became progressively sparser. It thus appears that interstitial collagens and fibronectin are distributed in a manner which is related to hair morphogenesis. In morphogenetically active regions, collagen density is low, while that of fibronectin is high. Conversely, in histologically stabilized zones, collagen is abundant and fibronectin is sparse. This microheterogeneous distribution of interstitial collagens and of fibronectin might thus constitute part of the morphogenetic message that the dermis is known to transmit to the epidermis during the development of skin and of cutaneous appendages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00395953
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  • 2
    Electronic Resource
    Electronic Resource
    Distribution and organization of the elastic system fibres in healthy human gingiva (1988)
    Springer
    Histochemistry and cell biology 89 (1988), S. 47-52 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The ultrastructural distribution and organization of the elastic system fibres, i.e. oxytalan, elaunin and elastic fibres, were studied by transmission electron microscopy and by an immunohistochemical method for the detection of elastin in healthy human gingiva. The morphological distribution of these fibres was characterized by the presence of oxytalan, elaunin and elastic fibres, respectively, in the upper, medium, and deep layers of gingival connective tissue. Anti-elastin antibody reacted with microfibrils and amorphous material of the elastic system fibres throughout the gingival connective tissue. These findings were interpreted as indicating that the microfibrils were associated with small amounts of elastin at their surface.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00496583
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  • 3
    Electronic Resource
    Electronic Resource
    Immunohistochemical study of the biological fate of a subcutaneous bovine collagen implant in rat (1989)
    Springer
    Histochemistry and cell biology 91 (1989), S. 177-184 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The biological fate of a bovine collagen implant (Zyderm Collagen Implant ZCI), injected subcutaneously into rats, was studied by the immunoperoxidase technique using specific antibodies against the bovine implant and against types I, III, IV, V collagens, fibronectin and elastin. The implant remained in the animals until the end of the experiment (90 days), with no visible modification, as demonstrated by immunoperoxidase labelling and scanning electron microscopy. A slight inflammatory reaction was visible around the implant 24 h after injection and within the implant 3 days after injection. Fibroblast invasion began 7 days after injection. The chronology of the deposition in the implant of the host (rat) extracellular matrix components was as follows: by 24 h after injection, fibronectin was observed throughout the implant; types I and V collagens appeared on the 7th day, and, in contrast to surrounding connective tissue, type V collage labelling was obtained without acid pretreatment of the section. Types III and IV collagens were detected inside the implant only 30 days after injection. At the end of the experiment (90 days), there was abundant types I and V collagens after fibroblast migration, and abundant type IV collagen demonstrating an important vascularization. No elastic fibres could be detected inside the implant but they appeared as a dense network around the implant in host connective tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00490129
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  • 4
    Electronic Resource
    Electronic Resource
    Ultrastructural organization of type XI collagen in fetal bovine epiphyseal cartilage (1993)
    Springer
    Histochemistry and cell biology 100 (1993), S. 231-239 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Type XI collagen was localized with polyclonal antibodies specific for α1(XI) and α2(XI) chains in the resting zone of epiphyseal cartilage from calf fetuses. The immunofluorescence technique was used on sections of cartilage, and the immunogold labelling technique for electron microscopy on fibrils isolated from cartilage and, for the fist time, in situ on blocks of cartilage fractured in liquid nitrogen. Immunofluorescence showed that without pepsin treatment the staining of type XI collagen was restricted to the pericellular zones; after pepsin treatment, the staining was co-distributed with that of type II collagen. Immunoelectron microscopy performed on isolated fibrils and on cartilage blocks showed that after disruption of fibrils with pepsin, type XI collagen was labelled on small filaments on the fibrils. When the fibrils were not disrupted, labelling was observed in situ only at the ends of the fibrils or on cross-sections of some fibrils. These results indicate that type XI collagen is located inside type II collagen fibrils in fetal bovine epiphyseal cartilage, as already postulated for embryonic chicken sterna.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269096
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  • 5
    Electronic Resource
    Electronic Resource
    Localization and synthesis of type III collagen and fibronectin in human reparative dentine (1988)
    Springer
    Histochemistry and cell biology 88 (1988), S. 141-149 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The injury of dental pulp tissue, following caries, is accompanied by the deposit of a typical hard scar tissue known as reparative dentine which should be regarded as the mineralization of a new organic matrix. Highly purified antibodies were used in combination with immunoperoxidase or immunogold technique at the ultrastructural level to reveal the distribution and synthesis of types I and III collagen and fibronectin elaborated by typical matrix-forming cells in the new tissue. Specific immunoperoxidase labelling, on demineralized teeth, clearly demonstrated that type I collagen represents the main type of collagen (88%). It is associated with bundles of fine striated fibrils of type III collagen and in close vicinity with fibronectin and constituted, at least, the new organic matrix of reparative dentine. Immunogold staining gave precise localization mainly over Golgi apparatus for the 3 components, thus suggesting that the cells concerned should not be considered as new odontoblasts but rather as pulpal cells in the process of differentiation participating in the formation of new dentine. Moreover, these events are very similar to those observed during wound healing in other tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00493296
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  • 6
    Electronic Resource
    Electronic Resource
    Distribution and synthesis of type I and type III collagens in developing mouse molar tooth root (1988)
    Springer
    Histochemistry and cell biology 88 (1988), S. 131-140 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution and synthesis of type I and type III collagens in the mouse molar tooth root have been investigated by correlating light and electron immunohistochemical data. Purified rabbit antibodies were raised against mouse type I and type III collagens and indirect immunoperoxidase procedures were used. In these conditions, predentin, pre-bone, and pre-acellular cementum were intensely immunostained for type I collagen. Both optic and ultrastructural data confirmed the presence of type I collagen at the epithelio-mesenchymal junction, but Hertwig's basement membranes remained unlabelled. The odontoblasts including the short polarized ones, osteoblasts, some cells of pulp mesenchyme and the perifollicular cells possessed type I collagen immunoreactivity in the rough endoplasmic reticulum (RER), Golgi complex and the secretory vesicles. Type III collagen immunoreactivity was strong in the perifollicular mesenchyme, light in the pulp mesenchyme and absent from the epithelio-mesenchymal junction, the predentin, pre-bone and pre-acellular cementum. Intracellular immunolabelling was detected at the ultrastructural level in the perifollicular cells by a faint homogeneous peroxidase deposit in the RER cisternae. Finally, these results, compared with previous biochemical and morphological data, represent the first dynamic aspect of collagens distribution and synthesis in the mouse molar root development. In terms of cell differentiation, our data also suggest that type III collagen synthesis does not occur during the odontoblast process of differentiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00493295
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  • 7
    Electronic Resource
    Electronic Resource
    Type-I collagen production by human odontoblast-like cells in expiants cultured on cyanoacrylate films (1986)
    Springer
    Cell & tissue research 244 (1986), S. 133-140 
    Details
    ISSN: 1432-0878
    Keywords: Collagen ; Odontoblast ; Cyanoacrylate ; Fibronectin ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Odontoblast-like cells derived from human tooth pulps were maintained in expiant culture and grown either on glass coverslips only (used as control) or on glass coverslips coated with cyanoacrylate films. Ultrastructural and cyto-morphometric evidence showed that cells exposed to cyanoacrylate, in contrast to controls, display a significant decrease of rough endoplasmic reticulum and mitochondria. In addition, immunofluorescent staining and radioimmunoassays for type-I collagen suggested disturbances in production for the exposed cells. The use of anti-fibronectin antibodies with electron-microscopic immunoperoxidase-labelling demonstrated that the adherence of cells to cyanoacrylate can involve both adhesion plaques and fibronectin. These results therefore suggest that there were no apparent differences in the adhesion interaction of cells between glass and cyanoacrylate substrates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218390
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  • 8
    Electronic Resource
    Electronic Resource
    Tissue reaction to subcutaneous implantation of a collagen sponge. A histological, ultrastructural, and immunological study (1990)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 24 (1990), S. 689-703 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The biocompatibility of a subcutaneously implanted bovine collagen sponge (Haemostagen) was studied in rats by analyzing tissue reactions up to 3 months by histological and ultrastructural methods; in addition, the level of serum antibodies to bovine type I collagen (the major implant collagen) was measured by solid-phase radio-immunoassay. By 8 h after implantation, the implant was completely filled with polymorphonuclear cells (PMNs). After 8 days, fibroblasts had developed a granulation tissue within the sponge and the PMNs had almost disappeared. The small residue that remained after 1 month consisted of some densely packed collagen fibrils containing giant cells, which had disappeared by 3 months. No antibodies to bovine type I collagen were found in the sera of implanted rats.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820240605
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  • 9
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    Immunofluorescent localization of collagen types I, III and IV, fibronectin, laminin, and basement membrane proteoglycan in developing mouse skin (1987)
    Springer
    Details
    Publication Date: 1987-07-01
    Print ISSN: 0949-944X
    Electronic ISSN: 1432-041X
    Topics: Biology
    Published by Springer
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  • 10
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    Localization and synthesis of type III collagen and fibronectin in human reparative dentine (1988)
    Springer
    Details
    Publication Date: 1988-03-01
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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