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  • 1
    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.
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  • 2
    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.
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  • 3
    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.
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  • 4
    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.
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  • 5
    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.
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  • 6
    ISSN: 1433-2965
    Keywords: Key words:Bedrest unloading – Biochemical markers – Bone metabolism – Whole-body composition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract: Eight male volunteers were submitted to a 6-week anti-orthostatic bedrest trial followed by a 1-month reambulation period. We prospectively monitored whole-body composition by dual-energy X-ray absorptiometry, bone and connective tissue metabolism by biochemical markers and calcium regulating hormones by 1–84 parathyroid hormone and 1,25-dihydroxyvitamin D3. Bone mineral density (BMD) did not vary significantly; however, a trend toward an increase in head BMD and a decrease in trunk, lumbar vertebrae and lower limb BMD was observed. A decrease in the lower limb lean content occurred by day 27 and was maximum by day 42 after the beginning of bedrest; it normalized by day 30 after bedrest. The serum levels of both osteocalcin and C-terminal crosslinked telopeptide of type I collagen increased as a consequence of bedrest. A slight increase in the serum levels of the N-terminal propeptide of type III collagen, a marker of connective tissue metabolism, was observed during the bedrest period. Except for the C-terminal extension propeptide of type I collagen, all markers decreased to baseline pre-immobilization levels during the 1-month recovery phase. Serum PTH and 1,25-dihydroxyvitamin D3 levels were low during the bedrest period and rose during the reambulation phase. These results seem to reflect early changes in bone and connective tissue metabolism as a result of bedrest unloading, but their order of magnitude remains moderate, thus emphasizing the necessity to perform longer-duration trials.
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  • 7
    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.
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  • 8
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Biopsies were taken from the upper and inner arm of 10 60-year-old male cigarette smokers and compared with 10 age-matched controls who were non-smokers. The mean relative area, number and thickness of the elastic fibres were significantly increased in the cigarette smokers compared to the controls. These results were confirmed using antibodies to elastin or the microfibrillar component of elastic tissue. In the smokers the broader and more fragmented elastic fibres in the skin were not as intensely stained as those of the non-smokers and the ultrastructural alterations of the elastic fibres were similar to those in solar elastosis.
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  • 9
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Human palatal epithelial cells were grown on lethally irradiated 3T3 fibroblasts. Under these conditions, epithelial cultures become stratified. The basal cells have a cuboïdal shape and suprabasal layers are flattened. The reconstituted epithelium exhibits markers of differentiation: intracytoplasmic bundles of keratin-like filaments and abundant desmosmes present in every layer. Type IV collagen fibronectin and laminin are synthesized by these cultures. Basal cells grip the culture substratum via an extracellular matrix made up of type IV collagen, laminin and fibronectin.
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  • 10
    ISSN: 1600-0501
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The purpose of this study was to analyse the distribution of interstitial collagenous and noncollagenous glycoproteins of keratinized mucosa surrounding successful endosseous implants. Biopsies were incubated with highly purified antibodies against types I. III. IV collagen. laminin and fibronectin and routinely observed by immunofluorescence staining. Whereas no significative difference in the distribution of collagenous components was observed in comparison with healthy human gingiva, the collagen fibers of the connective tissue attachment ran parallel to the long axis of the implant. In 50% of the biopsies the gingival connective tissue underlying the junctional epithelium was rich in inflammatory cells and poor in collagenous components. However, the increased staining of type III collagen and the intense presence of fibronectin in this area reflect the very important remodeling ability of the local keratinized mucosa.
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