[Elimination of gingival clefts following extractions in orthodontics].
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Biomedical subjects
Publications and source records attributed to M L Couble.
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New minor disulfide-bonded collagens were recently described in cartilaginous tissues. The localization of these molecules in epiphyseal proper and growth plate cartilage of fetal calf has been studied using light and electron immunoperoxidase microscopy. The labeling was restricted to the pericellular region of the chondrocytes with an increasing intensity form the superficial to the inner zone of the epiphysis. At the ultrastructural level, the fine-non striated fibrils of the pericellular matrix were stained, demonstrating their collagenous nature. These minor collagenous chains are thus new components of the chondrocyte "exoskeleton" in which other molecules (proteoglycans, chondronectin, fibronectin and type V collagen) have been previously demonstrated.
The distribution of collagen type III throughout the pulp tissue from human developing tooth was studied using specific antibodies, immuno-fluorescence as well as immuno-peroxidase labelling for electron microscopy. Our results indicate that type III and type I collagen are present in the pulp. The staining intensity seems to correlate with the relatively high proportions of type III collagen biochemically found in pulp. In addition, type III collagen and reticulin fibres are similarly distributed, except that the Von Korff fibres were never detected with anti-type III collagen antibodies. Correspondingly, at the ultrastructural level, type III collagen appears as fine, branched filaments or electron dense material distributed throughout the tissue and particularly in close association with the plasma membrane of pulp fibroblasts. In contrast, type I collagen appears as typical coarse cross banded fibres.
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The distribution of type I, III and IV collagen in the gingival connective matrix was studied by indirect immunofluorescent techniques on biopsies of healthy human attached gingiva. This connective matrix would seem to be made up of an intricate pattern of these 3 collagen types. Type I collagen is the main component of all the layers of the gingival corium while type III collagen is mostly found in the upper layers underlying the gingival epithelium and within the blood vessel walls. Type IV collagen is only associated with basement membranes, particularly of the gingiva, endothelial cells of capillaries, blood vessel walls and nerves.
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The ultrastructural study of the gingival lamina propria of 4 patients from the same family with hereditary gingival hyperplasia showed a density increase of the collagen fibres, a decrease in their mean diameter and the dissociation in sub-units of certain fibres whereas their periodicity was not altered. This study showed also the presence of elastic and oxytalan fibres in greater amounts than in normal gingiva, whereas the number of fibroblasts did not seem to increase. However these fibroblasts seemed to undergo modifications in relation to age and to secrete a large quantity of amyloid substance in the extracellular spaces. The glycoproteins and the glycosaminoglycans more abundant than in normal gingiva were not influenced by the age of the tissue.
The aim of this study was to investigate the ultrastructural and immunohistochemical organization of the main collagenous components of healthy human keratinized mucosa surrounding endosseous implants. Eight patients with completely edentulous mandibles were selected. Four endosseous implants were placed in the mandible of each patient, connected with a bar to support a complete overdenture, and loaded 4 months later. Two years after placement, biopsies of surrounding soft tissue, including the sulcular and junctional epithelium with the underlying and supracrestal connective tissue, were routinely prepared for standard electron microscopy and for ultrastructural immunolabeling of Types I, III, and IV collagen. The connective tissue located under the junctional epithelium comprised Types I and III collagen, whereas the supracrestal connective tissue was composed mainly of Type I collagen. Type IV collagen was located exclusively in the basement membrane of the junctional epithelium.