The Experts below are selected from a list of 45 Experts worldwide ranked by ideXlab platform

Bruno Gogly - One of the best experts on this subject based on the ideXlab platform.

  • Expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in healthy and diseased human gingiva.
    Journal of periodontology, 2003
    Co-Authors: Anne-laure Ejeil, Sylvie Igondjo-tchen, Sabah Ghomrasseni, Bernard Pellat, Gaston Godeau, Bruno Gogly
    Abstract:

    Background: The purpose of this study was to quantify the amount of matrix metalloproteinases such as MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, and MMP-13 and tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2 expressed by human Gingival explants in culture media and the area fraction (AA%) of Gingival collagen Fibers according to the degree of inflammation, to investigate a possible correlation between these enzymes and collagen loss. Methods: Gingival tissue specimens from 6 healthy controls (group 1), 17 patients with mild Gingival inflammation (group 2), 10 patients with moderate Gingival inflammation (group 3), and 9 patients with severe Gingival inflammation (group 4) were placed in organ culture for 3 days. The MMPs and TIMPs in the culture media were quantified using zymography, dot blotting, and Western blotting. Paraffin Gingival sections were stained with sirius red F3Ba for visualization of collagen Fibers, then the area fraction (AA%) occupied by the Gingival Fibers was determined by automate...

Palle Holmstrup - One of the best experts on this subject based on the ideXlab platform.

  • Expression of VLA‐integrins and their related basement membrane ligands in gingiva from patients of various periodontitis categories
    Journal of clinical periodontology, 1999
    Co-Authors: Nurcan Gürses, Alis Karabulut Thorup, Jesper Reibel, William G. Carter, Palle Holmstrup
    Abstract:

    Abstract. Periodontitis is characterized by destruction of dento-Gingival Fibers and apical migration of the junctional epithelium. Tissue destruction may be associated with altered interactions between epithelium and connective tissue mediated by integrins localized in the basement membrane zone. We examined the expression of α2β1, α3β1, α4/α5β1, α6β4 and their related extracellular matrix (ECM) ligands: laminin-1, laminin-5, and collagen type IV in untreated periodontitis sites of various categories. The expression and location of ECM proteins along the basement membrane were found to be similar between clinically healthy and periodontitis affected tissues. However, ECM proteins were more diffusely distributed in connective tissue (CT) of periodontitis tissues as streak-like/fibrillar/granular stainings, particularly beneath the pocket epithelium (PE) and around the blood vessels. This may reflect an increase in inflammatory cell migration. The more widespread distribution of integrins α2β1, α3β1 in PE of periodontitis specimens may be related to disease activity and increased rate of keratinocyte proliferation and migration. Moreover, the weaker expression of α6β4 in junctional epithelium (JE) of periodontitis affected tissues may be related to the epithelial detachment from the tooth surface. Clarification of expressions of integrins and their ligands in relation to known clinical disease susceptibility factors may provide information on the onset and progression mechanisms of periodontal disease destruction.

Anne-laure Ejeil - One of the best experts on this subject based on the ideXlab platform.

  • Expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in healthy and diseased human gingiva.
    Journal of periodontology, 2003
    Co-Authors: Anne-laure Ejeil, Sylvie Igondjo-tchen, Sabah Ghomrasseni, Bernard Pellat, Gaston Godeau, Bruno Gogly
    Abstract:

    Background: The purpose of this study was to quantify the amount of matrix metalloproteinases such as MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, and MMP-13 and tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2 expressed by human Gingival explants in culture media and the area fraction (AA%) of Gingival collagen Fibers according to the degree of inflammation, to investigate a possible correlation between these enzymes and collagen loss. Methods: Gingival tissue specimens from 6 healthy controls (group 1), 17 patients with mild Gingival inflammation (group 2), 10 patients with moderate Gingival inflammation (group 3), and 9 patients with severe Gingival inflammation (group 4) were placed in organ culture for 3 days. The MMPs and TIMPs in the culture media were quantified using zymography, dot blotting, and Western blotting. Paraffin Gingival sections were stained with sirius red F3Ba for visualization of collagen Fibers, then the area fraction (AA%) occupied by the Gingival Fibers was determined by automate...

Nurcan Gürses - One of the best experts on this subject based on the ideXlab platform.

  • Expression of VLA‐integrins and their related basement membrane ligands in gingiva from patients of various periodontitis categories
    Journal of clinical periodontology, 1999
    Co-Authors: Nurcan Gürses, Alis Karabulut Thorup, Jesper Reibel, William G. Carter, Palle Holmstrup
    Abstract:

    Abstract. Periodontitis is characterized by destruction of dento-Gingival Fibers and apical migration of the junctional epithelium. Tissue destruction may be associated with altered interactions between epithelium and connective tissue mediated by integrins localized in the basement membrane zone. We examined the expression of α2β1, α3β1, α4/α5β1, α6β4 and their related extracellular matrix (ECM) ligands: laminin-1, laminin-5, and collagen type IV in untreated periodontitis sites of various categories. The expression and location of ECM proteins along the basement membrane were found to be similar between clinically healthy and periodontitis affected tissues. However, ECM proteins were more diffusely distributed in connective tissue (CT) of periodontitis tissues as streak-like/fibrillar/granular stainings, particularly beneath the pocket epithelium (PE) and around the blood vessels. This may reflect an increase in inflammatory cell migration. The more widespread distribution of integrins α2β1, α3β1 in PE of periodontitis specimens may be related to disease activity and increased rate of keratinocyte proliferation and migration. Moreover, the weaker expression of α6β4 in junctional epithelium (JE) of periodontitis affected tissues may be related to the epithelial detachment from the tooth surface. Clarification of expressions of integrins and their ligands in relation to known clinical disease susceptibility factors may provide information on the onset and progression mechanisms of periodontal disease destruction.

Shmuel Shoshan - One of the best experts on this subject based on the ideXlab platform.

  • The response of supraalveolar Gingival collagen to orthodontic rotation movement in dogs
    American journal of orthodontics and dentofacial orthopedics : official publication of the American Association of Orthodontists its constituent socie, 1996
    Co-Authors: Meir Redlich, Ezra Rahamim, Anna Gaft, Shmuel Shoshan
    Abstract:

    An orthodontically rotated tooth relapses toward its pretreatment position. Explanations for thisphenomenon have been given after light microscopic studies, according to which it had been assumed that stretched supraalveolar Gingival Fibers pulled back the tooth and brought about relaxation of the stretched Fibers. The rotational relapse, however, can be prevented by supraalveolar fiberotomy of the gingiva around the tooth. This investigation was initiated to reevaluate the validity of the hitherto assumed causes for the relapse, by obtaining ultrastructural data on the response of collagen Fibers after orthodontic intervention. Lateral maxillary incisors in the dog were rotated with bonded fixed appliances. The teeth were divided into groups according to different orthodontic procedures. Scanning and transmission electron microscopic analyses were performed on Gingival samples after proper processing. Analyses of the untreated control samples showed well-organized, parallel, and densely packed thick bundles of collagen Fibers, interconnected with thin Fibers. After rotation-followed-by-retention, the Gingival Fibers were torn, ripped, disorganized, and laterally spaced and of increased diameter. Thus it was concluded that all these patterns are incompatible with stretching. Also, an increased number of elastic Fibers were seen in proximity to the torn collagen Fibers. After Gingival fiberotomy, most Fibers resumed the appearance of the organized pattern of large fiber bundles similar to those seen in the controls