title: Distribution pattern of versican, link protein and hyaluronic acid in the rat periodontal ligament during experimental tooth movement.
abstract: The ability of the periodontal ligament (PDL) to rapidly remodel is the basis of orthodontic tooth movement. During the tooth movement, matrix proteoglycans (PGs) may play important roles in spatial, mechanical and biological aspects for the maintenance and repair of the PDL. The aim of this study was to characterize the distribution of a large hyaluronic acid (HA)-binding proteoglycan, versican, link protein (LP) and HA in the rat molar PDL during experimental tooth movement by histochemical and immunohistochemical methods. Experimental tooth movement was performed according to Waldo's method. Histologically, regressive changes, such as decrease of fibroblasts and collagen fibers and exudative change of edema were observed in the compressive side and progressive changes, such as proliferation of fibroblasts and collagen fibers, in the strain side one day after treatment. By 3 days after tooth movement, regressive or progressive changes were not observed in either side. Using monoclonal antibodies specific to versican core protein or LP, the positive immunoreactivity for both molecules was constantly observed throughout the PDL. After the experimental force was applied to the tooth, however, the immunostainings of versican and LP became significantly intense only in the compressive side but decreased in the strain side. The intensity in the compressive side was strongest one day after the force was applied and gradually diminished thereafter. HA of both sides did not change during experimental tooth movement. Since HA is present in the PDL, large amounts of versican and LP expressed in the compressive side may create large hydrated aggregates via their association with HA that dissipates the compressive force applied to this tissue.
authors.affiliation: Department of Orthodontics, Nihon University School of Dentistry at Matsudo, Japan.
authors.forename: R
authors.initials: R
authors.lastname: Sato
authors.forename: H
authors.initials: H
authors.lastname: Yamamoto
authors.forename: K
authors.initials: K
authors.lastname: Kasai
authors.forename: M
authors.initials: M
authors.lastname: Yamauchi
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D002455:Cell Division; D011508:Chondroitin Sulfate Proteoglycans / Q000032:analysis*; D003094:Collagen; D004396:Coloring Agents; D004487:Edema / Q000473:pathology; D016326:Extracellular Matrix Proteins / Q000032:analysis*; D005122:Exudates and Transudates; D005347:Fibroblasts / Q000473:pathology; D005456:Fluorescent Dyes; D006023:Glycoproteins / Q000032:analysis*; D006651:Histocytochemistry; D006820:Hyaluronic Acid / Q000032:analysis*; D007150:Immunohistochemistry; D037181:Lectins, C-Type; D008024:Ligands; D008297:Male; D010513:Periodontal Ligament / Q000473:pathology*; D011506:Proteins / Q000032:analysis*; D011509:Proteoglycans / Q000032:analysis*; D051381:Rats; D017208:Rats, Wistar; D013314:Stress, Mechanical; D014087:Tooth Movement Techniques; D053675:Versicans; D000099249:Proteoglycan Link Protein
chemical_list: D000911:Antibodies, Monoclonal; D011508:Chondroitin Sulfate Proteoglycans; D003094:Collagen; D004396:Coloring Agents; D016326:Extracellular Matrix Proteins; D005456:Fluorescent Dyes; D006023:Glycoproteins; D006820:Hyaluronic Acid; D037181:Lectins, C-Type; D008024:Ligands; D011506:Proteins; D011509:Proteoglycans; D053675:Versicans; D000099249:Proteoglycan Link Protein; C508324:Vcan protein, rat