title: Dilated capillaries, disorganized collagen fibers and differential gene expression in periodontal ligaments of hypomorphic fibrillin-1 mice.
abstract: The periodontal ligaments (PDLs) are soft connective tissue between the cementum covering the tooth root surface and alveolar bone. PDLs are composed of collagen and elastic system fibers, blood vessels, nerves, and various types of cells. Elastic system fibers are generally formed by elastin and microfibrils, but PDLs are mainly composed of the latter. Compared with the well-known function of collagen fibers to support teeth, little is known about the role of elastic system fibers in PDLs. To clarify their role, we examined PDLs of mice under-expressing fibrillin-1 (mgR mice), which is one of the major microfibrillar proteins. The PDLs of homozygous mgR mice showed one-quarter of the elastic system fibers of wild-type (WT) mice. A close association between the elastic system fibers and the capillaries was noted in WT, homozygous and heterozygous mgR mice. Interestingly, capillaries in PDLs of homozygous mice were dilated or enlarged compared with those of WT mice. A comparable level of type I collagen, which is the major collagen in PDLs, was expressed in PDL-cells of mice with three genotypes. However, multi-oriented collagen fiber bundles with a thinner appearance were noted in homozygous mice, whereas well-organized collagen fiber bundles were seen in WT mice. Moreover, there was a marked decrease in periostin expression, which is known to regulate the fibrillogenesis and crosslinking of collagen. These observations suggest that the microfibrillar protein, fibrillin-1, is indispensable for normal tissue architecture and gene expression of PDLs.
authors: Maxillofacial Orthognathics, Department of Maxillofacial Reconstruction and Function, Division of Maxillofacial/Neck Reconstruction, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan.
authors: Ganjargal
authors: G
authors: Ganburged
authors: Naoto
authors: N
authors: Suda
authors: Masahiro
authors: M
authors: Saito
authors: Yosuke
authors: Y
authors: Yamazaki
authors: Keitaro
authors: K
authors: Isokawa
authors: Keiji
authors: K
authors: Moriyama
mesh_terms: D000818:Animals; D002196:Capillaries / Q000473:pathology*; D003094:Collagen / Q000378:metabolism; D003095:Collagen Diseases / Q000150:complications* / Q000235:genetics / Q000378:metabolism; D004108:Dilatation, Pathologic / Q000150:complications* / Q000235:genetics / Q000378:metabolism; D004547:Elastic Tissue / Q000378:metabolism / Q000473:pathology* / Q000648:ultrastructure; D000071838:Fibrillin-1; D000071837:Fibrillins; D005786:Gene Expression Regulation; D006579:Heterozygote; D006720:Homozygote; D017403:In Situ Hybridization; D008297:Male; D051379:Mice; D008822:Mice, Transgenic; D020894:Microfibrils / Q000378:metabolism / Q000473:pathology / Q000648:ultrastructure; D008840:Microfilament Proteins / Q000235:genetics* / Q000378:metabolism; D010513:Periodontal Ligament / Q000378:metabolism* / Q000473:pathology / Q000648:ultrastructure; D019408:Platelet Endothelial Cell Adhesion Molecule-1 / Q000378:metabolism; D054392:Adipokines
chemical_list: D003094:Collagen; D000071838:Fibrillin-1; D000071837:Fibrillins; D008840:Microfilament Proteins; D019408:Platelet Endothelial Cell Adhesion Molecule-1; C000605724:Fbn1 protein, mouse; D054392:Adipokines