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Distinct characteristics of mandibular bone collagen relative to long bone collagen: relevance to clinical dentistry.
Matsuura, Takashi; Tokutomi, Kentaro; Sasaki, Michiko; Katafuchi, Michitsuna; Mizumachi, Emiri; Sato, Hironobu.
  • Matsuura T; Section of Fixed Prosthodontics, Department of Oral Rehabilitation, Fukuoka Dental College, 15-1 Tamura 2-Chome, Sawara-ku, Fukuoka 814-0193, Japan.
  • Tokutomi K; Section of Fixed Prosthodontics, Department of Oral Rehabilitation, Fukuoka Dental College, 15-1 Tamura 2-Chome, Sawara-ku, Fukuoka 814-0193, Japan.
  • Sasaki M; Section of Fixed Prosthodontics, Department of Oral Rehabilitation, Fukuoka Dental College, 15-1 Tamura 2-Chome, Sawara-ku, Fukuoka 814-0193, Japan.
  • Katafuchi M; Section of Fixed Prosthodontics, Department of Oral Rehabilitation, Fukuoka Dental College, 15-1 Tamura 2-Chome, Sawara-ku, Fukuoka 814-0193, Japan.
  • Mizumachi E; Section of Fixed Prosthodontics, Department of Oral Rehabilitation, Fukuoka Dental College, 15-1 Tamura 2-Chome, Sawara-ku, Fukuoka 814-0193, Japan.
  • Sato H; Section of Fixed Prosthodontics, Department of Oral Rehabilitation, Fukuoka Dental College, 15-1 Tamura 2-Chome, Sawara-ku, Fukuoka 814-0193, Japan.
Biomed Res Int ; 2014: 769414, 2014.
Article en En | MEDLINE | ID: mdl-24818151
ABSTRACT
Bone undergoes constant remodeling throughout life. The cellular and biochemical mechanisms of bone remodeling vary in a region-specific manner. There are a number of notable differences between the mandible and long bones, including developmental origin, osteogenic potential of mesenchymal stem cells, and the rate of bone turnover. Collagen, the most abundant matrix protein in bone, is responsible for determining the relative strength of particular bones. Posttranslational modifications of collagen, such as intermolecular crosslinking and lysine hydroxylation, are the most essential determinants of bone strength, although the amount of collagen is also important. In comparison to long bones, the mandible has greater collagen content, a lower amount of mature crosslinks, and a lower extent of lysine hydroxylation. The great abundance of immature crosslinks in mandibular collagen suggests that there is a lower rate of cross-link maturation. This means that mandibular collagen is relatively immature and thus more readily undergoes degradation and turnover. The greater rate of remodeling in mandibular collagen likely renders more flexibility to the bone and leaves it more suited to constant exercise. As reviewed here, it is important in clinical dentistry to understand the distinctive features of the bones of the jaw.
Asunto(s)

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Huesos / Colágeno / Odontología / Mandíbula Límite: Humans Idioma: En Año: 2014 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Huesos / Colágeno / Odontología / Mandíbula Límite: Humans Idioma: En Año: 2014 Tipo del documento: Article