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The primary calcification in bones follows removal of decorin and fusion of collagen fibrils.
Hoshi, K; Kemmotsu, S; Takeuchi, Y; Amizuka, N; Ozawa, H.
Afiliación
  • Hoshi K; First Department of Oral Anatomy, Niigata University School of Dentistry, Niigata, Japan.
J Bone Miner Res ; 14(2): 273-80, 1999 Feb.
Article en En | MEDLINE | ID: mdl-9933482
To elucidate the mechanisms of primary calcification in bone, ultrastructural changes in collagen fibrils, as well as cytochemical alteration of proteoglycan, especially decorin, were investigated morphologically in 19-day postcoitum embryonic rat calvariae. Below the osteoblast layer, calcification of the osteoid area increased in direct proportion to its distance from the osteoblasts. In the uncalcified osteoid area, collagen fibrils near matrix vesicles possessed sharp contours and were a uniform 50 nm in diameter. Immunoelectron microscopy revealed decorin to be abundantly localized in the vicinity of the collagen fibrils. In the osteoid area undergoing the process of calcification, collagen fibrils tended to fuse side by side. Where calcification was progressed, this fusion was even more so. Some very large fibrils exhibited complicated contours, 400 nm or more in diameter. Although the calcification at this stage affected areas both inside and outside of the collagen fibrils, the interior areas manifested a lower density of calcification. The immunolocalization of decorin was also much decreased around these fibrils. Thus, primary calcification in bone matrix follows the removal of decorin and fusion of collagen fibrils. This phenomenon may aid in the process of calcification and bone formation, because (1) inhibitors of calcification, such as decorin, are removed, (2) the fusion of collagen fibrils provides the room necessary for rapid growth of mineral crystals, and (3) the soft elastic bone matrix containing abundant fused collagen fibrils less subjective to calcification is safe for both maternal and embryonic bodies and is convenient for subsequent bone remodeling.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteoglicanos / Huesos / Calcificación Fisiológica / Colágeno Límite: Animals / Pregnancy Idioma: En Revista: J Bone Miner Res Asunto de la revista: METABOLISMO / ORTOPEDIA Año: 1999 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteoglicanos / Huesos / Calcificación Fisiológica / Colágeno Límite: Animals / Pregnancy Idioma: En Revista: J Bone Miner Res Asunto de la revista: METABOLISMO / ORTOPEDIA Año: 1999 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos