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Postnatal expression of calretinin-immunoreactivity in periodontal Ruffini endings in the rat incisor: a comparison with protein gene product 9.5 (PGP 9.5)-immunoreactivity.
Asahito, T; Ohshima, H; Hanada, K; Wakisaka, S; Maeda, T.
Afiliación
  • Asahito T; Department of Oral Anatomy, Niigata University School of Dentistry, Japan.
Arch Histol Cytol ; 62(1): 57-69, 1999 Mar.
Article en En | MEDLINE | ID: mdl-10223743
The postnatal expression of immunoreactivity for calretinin, one of the calcium binding proteins, and for protein gene product 9.5 (PGP 9.5), a general neuronal marker, was investigated in mechanoreceptive Ruffini endings in the periodontal ligament of the rat incisor. Age-related changes in the expression of these two proteins in periodontal nerves were further quantified with a computerized image analysis. At 1 day after birth, a few PGP 9.5-immunoreactive nerve fibers and a still smaller number of calretinin-positive fibers were found in the periodontal ligament: they were thin and beaded in appearance and no specialized nerve terminals were recognized. Tree-like terminals, reminiscent of immature Ruffini endings, were recognizable in 4-day-old rats by PGP 9.5-immunohistochemistry, while calretinin-immunostaining failed to reveal these specialized endings. At postnatal 7-11 days when PGP 9.5-immunostaining could demonstrate typical Ruffini endings, calretinin-immunopositive nerve fibers merely tapered off without forming the Ruffini type endings. A small number of Ruffini endings showing calretinin-immunoreactivity began to occur in the periodontal ligament at 24-26 days after birth when the occlusion of the first molars had been established. At the functional occlusion stage (60-80 days after birth), the Ruffini endings showing calretinin-immunoreactivity drastically increased in number and density, but less so than those positive for PGP 9.5-immunoreaction. The delayed expression of calretinin suggests that the function of the periodontal Ruffini endings is established after the completion of terminal formation because Ca2+, which binds to calcium binding proteins including calretinin with high affinity, plays an important role in mechano-electric transduction.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ligamento Periodontal / Tioléster Hidrolasas / Proteína G de Unión al Calcio S100 / Incisivo / Mecanorreceptores Límite: Animals Idioma: En Revista: Arch Histol Cytol Asunto de la revista: HISTOLOGIA Año: 1999 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Japón
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ligamento Periodontal / Tioléster Hidrolasas / Proteína G de Unión al Calcio S100 / Incisivo / Mecanorreceptores Límite: Animals Idioma: En Revista: Arch Histol Cytol Asunto de la revista: HISTOLOGIA Año: 1999 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Japón