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The Ca(2+)-binding protein calretinin is selectively enriched in a subpopulation of the epithelial rests of Malassez.
Korkmaz, Yüksel; Klinz, Franz-Josef; Beikler, Thomas; Blauhut, Thorsten; Schneider, Kurt; Addicks, Klaus; Bloch, Wilhelm; Raab, Wolfgang H-M.
Afiliação
  • Korkmaz Y; Department of Operative Dentistry, Periodontics and Endodontics, Heinrich Heine University, Moorenstrasse 5, 40225 Düsseldorf, Germany. yueksel.korkmaz@uni-duesseldorf.de
Cell Tissue Res ; 342(3): 391-400, 2010 Dec.
Article em En | MEDLINE | ID: mdl-21080000
ABSTRACT
During tooth development, the inner and outer enamel epithelia fuse by mitotic activity to produce a bilayered epithelial sheath termed Hertwig's epithelial root sheath (HERS). The epithelial rests of Malassez (ERM) are the developmental residues of HERS and remain in the adult periodontal ligament (PDL). Although the cellular regulation of the Ca(2+)-binding proteins parvalbumin, calbindin-D28k, and calretinin has been reported in the inner and outer enamel epithelia during tooth development, an involvement of Ca(2+)-binding proteins in the ERM has not so far been characterized. Among the three Ca(2+)-binding proteins tested (calbindin D28k, parvalbumin, calretinin), we have only been able to detect calretinin in a subpopulation of adult rat molar ERM, by using quantitative immunohistochemical and confocal immunofluorescence techniques. TrkA (a marker for ERM) is present in numerous epithelial cell clusters, whereas calretinin has been localized in the cytosol and perinuclear region of a subpopulation of TrkA-positive cells. We conclude that, in inner and outer enamel epithelial cells, Ca(2+) is regulated by calbindin, parvalbumin, and calretinin during tooth development, whereas in the ERM of adult PDL, Ca(2+) is regulated only by calretinin. The expression of Ca(2+)-binding proteins is restricted in a developmental manner in the ERM.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ligamento Periodontal / Proteína G de Ligação ao Cálcio S100 / Odontogênese Limite: Animals Idioma: En Ano de publicação: 2010 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ligamento Periodontal / Proteína G de Ligação ao Cálcio S100 / Odontogênese Limite: Animals Idioma: En Ano de publicação: 2010 Tipo de documento: Article