Localization of the endogenous cysteine proteinase inhibitor, cystatin C, and the cysteine proteinase, cathepsin B, to the junctional epithelium in rat gingiva

Takayoshi Yamaza, Satoya Mino, Ikiru Atsuta, Atsushi Danjo, Tadayoshi Kagiya, Katsushi Nishijima, Jin Qi Zang, Mizuho A. Kido, Teruo Tanaka

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The junctional epithelium (JE) is a primary site of defense against periodontal pathogens. Cystatin C is an endogenous inhibitor of cysteine proteinases such as cathepsin B and also has antibacterial actions against periodontal pathogens. However, the distribution and role of cystatin C in JE have not been clarified. To investigate the function of cystatin C in the host defense at dentogingival junction, we examined the immunolocalization of cystatin C and cathepsin B in rat gingiva using light and electron microscopy. The JE (particularly the coronal portion) was immunopositive for cystatin C, and immunoelectron microscopy revealed that cystatin C was localized to the vesicular, granular, and vacuolar compartments of JE cells. The pattern of cathepsin B immunoreactivity in JE cells resembled that of cystatin C. Both cystatin C and cathepsin B appeared to be localized to endosomal/lysosomal compartments within JE cells. These findings suggest that cystatin C regulates cysteine proteinase activity and exerts antibacterial effects both in the lysosomal compartments of JE cells and in the intercellular spaces of the JE. Cystatin C is thus able to participate in host defense against periodontal pathogens at the dentogingival junction.

Original languageEnglish
Pages (from-to)121-129
Number of pages9
JournalActa Histochemica et Cytochemica
Issue number2
Publication statusPublished - May 18 2005


All Science Journal Classification (ASJC) codes

  • Pathology and Forensic Medicine
  • Biochemistry
  • Physiology
  • Histology
  • Cell Biology

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