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

Research output: Contribution to journalArticle

Abstract

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
Volume38
Issue number2
DOIs
Publication statusPublished - May 18 2005

Fingerprint

yeast proteinase B
Epithelial Attachment
Cysteine Proteinase Inhibitors
Cystatin C
Cathepsin B
Cysteine Proteases
Gingiva
Rats
Cystatin B
Pathogens

All Science Journal Classification (ASJC) codes

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

Cite this

Localization of the endogenous cysteine proteinase inhibitor, cystatin C, and the cysteine proteinase, cathepsin B, to the junctional epithelium in rat gingiva. / Yamaza, Takayoshi; Mino, Satoya; Ikiru, Atsuta; Danjo, Atsushi; Kagiya, Tadayoshi; Nishijima, Katsushi; Zang, Jin Qi; Kido, Mizuho A.; Tanaka, Teruo.

In: Acta Histochemica et Cytochemica, Vol. 38, No. 2, 18.05.2005, p. 121-129.

Research output: Contribution to journalArticle

Yamaza, Takayoshi ; Mino, Satoya ; Ikiru, Atsuta ; Danjo, Atsushi ; Kagiya, Tadayoshi ; Nishijima, Katsushi ; Zang, Jin Qi ; Kido, Mizuho A. ; Tanaka, Teruo. / Localization of the endogenous cysteine proteinase inhibitor, cystatin C, and the cysteine proteinase, cathepsin B, to the junctional epithelium in rat gingiva. In: Acta Histochemica et Cytochemica. 2005 ; Vol. 38, No. 2. pp. 121-129.
@article{d7cda389675044408c8b68c918ea9013,
title = "Localization of the endogenous cysteine proteinase inhibitor, cystatin C, and the cysteine proteinase, cathepsin B, to the junctional epithelium in rat gingiva",
abstract = "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.",
author = "Takayoshi Yamaza and Satoya Mino and Atsuta Ikiru and Atsushi Danjo and Tadayoshi Kagiya and Katsushi Nishijima and Zang, {Jin Qi} and Kido, {Mizuho A.} and Teruo Tanaka",
year = "2005",
month = "5",
day = "18",
doi = "10.1267/ahc.38.121",
language = "English",
volume = "38",
pages = "121--129",
journal = "Acta Histochemica et Cytochemica",
issn = "0044-5991",
publisher = "Japan Society of Histochemistry and Cytochemistry",
number = "2",

}

TY - JOUR

T1 - Localization of the endogenous cysteine proteinase inhibitor, cystatin C, and the cysteine proteinase, cathepsin B, to the junctional epithelium in rat gingiva

AU - Yamaza, Takayoshi

AU - Mino, Satoya

AU - Ikiru, Atsuta

AU - Danjo, Atsushi

AU - Kagiya, Tadayoshi

AU - Nishijima, Katsushi

AU - Zang, Jin Qi

AU - Kido, Mizuho A.

AU - Tanaka, Teruo

PY - 2005/5/18

Y1 - 2005/5/18

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=18244409352&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18244409352&partnerID=8YFLogxK

U2 - 10.1267/ahc.38.121

DO - 10.1267/ahc.38.121

M3 - Article

AN - SCOPUS:18244409352

VL - 38

SP - 121

EP - 129

JO - Acta Histochemica et Cytochemica

JF - Acta Histochemica et Cytochemica

SN - 0044-5991

IS - 2

ER -