Language：English   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

Language：Japanese  

Language：English   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1016/S8756-3282(01)00466-5

Publishing type：Research paper (scientific journal)  

DOI： 10.1902/jop.1999.70.9.973

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1007/BF00315829

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1177/00220345930720030701

Event date： 2023.6

Language：Japanese  

Venue：愛知学院大学   Country：Japan  

Event date： 2015.8

Language：Japanese  

Venue：九州歯科大学   Country：Japan  

Event date： 2013.8

Language：English   Presentation type：Oral presentation (general)  

Venue：Bangkok   Country：Thailand  

Abstract
Objectives: It was reported that activated T cells in periodontal diseased gingival tissues expressed RANKL. Hence we investigated whether T cells in the tissues suffered from peri-implantitis could express RANKL or not.

Methods: Mini pure titanium implants (mini-implant) were placed into palatine bone of Wistar rats, followed by that lipopolysaccharide derived from Porphyromonas gingivalis (P.g.-LPS) was intermittently injected into the gingival tissues around mini-implant. Inflamed tissues by P.g.-LPS (P.g.-LPS samples) were collected from around mini-implant. The mRNA expression patterns of RANKL and OPG in the tissues, which were known as the markers of bone resorption, were examined by real-time RT-PCR. In addition, Immunohistochemical analysis was performed for comparative investigation of T cells expressing RANKL by using anti-CD3 and anti-RANKL antibodies. The tissues without P.g.-LPS were used as the control samples.

Results: P.g.-LPS enhanced the mRNA expressions of RANKL in the tissues around mini-implant, as compared with those of control samples without P.g.-LPS. On the other hand, the mRNA expressions of OPG in the P.g.-LPS samples were decreased. CD3- or RANKL-positive cells were observed in each tissue sample. However, only in the P.g.-LPS samples, the cells stained with both anti-CD3 and anti-RANKL antibodies were detected.

Conclusions: These data, taken together, revealed that P.g.-LPS injection enhanced the mRNA expressions of RANKL in the tissues around mini-implant of the rat model. Additionally, the CD3-positive cells in the tissues around mini-implant injected with P.g.-LPS expressed the RANKL molecules. Therefore, it is suggested that the activated T cells in the tissues suffered from peri-implantitis may be the primary sources of RANKL, similar to the case for periodontitis, and be involved in the bone resorption associated with peri-implantitis.

Event date： 2013.6

Language：Japanese  

Venue：大阪国際会議場   Country：Japan  

Antimicrobial and Antifungal Effects of Tissue Conditioners Containing the Photocatalyst

Event date： 2009.8

Presentation type：Public lecture, seminar, tutorial, course, or other speech  

Venue：カンポの宿柳川（福岡県柳川市）   Country：Japan  

Event date： 2009.6

Venue：国立京都国際会館   Country：Japan  

Antimicrobial and Antifungal Effects of Tissue Conditioners Containing the Photocatalyst

Venue：札幌コンベンションセンター（札幌）  

Venue：朱鷺メッセ（新潟）   Country：Japan  

Application of the Photocatalyst Titanium-Oxide to the Denture Base Resin-Responce of Cultured Gingival Fibroblasts-

Language：Japanese  

Language：Japanese  

Language：English  

We compared the distribution of a cysteine proteinase inhibitor, cystatin C, with that of cathepsin K in osteoclasts of the mouse tibia by immunolight and immunoelectron microscopy. Light microscopically, strong immunoreactivity for cystatin C was found extracellularly along the resorption lacuna and intracellularly in the organelles of osteoclasts. In serial sections, various patterns of cystatin C and cathepsin K localization were seen, specifically: (1) some resorption lacuna were positive for both cystatin C and cathepsin K; (2) others were positive for either cystatin C or cathepsin K, but not both; and (3) some lacuna were negative for both. In osteoclasts, the localization of cystatin C was similar to that of cathepsin K. Furthermore, cystatin C immunoreactivity was detected in preosteoclasts and osteoblasts, whereas cathepsin K was seen only in preosteoclasts. Electron microscopically, cystatin C immunoreactive products were found in the rough endoplasmic reticulum (ER), Golgi apparatus, vesicles, granules, and vacuoles of osteoclasts. These cystatin C-positive vesicles had fused or were in the process of fusion with the ampullar vacuoles (extracellular spaces) containing cystatin C-positive, fragmented, fibril-like structures. The extracellular cystatin C was deposited on and between the cytoplasmic processes of ruffled borders, and on and between type I collagen fibrils. In the basolateral region of osteoclasts, cystatin C-positive vesicles and granules also fused with vacuoles that contained cystatin C-positive or negative fibril-like structures. These results indicate that osteoclasts not only synthesize and secrete cathepsin K from the ruffled border into the bone resorption lacunae, but also a cysteine proteinase inhibitor, cystatin C. Therefore, it is suggested that cystatin C regulates the degradation of bone matrix by cathepsin K, both extracellularly and intracellularly. (C) 2001 by Elsevier Science Inc. All rights reserved.

DOI： 10.1016/S8756-3282(01)00466-5

Language：English  

We compared the distribution of a cysteine proteinase inhibitor, cystatin C, with that of cathepsin K in osteoclasts of the mouse tibia by immunolight and immunoelectron microscopy. Light microscopically, strong immunoreactivity for cystatin C was found extracellularly along the resorption lacuna and intracellularly in the organelles of osteoclasts. In serial sections, various patterns of cystatin C and cathepsin K localization were seen, specifically: (1) some resorption lacuna were positive for both cystatin C and cathepsin K; (2) others were positive for either cystatin C or cathepsin K, but not both; and (3) some lacuna were negative for both. In osteoclasts, the localization of cystatin C was similar to that of cathepsin K. Furthermore, cystatin C immunoreactivity was detected in preosteoclasts and osteoblasts, whereas cathepsin K was seen only in preosteoclasts. Electron microscopically, cystatin C immunoreactive products were found in the rough endoplasmic reticulum (ER), Golgi apparatus, vesicles, granules, and vacuoles of osteoclasts. These cystatin C-positive vesicles had fused or were in the process of fusion with the ampullar vacuoles (extracellular spaces) containing cystatin C-positive, fragmented, fibril-like structures. The extracellular cystatin C was deposited on and between the cytoplasmic processes of ruffled borders, and on and between type I collagen fibrils. In the basolateral region of osteoclasts, cystatin C-positive vesicles and granules also fused with vacuoles that contained cystatin C-positive or negative fibril-like structures. These results indicate that osteoclasts not only synthesize and secrete cathepsin K from the ruffled border into the bone resorption lacunae, but also a cysteine proteinase inhibitor, cystatin C. Therefore, it is suggested that cystatin C regulates the degradation of bone matrix by cathepsin K, both extracellularly and intracellularly. (C) 2001 by Elsevier Science Inc. All rights reserved.

DOI： 10.1016/S8756-3282(01)00466-5

Language：English  

Background: Age-dependent morphological and cell kinetic changes of the gingival tissue seem to be related to the occurrence of periodontal disease. The purpose of this study was to investigate the age-dependent changes in the distribution of BrdU- and TUNEL-positive cells in murine gingival tissue.
Methods: Gingival tissue of the lower first molar region of 2-, 3-, 5-, 7-, 10-, 15-, 20-, 30-, 40-, 50-, 60-, 70- and 80-week-old mice was used in this study. BrdU- and TUNEL-positive cells were evaluated at the following 4 sites: 1) gingival epithelium (GE); 2) junctional epithelium (JE); 3) submucosal connective tissue of the gingival epithelium (GECT); and 4) submucosal connective tissue of the junctional epithelium (JECT).
Results: No significant differences in the mean number of BrdU-positive cells at each site were demonstrated among the various age groups. No significant change in the mean number of TUNEL-positive cells was demonstrated in either the GE or JE groups among the various age groups. Meanwhile, a significant increase in the TUNEL-positive cells was observed in the GECT of mice 40 weeks or older, and in the JECT of mice 20 weeks or older.
Conclusions: These results indicate that no age-dependent change in the cell proliferation or cell death occurred in the gingival and junctional epithelial layers as well as in the cell proliferation in the submucosal connective tissue. Meanwhile, a significant decrease in the cellular component of the submucosal connective tissue of both gingival and junctional epithelial layers caused by apoptosis occurred with aging. The decreased cellular component in the submucosal connective tissue thus seems to be related to either gingival recession or to the apical migration of the JE with aging. These morphological changes with aging possibly occur in humans and may be related to the susceptibility to periodontal disease in aged individuals.

DOI： 10.1902/jop.1999.70.9.973

Language：English  

Background: Age-dependent morphological and cell kinetic changes of the gingival tissue seem to be related to the occurrence of periodontal disease. The purpose of this study was to investigate the age-dependent changes in the distribution of BrdU- and TUNEL-positive cells in murine gingival tissue.
Methods: Gingival tissue of the lower first molar region of 2-, 3-, 5-, 7-, 10-, 15-, 20-, 30-, 40-, 50-, 60-, 70- and 80-week-old mice was used in this study. BrdU- and TUNEL-positive cells were evaluated at the following 4 sites: 1) gingival epithelium (GE); 2) junctional epithelium (JE); 3) submucosal connective tissue of the gingival epithelium (GECT); and 4) submucosal connective tissue of the junctional epithelium (JECT).
Results: No significant differences in the mean number of BrdU-positive cells at each site were demonstrated among the various age groups. No significant change in the mean number of TUNEL-positive cells was demonstrated in either the GE or JE groups among the various age groups. Meanwhile, a significant increase in the TUNEL-positive cells was observed in the GECT of mice 40 weeks or older, and in the JECT of mice 20 weeks or older.
Conclusions: These results indicate that no age-dependent change in the cell proliferation or cell death occurred in the gingival and junctional epithelial layers as well as in the cell proliferation in the submucosal connective tissue. Meanwhile, a significant decrease in the cellular component of the submucosal connective tissue of both gingival and junctional epithelial layers caused by apoptosis occurred with aging. The decreased cellular component in the submucosal connective tissue thus seems to be related to either gingival recession or to the apical migration of the JE with aging. These morphological changes with aging possibly occur in humans and may be related to the susceptibility to periodontal disease in aged individuals.

DOI： 10.1902/jop.1999.70.9.973

Language：English  

The localization of cathepsin L and rat salivary cystatin-3 (RSC-3) in rat osteoclasts (rat femoral and alveolar bones) treated with or without E-64 (control) was examined immunocytochemically. In osteoclasts pretreated with E-64, immunoreactivity for cathepsin L was very weak extracellularly compared to that in the control osteoclasts. However, it was strong intracellularly. The localization of RSC-3 was unclear in the control osteoclasts, while in E-64 treated osteoclasts, both the clear zone and ruffled border areas showed a very strong immunoreaction. At the electron-microscopic level, in normal osteoclasts, numerous immunoreaction products for cathepsin L were found extracellularly in the bone matrix under the ruffled border, while few intracellular products were observed. In contrast, in the E-64-treated osteoclasts, only a few immunoreaction products were found extracellularly, while intracellularly cathepsin L was found in numerous endosome-lysosomal vacuoles. In the immunoreaction for RSC-3, the cytoplasm of the ruffled border was positive, and the tips of the RSC-3-positive ruffled border appeared to enter deeply into the bone matrix. Intracellularly, the granular reaction products of RSC-3 were found in the vacuoles (probably autophagolysosomes). Thus, in E-64-treated osteoclasts, inhibition of the extracellular release of cathepsin L was demonstrated. In addition, intralysosomal accumulation of RSC-3 and deep penetration of the RSC-3-positive ruffled border into the bone matrix were found. These findings suggest that RSC-3 is associated with the inhibition of cathepsin L in both the lysosomes (in the osteoclasts) and bone matrix. (C) 1997 Elsevier Science Ltd.

DOI： 10.1016/S0003-9969(97)00003-4

Language：English  

The localization of cathepsin L and rat salivary cystatin-3 (RSC-3) in rat osteoclasts (rat femoral and alveolar bones) treated with or without E-64 (control) was examined immunocytochemically. In osteoclasts pretreated with E-64, immunoreactivity for cathepsin L was very weak extracellularly compared to that in the control osteoclasts. However, it was strong intracellularly. The localization of RSC-3 was unclear in the control osteoclasts, while in E-64 treated osteoclasts, both the clear zone and ruffled border areas showed a very strong immunoreaction. At the electron-microscopic level, in normal osteoclasts, numerous immunoreaction products for cathepsin L were found extracellularly in the bone matrix under the ruffled border, while few intracellular products were observed. In contrast, in the E-64-treated osteoclasts, only a few immunoreaction products were found extracellularly, while intracellularly cathepsin L was found in numerous endosome-lysosomal vacuoles. In the immunoreaction for RSC-3, the cytoplasm of the ruffled border was positive, and the tips of the RSC-3-positive ruffled border appeared to enter deeply into the bone matrix. Intracellularly, the granular reaction products of RSC-3 were found in the vacuoles (probably autophagolysosomes). Thus, in E-64-treated osteoclasts, inhibition of the extracellular release of cathepsin L was demonstrated. In addition, intralysosomal accumulation of RSC-3 and deep penetration of the RSC-3-positive ruffled border into the bone matrix were found. These findings suggest that RSC-3 is associated with the inhibition of cathepsin L in both the lysosomes (in the osteoclasts) and bone matrix. (C) 1997 Elsevier Science Ltd.

DOI： 10.1016/S0003-9969(97)00003-4

Language：English  

The localization of cathepsins B, D, and L was studied in rat osteoclasts by immuno-light and -electron microscopy using the avidin-biotin-peroxidase complex (ABC) method. In cryosections prepared for light microscopy, immunoreactivity for cathepsin D was found in numerous vesicles and vacuoles but was not detected along the resorption lacunae of osteoclasts. However, immunoreactivity for cathepsins B and L occurred strongly along the lacunae, and only weak intracellular immunoreactivity was observed in the vesicles and peripheral part of the vacuoles near the ruffled border. In control sections that were not incubated with the antibody, no cathepsins were found in the osteoclasts or along the resorption lacunae of osteoclasts. At the electron microscopic level, strong intracellular reactivity of cathepsin D was found in numerous vacuoles and vesicles, while extracellular cathepsin D was only slightly detected at the base of the ruffled border but was not found in the eroded bone matrix. Most osteoclasts showed strong extracellular deposition of cathepsins B and L on the collagen fibrils and bone matrix under the ruffled border. The extracellular deposition was stronger for cathepsin L than for cathepsin B. Furthermore cathepsins B and L immunolabled some pits and part of the ampullar extracellular spaces, appearing as vacuoles in the sections. Conversely, the intracellular reactivity for cathepsins B and L was weak: cathepsin-containing vesicles and vacuoles as primary and secondary lysosomes occurred only sparsely. These findings suggest that cathepsins B and L, unlike cathepsin D, are rapidly released into the extracellular matrix and participate in the degradation of organic bone matrix containing collagen fibrils near the tip of the ruffled border. Cathepsin L may be more effective in the degradation of bone matrix than cathepsin B.

Language：English  

The density and distribution of substance P-like immunoreactive (SP-LI) and calcitonin gene-related peptide-like immunoreactive (CGRP-LI) nerve fibers in rat temporomandibular joint (TMJ) were investigated in whole-mount preparations and frozen sections by immunohistochemistry with the avidin-biotin-peroxidase complex method.
Both types of immunoreactive nerves were observed primarily in the joint capsule, the peripheral articular disc, the synovial membrane, and the periosteum. The distribution of CGRP-LI nerves was similar to that of SP-LI nerves. The anterior portion of the joint capsule and disc was most densely innervated, followed by the posterior, lateral, and medial portions. In addition, CGRP-LI nerves were more numerous and more dense in immunointensity than SP-LI nerves. In the synovial membrane, many SP- and CGRP-LI nerves terminated in the subsynovial layer, but some branches extended into the superficial synovial lining layer close to the joint cavity. Immunolabeled nerves were prominently located in the disc attachment and peripheral portion of the disc, and occasional nerves were located in the dense collagenous disc band as an actual disc. However, no fibers were detected in the central disc band. Thus, most of the disc was not innervated by any nerves.
The present study provides a morphological basis for the possible roles of neuropeptides in endocytosis by synoviocytes, regulation of blood flow in the synovial membrane, nociception mechanisms of the TMJ, and modulation of the inflammatory response in the TMJ.

研修医の教育（指導医）

OSCE　外部評価者　長崎大学

OSCE　外部評価者　朝日大学

研修医の教育（指導医）

OSCE　外部評価者　福岡歯科大学

研修医の教育（指導医）

研修医の教育（指導医）

研修医の教育(指導医）

研修医の教育(指導医）

OSCE内部評価者参加

Clinical Instructor for resident

OSCE内部評価者参加

研修医の教育（指導医）

研修医の教育（指導医）

OSCE内部評価者参加

研修医の教育（指導医）

OSCE補助者参加