| Project/Area Number |
10470447
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B).
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
矯正・小児・社会系歯学
|
|---|
| Research Institution | The University of Tokushima |
|---|
Principal Investigator |
HINODE Daisuke The University of Tokushima, School of Dentistry, Associate Professor, 歯学部, 助教授 (70189801)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
MASUDA Kaname The University of Tokushima, School of Dentistry, Research Associate, 歯学部, 助手 (30243710)
YOSHIOKA Masami The University of Tokushima, School of Dentistry, Assistant Professor, 歯学部・附属病院, 講師 (90243708)
NAKAMURA Ryo The University of Tokushima, School of Dentistry, Professor, 歯学部, 教授 (30034169)
YOKOYAMA Masaaki The University of Tokushima, School of Dentistry, Research Associate, 歯学部・附属病院, 助手 (10314882)
TANABE Shin-ichi The University of Tokushima, School of Dentistry, Research Associate, 歯学部, 助手 (40284301)
杉山 明子 徳島大学, 歯学部, 助手 (90304534)
三木 修 徳島大学, 歯学部, 助手 (30284300)
|
|---|
| Project Period (FY) |
1998 – 2000
|
| Project Status |
Completed (Fiscal Year 2000)
|
| Budget Amount *help |
¥10,100,000 (Direct Cost: ¥10,100,000)
Fiscal Year 2000: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1999: ¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1998: ¥6,300,000 (Direct Cost: ¥6,300,000)
|
|---|
| Keywords | Heat shock proteins / Periodontopathogenic bacteria / Host response / Homology / Cytotoxicity / Interleukin secretion / Campylobacter rectus / Actinobacillus actinomycetemcomitans / GroEL様蛋白質 / 遺伝子解析 / 局在性 / 炎症性サイトカイン / ヒト歯肉線維芽細胞 / Helicobacter pylori / N-末端アミノ酸配列 / 歯周病原細菌 / 病原因子 / 精製 |
|---|
| Research Abstract |
The metabolism of oral microorganisms is largely influenced by the changing environment which also lead to the synthesis of stress proteins such as heat shock proteins (HSPs). HSPs belong to some families of highly conserved homology. We focused on the periodontal disease and HSPs as periodontopathogen because these proteins were immunodominant antigens. Our results indicated that the GroEL-like protein, belonging to HSP60 family, from periodontopathogens possessed epitope cross-reactive with that from human origin. The nucleotide sequence was determined directly using the PCR product corresponding to the Campylobacter rectus GroEL-like protein, and analyzed. By the comparison of the alignment of the deducted amino acid sequence with those of human HSP60, the similarity throughout its length was confirmed. It is possible that high homology of HSPs within the same family and their common epitopes with host molecule lead to autoimmune responses.
The native GroEL-like protein from C.rectus and Actinobacillus actinomycetemcomitans possessed biological activities. The C.rectus GroEL-like protein stimulated both interleukin-6 (IL-6) and IL-8 secretion by a confluent monolayer of human gingival fibroblast in their culture supernatant. During the 22h-incubation, the amounts of IL-6 and IL-8 were increased by 5.4- and 3.5-fold, respectively. A.actinomycetemcomitans GroEL-like protein had a significant cytotoxic effect on both periodontal ligament epithelial cells and HaCaT epithelial cells grown in vitro at higher concentrations. On the other hand, we determined the external localization of A.actinomycetemcomitans GroEL-like protein with specific antibodies using immunoelectron microscopy. These results demonstrated that the A.actinomycetemcomitans GroEL-like protein and the C.rectus GroEL-like protein possessed biological activities influencing on the host cells, therefore, these proteins could play important roles in periodontal disease.
|
