• Title/Summary/Keyword: 열충격단백

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T-and cross-reactive B-cell epitopes of Porphyromonas gingivalis and human heat shock protein 60 in atherosclerosis (동맥경화증에 있어서 Porphyromonas gingivalis와 인체 열충격단백의 T-세포 및 교차성 B-세포 epitope)

  • Choi, Jeom-Il
    • Journal of Periodontal and Implant Science
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    • v.33 no.3
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    • pp.331-340
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    • 2003
  • 본 연구의 목적은 인간의 동맥경화증에서 Porphyromonas gingivalis (P. gingivalis)와 인체 열충격단백 60의 T-세포 및 교차성 B-세포 epitope를 규명하고 수립된 T-세포주의 T-세포 주요조직적합체 양상을 파악하려는 데 있다. P. gingivalis 열충격단백-반응성 T 세포주와 환자의 혈청을 이용하여 P. gingivalis 열충격단백60 분자를 구성하는 104개의 중복성 합성 펩타이드의 T-세포 epitope과 B-세포 epitope을 규명하였다. 인체 열충격단백60에 대한 B-세포 epitope도 같은 방법으로 파악하였다. P. gingivalis, P. gingivalis 열충격단백60 또는 인체 열충격단백60에 대한 IgG 항체는 모든 동맥경화증 환자에서 상승하였다. P. gingivalis 열충격단백60의 3, 15, 24, 33, 45, 53, 64, 84, 88, 99번 펩타이드가 주요한 T-세포 epitope였고 이것들은 T-세포 및 B-세포 공동 epitope이기도 했다. 또한 인체 열충격단백60 교차반응 B-세포 epitope은 15, 29, 53, 56, 69, 74번 펩타이드로 판명되었다. 대부분 환자의 주요조직적합체는 $HLA-DRB1^{\ast}1504$$HLA-DZB1^{\ast}0603$으로 나타났다. 결론적으로 P. gingivalis 열충격단백60은 제 2급 주요조직적합제-제한적으로 분해되고 전달되었으며 이 단백질이 공통적인 T-세포 및 B-세포 epitope를 가지면서 동시에 인체 열충격단백60과 교차성 B-세포 epitope을 가지면서 동맥경화증의 면역조절기능에 관여한다고 볼 수 있다.

Antibody response of periodontal patients to Porphyromonas gingivalis heat shock protein (P. gingivalis 열충격단백에 대한 치주질환자의 항체반응)

  • Choi, Jeom-IL;Kim, Sung-Jo;Kim, Su-Jin
    • Journal of Periodontal and Implant Science
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    • v.32 no.1
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    • pp.25-32
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    • 2002
  • 재조합 P. gingivalis 열충격단백에 대한 치주질환자의 항체반응과 세포성 면역반을을 검사한 결과, 항체역가는 건강군의 역가에 비해 통계적으로 유의성 있게 상승되어 있었고, 항원특이성 T 세포면역반응을 관찰할 수 있었다. 이러한 결과로 미루어보아 P. gingivalis 열충격단백은 치주질환의 면역병리기전에 관여한다는 것을 관찰할 수 있었다.

Environmental factors regulating the expression of Porphyromonas gingivalis heat shock protein (Porphyromonas gingivalis의 열충격단백 발현조절 환경인자에 관한 연구)

  • Choi, Jeom-Il
    • Journal of Periodontal and Implant Science
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    • v.34 no.1
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    • pp.29-33
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    • 2004
  • The present study was done to evaluate the environmental factors responsible for the expression of Porphyromonas gingivalis heat shock protein. The intensity of the heat shock protein gene expression was comparable to those seen by the heat shock ptreatment of the bacteria $(44^{\circ}C)$ when the bacteria was grown as a mixed culture or biofilm state at $37^{\circ}C$.

The Expression of Heat Shock Protein in the Experimental Tooth Movement in Rats (백서의 실험적 치아이동시 열충격 단백의 발현)

  • Yoo, Dong-Whan;Kim, Eun-Cheol;Kim, Sang-Cheol
    • The korean journal of orthodontics
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    • v.31 no.2 s.85
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    • pp.249-259
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    • 2001
  • This study was designed to evaluate the expression of heat shock protein in tooth and surrounding tissue during the experimental movement of rat incisors, by LSAB(labelled streptavidine biotin) immunohistochemical staining for heat shock protein. Twenty seven Sprague-Dawley rats were divided into a control group(3 rats), and 6 experimental groups(24 rats), to which 75g of force was applied from helical springs across the maxillary incisors. Rats of experimental groups were sacrificed at 0.5, 1, 4, 7, 14 and 28 days after force application, respectively. And the periodontal tissues of a control group and experimental groups were studied immunohistochemically. The results were as follows : 1. In control group, the expression of HSP47 was rare in gingiva, dentin and cementum, and mild in periodontal ligament and alveolar bone. But it was more evident than that of HSP70. 2. The expression of HSP47 or HSP70 was rare or mild in dentin, cementum and odontoblast of experimental group, regardless of the duration of force application, which was not different from that of control group. 3. In experimental group, the expression of HSP47 got to the highest degree in periodontal ligament and alveolar bone at 4 days after force application, and then decreased. And the expression was more evident in the pressure side than in the tension side of periodontal ligament 4. The expression of HSP70 began to increase at 12 hours after force application and got to the highest degree at 4 days, in the capillary of pulp and periodontal ligament. And the expression was more evident in the pressure side than in the tension side of periodontal ligament 5. The expression of HSP70 in alveolar bone of experimental group was rare, which was similar to that of control group.

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T-cell epitope specificity for Porphyromonas gingivalis heat shock protein in periodontitis (치주염환자의 Porphyromonas gingivalis 열충격단백에 대한 T-세포 항원 결정부위 특이성 연구)

  • Lee, Ji-Young;Lee, Ju-Yeon;Choi, Jeom-Il
    • Journal of Periodontal and Implant Science
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    • v.33 no.4
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    • pp.543-553
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    • 2003
  • Due to considerably high degree of sequence homology between bacterial and human heat shock proteins(hsp), it has been widely thought that this protein might be involved in autoimmune disease mechanisms in humans. To elucidate how stress proteins contribute in the immunopathogenesis of periodontitis, the present study was performed to evaluate the T cell immune responses specific to Porphyromonas gingivalis (P. gingivalis) heat shock protein (hsp)60 and T-cell epitope specificities for P. gingivalis hsp60 in periodontitis. Anti-P. gingivalis IgG antibody titers were elevated in all patients. We could establish P. gingivalis hsp-specific T cell ines from the peripheral blood of peridontitis, a mixture of $CD4^+$ and $CD8^+$ cells. Of 108 overlapping synthetic peptides spanning whole P. gingivalis hsp60 moleculc, ten peptides with cpitopes specifities for T-cell were showed. Interestingly, ten epitopes were also identified as T-cell epitopes in the present study as well as B-cell epitopes in peridontitis. Therefore, all the ten representative epitopes were designated as common T-and B-cell epitopes for peridontitis. It is critical in developing a peptide vaccine strategy for potential prevention of periodontitis. It was concluded that P. gingivalis hsp60 might be involved in the immunoregulatory process of periodontitis with heat shock protein specificities.

Development of monoclonal antibody against Porphyromonas gingivalis heat shock protein (Porphyromonas gingivali의 열충격단백-특이성 단클론항체의 개발)

  • Yi, Ni-Na;Lee, Ju-Youn;Kim, Sung-Jo;Choi, Jeom-II
    • Journal of Periodontal and Implant Science
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    • v.37 no.1
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    • pp.11-21
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    • 2007
  • Heat shock protein (HSP) is one of cellular protein commonly present in major periodontopathogenic bacteria as well as mammalian cells. The protein may play a role in the immunopathogenesis by modulating autoimmune reaction due to its high level of sequence homology between bacteria and human counterpart. Hence, identifying immunodomiant epitope of bacteria HSP that is cross-reactive to periodontopathogenic bacteria with a specificity to human HSP may comprise a critical strategy for development of a periodontal vaccine. The present study was performed to establish clones producing monoclonal antibody reactive to Porphyromonas gingivalis (p. gingivalis) HSP with a specificity to human HSP. 4 different hybridomas were cloned producing monoclonal IgG antibodies to P, gingivalis HSP and evaluated for their reactivity and specificity to other periodontopathogenic bacteria as well as to human HSP. These four monoclonal antibodies reacted with p. gingivalis HSP only with specificities to other bacteria tested and human HSP as well. The antigenic epitopes producing the 4 monoclonal antibody may be potentially developed as vaccine candidates. Further investigations are under way to identify more clones producing monoclonal antibodies reactive to P, gingivalis HSP and to other periodontopathogenic bacteria as well, while maintaining specificities to human counterpart.