• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.53 no.4
• /
• pp.515-523
• /
• 2020

Basal and heat shock-induced mRNA expression patterns of major heat shock protein (HSP) genes, including those encoding heat shock protein (HSP) 90, HSP70, HSP70-12A, heat shock inducible protein 70 (HSIP70), heat shock binding protein 1 (HSPBP1), HSP60, and HSP40 were examined in the gill and hepatopancreas of 1-year-old diploid and triploid abalone Haliotis discus hannai juveniles. Under non-stimulated conditions at 19℃, triploid abalones displayed, in general, higher mRNA levels of various HSPs (HSP70, HSIP70, HSPBP1, HSP70-12A, and HSP60 in the gill and HSIP70, HSPBP1, and HSP60 in the hepatopancreas) than did communally cultured diploids. Conversely, only the hepatopancreatic expression of HSP70-12A was higher in diploids than in triploids. However, the fold changes in gene expression in response to an acute thermal challenge (elevation from 19 to 30℃) were generally greater in diploids than in triploids, such that the difference in basal expression was diminished, weakened, or even reversed after heat shock treatment. However, unlike other HSP genes, the basal expression of HSP60 (higher in 3N) was more pronounced after heat shock treatment. Collectively, the results of this study suggest that triploid abalones have different capacities for not only basal expression but also the heat-induced expression of HSPs in an HSP member-dependent manner.

• Journal of Periodontal and Implant Science
• /
• v.33 no.4
• /
• pp.543-553
• /
• 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.

• Asian-Australasian Journal of Animal Sciences
• /
• v.30 no.1
• /
• pp.94-99
• /
• 2017

Objective: The aim of this study was to investigate the expression of heat shock protein (HSP) 90, 70, and 60 in chicken muscles and their possible relationship with quality traits of meat. Methods: The breast muscles from one hundred broiler chickens were analyzed for drip loss and other quality parameters, and the levels of heat shock protein (HSP) 90, 70, and 60 were determined by immunoblots. Results: Based on the data, chicken breast muscles were segregated into low (drip loss${\leq}5%$), intermediate (5%${\geq}9.5$) drip loss groups. The expression of HSP90 and HSP60 were significantly lower in the high drip loss group compared to that in the low and intermediate drip loss group (p<0.05), while HSP70 was equivalent in abundance in all groups (p>0.05). Conclusion: Results of this study suggests that higher levels of HSP90 and HSP60 may be advantageous for maintenance of cell function and reduction of water loss, and they could act as potential indicator for better water holding capacity of meat.

• Journal of Periodontal and Implant Science
• /
• v.33 no.4
• /
• pp.555-562
• /
• 2003

The present study has been performed to evaluate Porphyromonas gingivalis (P.gingivalis) heat shock protein(HSP)60 as a candidate vaccine to inhibit multiple bacteria-induced alveolar bone loss. Rats were immunized with P.gingivalis HSP60 and experimental alveolar bone loss was induced by infection with multiple periodonto -pathogenic bacteria. Post-immune rat anti-P.gingivalis HSP IgG levels were significantly elevated and have demonstrated highly significant inverse relationship with the amount of alveolar bone loss induced by multiple bacteria. Results from PCR detection of subgingival bacterial plaque indicated that the vaccine successfully eradicated the multiple pathogenic species. We concluded that P.gingivalis HSP60 could potentially be developed as a vaccine to inhibit periodontal disease induced by multiple pathogenic bacteria.

• The Korean Journal of Physiology and Pharmacology
• /
• v.8 no.6
• /
• pp.345-349
• /
• 2004

Heat shock ($43^{\circ}C$ for 60 minutes) is sufficient to induce apoptosis in a wide number of cell lines. In this study, we asked whether DNA strand breaks are responsible for this phenomenon. Using the highly sensitive comet assay for DNA damage detection, we were unable to demonstrate DNA breaks immediately after heat shock in Raji human Iymphoid cells. It showed that DNA breaks were not necessary for hyperthermic apoptosis, since its activity is indicative of DNA lesions. Here, we present a suggestion that a protein(s) is the major target for heat shock apoptosis. We firstly found glycerol, which reportedly stabilizes protein structure, showed a protective effect in Raji cells against hyperthermic apoptosis. In addition, quercetin, which modulates transcription of the heat shock protein family members, enhanced apoptotic death induced by hyperthermia. Furthermore, Raji cells are protected by a pre-mild heat treatment prior to the killing dose of heat shock.

• Food Science of Animal Resources
• /
• v.25 no.3
• /
• pp.350-356
• /
• 2005

We examined the enhancement of thermotolerance for storage conferred on Lactobacillus acidophilus 30SC by adaptation to different stresses. The viable cells of Lactobacillus acidophilus 30SC were compared with their viability prior to heating at $45,\;55^{\circ}C\;and\;60^{\circ}C$. Heat-adapted ($45^{\circ}C$ for 15 min) L. acidophilus 30SC in MRS broth exhibited higher survivability at lethal temperature of $55^{\circ}C$ than control. Cellular protein profiles of L. acidophilus 30SC during heat adaptation were examined with SDS-PAGE, and scanning electron microscopy. When L. acidophilus 30SC was heat-adapted at $55^{\circ}C$ for 15min, 5 new protein spots of ca $8\~45\;kDa$ size were observed on 2D SDS-PAGE. It was presumed that new proteins of L. acidophilus 30SC were produced to adapt to the environment of higher growth temperature.

• Journal of Periodontal and Implant Science
• /
• v.41 no.2
• /
• pp.54-59
• /
• 2011

Purpose: The aim of this study was to define the immunoreactive specificity of Porphyromonas gingivalis (P. gingivalis) heat shock protein (HSP) 60 in periodontitis and atherosclerosis. Methods: In an attempt to define the cross-reactive bacterial heat-shock protein with human self-antigen at molecular level, we have introduced a novel strategy for cloning hybridoma producing anti-P. gingivalis HSP 60 which is polyreactive to bacterial HSPs or to the human homolog. Results: Five cross-reactive clones were obtained which recognized the #19 peptide (TLVVNRLRGSLKICAVKAPG) among 37 synthetic peptides (20-mer, 5 amino acids overlapping) spanning the whole molecule of P. gingivalis HSP 60. We have also established three anti-P. gingivalis HSP 60 monoclonal antibodies demonstrating mono-specificity. These clones recognized the #29 peptide (TVPGGGTTYIRAIAALEGLK). Conclusions: Peptide #19 and #29 of P. gingivalis HSP 60 might be important immunoreactive epitopes in the immuno-pathogenic mechanism of bacterial antigen-triggered autoimmune diseases.

• Journal of Periodontal and Implant Science
• /
• v.33 no.2
• /
• pp.179-191
• /
• 2003

Since periodontal infections are suggested as risk factors for the development of cardiovascular diseases, the present study was performed to evaluate the T cell immune responses specific to Pophylomonas gingivalis(P. gingivalis) heat shock protein(hsp) 60 and T-cell and B-cell epitope specificities for P. gingivalis hsp60 in atherosclerosis. Anti-P, gingivalis IgG antibody titers were elevated in all patients. We could establish P. gingivalis hsp-specific T cell lines from the atheroma lesions, a mixture of $CD4^+$ and $CD8^+$ cells producing the cytokines characteristic of both Th1 and Th2 subsets. of 108 overlapping synthetic peptides spanning whole P. gingivalis hsp60 molecule, ten peptides with common epitopes specificities for both T-cell and B-cell were identified. it was concluded that P. gingivalis hsp60 might K involved in the immunoregulatory process of atherosclerotic diseases with epitope specificities.

• Journal of Microbiology
• /
• v.39 no.3
• /
• pp.162-167
• /
• 2001

Methylovorus sp. strain SS1 DSM 11726 was found to grow continuously when it was transferred from 30$\^{C}$ to 40$\^{C}$ and 43$\^{C}$. A shift in growth temperature from 30$\^{C}$ to 45$\^{C}$, 47$\^{C}$ and 50$\^{C}$ reduced the viability of the cell population by more than 10$^2$, 10$^3$and 10$\^$5/ folds, respectively, after 1h cultivation. Cells transferred to 47$\^{C}$ and 50$\^{C}$ after preincubation for 15 min at 43$\^{C}$, however, exhibited 10-fold increase in viability. It was found that incubation for 15 min at 40$\^{C}$ of Methylovorus sp. strain SSl grown at 30$\^{C}$ was sufficient to accelerate the synthesis of a specific subset of proteins. The major heat shock proteins had apparent molecular masses of 90, 70, 66, 60, and 58 kDA. The 60 and 58 kDa proteins were found to cross-react with the antiserum raised against GroEL protein. The heat shock response persisted for over 1h. The shock proteins were stable for 90 min in the cell. Exposure of the cells to methanol induced proteins identical to the heat shock proteins. Addition of ethanol induced a unique protein with a molecular mass of about 40 kDa in addition to the heat-induced proteins. The proteins induced in paraquat-treated cells were different from the heat shock proteins, except the 70 and 60 kDa proteins.

• Clinical and Experimental Reproductive Medicine
• /
• v.29 no.1
• /
• pp.37-44
• /
• 2002

Objective : Heat shock protein family is related to protective mechanism of cells by environmental changes. This study was performed to evaluate the effect of cryopreservation on the heat shock protein 90 (Hsp90) expression in mouse ovarian tissue. Methods : Cryopreservation of mouse ovarian tissue was carried out by slow freezing method. The mRNA level of Hsp90 expression in both fresh and cryopreserved mouse ovarian tissue was analyzed by RT-PCR. The protein expression of Hsp90 was evaluated by Western blot analysis and immunohistochemistry. Results: The mRNA and protein of Hsp90 were expressed in both fresh and cryopreserved mouse ovarian tissue. The amount of Hsp90 mRNA was increased in cryopreserved ovarian tissue after 60 and 90 minutes after thawing and incubation. The amount of Hsp90 protein was increased in the cryopreserved ovarian tissue after 6 hours of the incubation in Western blot analysis. In immunohistochemical study, Hsp90 protein was localized in cytoplasm of oocytes and granulosa cells. Significant level of immunoreactive Hsp90 protein was detected in theca cells contrast to the weak expression in ovarian epithelial cells. Conclusion: This results showed the increase of Hsp90 expression in both mRNA and protein level in the cryopreserved mouse ovarian tissue. It can be suggested that Hsp90 may play a role in the protective or recovery mechanism against the cell damage during cryopreservaion.