• Title/Summary/Keyword: Heat Shock protein

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Proteome Analysis of Pigs Fed with Tissue Culture Medium Waste after Harvest of Korean Wild Ginseng (산삼배양액을 급여한 돼지에서 근육의 프로테옴 분석)

  • Seol, Jae-Won;Chae, Joon-Seok;Kang, Hyung-Sub;Kang, Chun-Seong;Ihn, Dong-Chul;Park, Sang-Youel
    • Journal of Veterinary Clinics
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    • v.28 no.1
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    • pp.75-80
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    • 2011
  • Proteomics is a useful approach to know protein expression, post-translational modification and protein function. We investigated the protein expression pattern and identity in pigs fed with the tissue culture medium waste after harvest of Korean wild ginseng (TCM-KWG) (Panax ginseng). Two groups (n = 30/group) of pigs were administered with 0 (control) and 16 ml/L (treatment) TCM-KWG through drinking water. After 4 weeks, we examined the protein expression pattern of longissimus dorsi muscle by Two-dimensional electrophoresis analysis. TCM-KWG treatment significantly increased two spot's density, and markedly reduced one spot's density in the muscles. We identified 3 proteins (heat shock protein 90-alpha, myosin binding protein and cofilin 2) by the ESI-MS/MS (Q-TOF2, Micromass). These results demonstrate that TCM-KWG treatment may play a protection role against physiological stress in pigs, like as increased heat shock protein 90-alpha.

Heat Shock and Cell Cycle Dependence of Cell Surface Proteins in Mouse Tumor Cells (溫熱處理와 細胞週期에 따른 생쥐 腫瘍細胞의 膜表面蛋白質의 變化)

  • Kang, Man-Sik;Kim, Yunhee
    • The Korean Journal of Zoology
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    • v.26 no.3
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    • pp.155-170
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    • 1983
  • The primary concern has been focused on the response and adaptation of mouse fibroblast tumor cells to heat-shock in the level of membrane surface proteins, using two labeling techniques, lactoperoxidase-catalyzed iodination and galactose oxidase-sodium borohydride. Cells arrested in $G_1$ phase exhibited the highest level of LETS protein and high molecular proteins than did cells passing through $G_1/S, S, G_2$ and M, and unsynchronized cells. Confluent cells were found to show an increase in 125K proteins and a decrease in 130K and 100K proteins selectively. The adaptation processes of tumor cells after heat-shock were observed. All the proteins above 80K were reduced immediately after heat-shock, whereas 70K protein increased markedly 24 hours after heat-shock. The 70K protein and high molecular proteins returned to normal level in 48 hours. The 70K protein was found to be trypsin-sensitive and was similarly labeled by galactose-oxidase as well as by lactoperoxidase. It was, therefore, concluded that 70K protein is glycoprotein located on the surface membrane and might be the HSP 70. Possible function of heat-shock protein on the surface membrane and the relation of this protein to differential heat-sensitivity of tumor cells are discussed.

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Induction of Heat Shock Protein 70 Inhibits Tumor Necrosis $Factor{\alpha}-induced$ Lipid Peroxidation in Rat Mesangial Cells (Heat Shock Protein 70이 흰쥐 배양 혈관간 세포에서 관찰되는 $TNF{\alpha}$에 의한 지질과산화에 미치는 보호 효과)

  • Ha, Hun-Joo;Park, Young-Mee;Ahn, Young-Soo;Kim, Kyung-Hwan
    • The Korean Journal of Pharmacology
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    • v.31 no.3
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    • pp.323-331
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    • 1995
  • Monocyte/macrophage infiltration is the well known initial features associated with the development of glomerular disease including non-immune mediated nephropathy. Tumor necrosis factor ${\alpha}(TNF{\alpha})$, a cytokine produced primarily by monocyte/macrophage, exhibits similar effects as observed at the initial stages and during the progression of glomerular injury. Because the mesangial cells are target cells for glomerular injury, the present study examined the effect of $TNF{\alpha}$ on glomerular mesangial cell membrane lipid peroxidation as an index of cytotoxicity attributing to $TNF{\alpha}$. Primary culture of rat mesangial cell was established by incubation of glomeruli isolated from male Sprague-Dawley rat kidneys utilizing a standard sieving method. The levels of lipid peroxides in the mesangial cells were quantitated by malondialdehyde- thiobarbituric acid adduct formation. During an 8 hour incubation at $37^{\circ}C$, $TNF{\alpha}$ at 10 to 10,000 units/ml increased the levels of lipid peroxides dose dependently. Western blot analysis demonstrated that a short thermal stress induced heat shock response and the synthesis of heat shock protein 70(hsp70) in this mesangial cells. Further, this induction of hsp 70 prevented increase of lipid peroxides in the mesangial cells exposed to $TNF{\alpha}$. These data suggest that $TNF{\alpha}-induced$ lipid peroxidation in the mesangial cells may have pathophysiological relevance to glomerular injury and prior induction of heat shock response may play a role in the cellular resistance against $TNF{\alpha}-induced$ glomerular injury.

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Reduced alveolar bone loss in rats immunized with Porphyromonas gingivalis heat shock protein (Porphyromonas gingivalis 열충격 단백으로 면역한 백서에서의 치조골 파괴의 감소)

  • Yi, Ni-Na;Lee, Ju-Youn;Choi, Jeom-Il
    • Journal of Periodontal and Implant Science
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    • v.33 no.4
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    • pp.555-562
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    • 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.

Proposal of Dual Inhibitor Targeting ATPase Domains of Topoisomerase II and Heat Shock Protein 90

  • Jun, Kyu-Yeon;Kwon, Youngjoo
    • Biomolecules & Therapeutics
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    • v.24 no.5
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    • pp.453-468
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    • 2016
  • There is a conserved ATPase domain in topoisomerase II (topo II) and heat shock protein 90 (Hsp90) which belong to the GHKL (gyrase, Hsp90, histidine kinase, and MutL) family. The inhibitors that target each of topo II and Hsp90 are intensively studied as anti-cancer drugs since they play very important roles in cell proliferation and survival. Therefore the development of dual targeting anti-cancer drugs for topo II and Hsp90 is suggested to be a promising area. The topo II and Hsp90 inhibitors, known to bind to their ATP binding site, were searched. All the inhibitors investigated were docked to both topo II and Hsp90. Four candidate compounds as possible dual inhibitors were selected by analyzing the molecular docking study. The pharmacophore model of dual inhibitors for topo II and Hsp90 were generated and the design of novel dual inhibitor was proposed.

Immunohistochemical Localization of Heat Shock Protein 70 in the Central Nervous System of Nicotine-treated Rat Embryo (태서 중추신경계의 Heat Shock Protein 70 분포에 대한 Nicotine 영향)

  • 최병태;강호성
    • Journal of Life Science
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    • v.7 no.4
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    • pp.276-281
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    • 1997
  • This study was investigated to determine whether nicotine causes the morphological changes and expression of heat shock protein(HSP) 70 in the central nervous system of rat embryo. The pregnant rats were injected s.c. twice daily with 3 mg nicotine per 100g body weight from day 0 to 14 of gestation and embryos were removed on gestation day 15. As morphological changes, retardation of cell proliferaton was observed in the telencephalon of nicotine-treated groups and no changes in the other region were found. Minimal HSP 70 was expressed over chole central nervous system was similar between control and nicotine-treated group, the expression of blood cells in the meinges and chroid plexus was significantly greater in nicotine-treated group than in control.

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Inhibitory Effects of Tannic Acid on the Skin Toxicity and Heat Shock Protein Induction by UVB Irradiation in Hairless Mouse (자외선 B 파로 유도된 Hairless Mouse에서 타닌의 피부 독성 억제효과 및 Heat Shock Protein 70의 생성억제 효과)

  • 이세윤;이민경;장동덕;안령미;안형수
    • Toxicological Research
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    • v.13 no.1_2
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    • pp.79-86
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    • 1997
  • Inhibitory effects of tannic acid on skin toxicity and heat shock protein induced by UVB were investigated. Tannic acid was administered either topically or orally for 3 days to hairless mice, which were previously irradiated with UVB. UVB was found to cause skin erythema . However, the skin erythema was decreased when tannic acid was administered either topically or orally. The heat shock proteins, Hsp-78 kDa and 70 kDa, were induced by UVB irradiation, but the induction was decreased by treatment of tannic acid in both topically and orally administered groups. The hsp induction was more prominent in orally administered groups than in topically administerd groups. However, the difference between two groups was not statistically significant. The route of administrations, topical and oral, does not affect the activity of tannic acid. In the skin tissue observation, tannic acid regenerated the epithelial cells with 7-9 cell layers which were injured by UVB. In conclusion, tannic acid has an ability to protect against UVB irradiation and regenerate the skin.

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Expression of the Heat Shock Protein Genes in Response to Thermal Stress in the Silkworm Bombyx mori

  • Velu, Dhanikachalam;Ponnuvel, Kangayam. M.;Qadri, Syed. M. Hussaini
    • International Journal of Industrial Entomology and Biomaterials
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    • v.16 no.1
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    • pp.21-27
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    • 2008
  • The expression of heat shock protein genes (Hsp 70, Hsp 40, Hsp 20.8 and Hsp 20.4) against thermal stress in silkworm Bombyx mori was performed through semi-quantitative reverse transcriptase-polymerase chain reaction (RT-PCR). Upon exposure of silkworm to two temperature regimes ($38^{\circ}C$ and $42^{\circ}C$), significant change in the expression of Hsp gene was observed as compared to the control. Hsp 70 and Hsp 40 showed increased expression than the small heat shock protein genes Hsp 20.8 and Hsp 20.4. The Hsp 70 showed increased expression during the recovery period as compared to 1 hr thermal treatments ($38^{\circ}C$/1 hr and $42^{\circ}C$/1 hr). Whereas, Hsp 40, Hsp 20.8 and Hsp 20.4 genes showed higher expression level at initial stages that later gradually decrease during recovery period. Tissue specific expression of Hsp 70 showed variation in the level of expression amongst the tissues. The mid gut and fat body tissues showed higher expression than the cuticle and silk gland tissue. The Hsp 70, Hsp 40 gene expression was analyzed in thermotolerant (Nistari) and thermo susceptible silk worm strain (NB4D2) and results showed significant variation in their expression level. The Nistari showed higher expression of Hsp 70 and Hsp 40 genes than the NB4D2. These findings provide a better understanding of cellular protection mechanisms against environmental stress such as heat shock, as these Hsps are involved in an organism thermotolerance.

Expression of the Heat Shock Proteins and Glucose-Regulated Proteins during Phorbol 12-Myristate 13-Acetate-Induced Megakaryocytic Differentiation of K562 Erythroleukemia Cells (K562 백혈구암 세포의 Phorbol 12-Myristate 13-Acetate에 의한 대핵세포로의 분화과정에서 Heat Shock Proteins와 Glucose-Regulated Proteins의 발현)

  • 이창훈;김우진;김종묵;한송이;김정락;한규형;임운기;유미애;강호성
    • The Korean Journal of Zoology
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    • v.39 no.1
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    • pp.47-53
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    • 1996
  • We examined the expression of the heat shock proteins (HSPs) and glucose-regulated proteins (GRPs) during phorbol 1 2-myristate 1 3-acetate (PMA)-induced megakaryocytic differentiation of human er"'throleukemia K562 cells. PMA-treated K562 cells showed a cell growth arrest and alteration in morphology and patterns of gpllIa and c-myc expression, characteristic of megakaryocytic differentiation. During the megakaryocytic differentiation, HSP9OA, HSP9OB, and HSP28 mRNA and protein levels markedly decreased, while GRP78/B and GRP94 mRNA levels were enhanced. On the other hand, HSP7OA and HSP7OB mRNA levels were reduced, but HSP7O protein levels were not changed by PMA treatment. These results suggest specific roles for the HSPs and GRPs in K562 cell proliferation and megakaryocic differentiation.tion.

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