• Title/Summary/Keyword: Acid shock protein

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Adoptive transfer of Porphyromonas gingivalis heat shock protein epitope-specific T-cell lines into SCID mice in experimental atherosclerosis (실험적 동맥경화증에서 Porphyromonas gingivalis 열충격단백-항원결정부위-특이성 T-세포주의 SCID mice내로의 주입효과에 대한 연구)

  • Choi, Jeom-Il;Witztum, Joseph
    • Journal of Periodontal and Implant Science
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    • v.35 no.1
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    • pp.1-8
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    • 2005
  • Bacterial heat shock protein has been one of the components that are responsible to induce autoimmune disease mechanisms in the pathogenesis of atherosclerosis due to high level of homology in sequence with human counterpart. This mechanism may explain how bacterial infectious disease, such as periodontal disease, might contribute to the acceleration of the disease process of atherosclerosis. Porphyromonas gingivalis which is a major periodontal pathogenic bacterial species, has been implicated as one of the pathogenic bacteria playing the role in this context. The present study has been performed to evaluate the anti-atherosclerotic effect of adoptive transfer of Porphyromonas gingivalis heat shock protein epitope-specific T cell lines into severe combined immunodeficiency (SCID) mice. Peptide no. 15 with amino acid sequence VKEVASKTND-specific T cell line was selected for the transfer. When experimental atherosclerosis was induced in SCID mice adoptively transferred either by the T cell lines (experimental group) or by non-specific mouse T cells (control group), there was no significant difference in the severity and extent of the atherosclerosis induced by hypercholesterol diet.

Expression of a Heat Shock Protein 70 (Hsp70) in Red Seabream Pagrus major Infected with Longicollum pagrosomi (구두충(Longicollum pagrosomi)에 감염된 참돔(Pagrus major)의 Heat Shock Protein 70 (Hsp70) 발현)

  • Park, Hyung-Jun;Min, Byung-Hwa
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.51 no.2
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    • pp.163-169
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    • 2018
  • This study examined the expression of heat shock protein 70 (Hsp70) in red seabream Pagrus major infected by the, acanthocephalan parasites Longicollum pagrosomi. We cloned the full-length Hsp70 cDNA from the liver of the red seabream. The full-length cDNA had a 1,950 bp open reading frame (ORF) that encoded a protein of 650 amino acids. The deduced amino acid sequence of Hsp70 contained all of the conserved Hsp70 family signature sequences and an adenosine triphosphate (ATP)/guanosine triphosphate (GTP) binding motif, including the EEVD (consensus sequence that terminates in Hsp70 family) consensus sequence. The expression of Hsp70 mRNA was upregulated int the fish head-kidney and liver, as determined by quantitative real-time PCR. We quantified the Hsp70 mRNA expression in normal red seabream and fish infected fish by L. pagrosomi. The expression of Hsp70 mRNA was significantly higher in the infected red seabream. These results suggest that Hsp70 play a role of protection against stress and inflammation caused by the parasite and may help maintain homeostasis.

Comparative study on Hsp25 expression in Mongolian gerbil and mouse cerebellum

  • Lee, Heang-Yeon;Kim, Seong-Hwan;Lee, Jae-Bong;Shin, Chang-Ho
    • Korean Journal of Veterinary Service
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    • v.29 no.4
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    • pp.469-482
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    • 2006
  • The term 'heat shock protein (Hsps)' was derived from the fact that these proteins were initially discovered to be induced by hyperthermic conditions. In response to a range of stressful stimuli, including hyperthermia, immobilization, UV radiation, amino acid analogues, arsenite, various chemicals, and drugs the mammalian brain demonstrates a rapid and intense induction of the heat shock protein. Moreover, Hsps were expressed on the various pathological conditions including trauma, focal or global ischemia, hypoxia, infarction, infections, starvation, and anoxia. Especially, Hsp25 has a protective activity, facilitated by the ability of the protein to decrease the intracellular levels of reactive oxygen species (ROS) as well as its chaperone activity, which favors the degradation of oxidized proteins. Recently, it has clearly demonstrated that Hsp25 is constitutively expressed in the adult mouse cerebellum by parasagittal bands of purkinje cells in three distinct regions, the central zone (lobule VI-VII) and nodular zone (lobule IX-X), and paraflocculus. The Mongolian gerbil has been introduced into stroke study model because of its unique brain vasculature. There are no significant connections between the basilarvertebral system and the carotid system. This anatomy feature renders the mongolian gerbil susceptible to forebrain ischemia-induced seizure. The present study is designed to examine the pattern of Hsp25 expression in the cerebellum of this animal in comparison with that in mouse.

Differential Display Detection of Acid-inducible Genes from Porphyra yezoensis Thalli (해조류 방사무늬김 (Porphra yezoensis) 엽체로부터 산 유도 유전자의 분리)

  • JIN Long-Guo;KANG Se-Eun;CHOI Jae-Suk;PARK Sun-Mee;PARK Jung-Youn;JIN Duck-Hee;HONG Yong-Ki
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.37 no.4
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    • pp.269-274
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    • 2004
  • Genetic responses of the edible seaweed Porphyra yezoensis tissue to acid shock have been compared using differential display technique. The tissue was challenged in seawater containing $0.05{\%}$ hydrogen chloride (pH 3.0) for 5 min, then rehabilitated in normal seawater for 10 min, 30 min, 60 min and 4 hrs. Total RNA extracted by the LiCl-guanidium method was reverse transcribed and amplified by PCR with arbitrary primers. The amplified fragment responded by the acid shock was selectively isolated from agarose gel and sequenced with DNA auto sequencer. Sequence (1056 bp) of the cDNA contained at least two genes for ASP7K (MW 7418) and ASP5K (MW 5512) proteins.

Expression of the Heat Shock Proteins in HeLa and Fish CHSE-214 Cells Exposed to Heat Shock (어류 CHSE-214와 인간 HeLa 세포에서의 열충격에 의한 Heat Shock Protein의 발현)

  • 공회정;강호성김한도
    • The Korean Journal of Zoology
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    • v.39 no.2
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    • pp.123-131
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    • 1996
  • In this study, we examined the expression of heat shock proteins (HSPs) in fish cell line CHSE-2lnl and human HeLa cells exposed to heat shock. In fish CHSE-214 cells HSP70 was the major polvpeptide induced by an elevated temperature or an amino acid analog, while in HeLa cells HSP90 as well as HSP70 were prominently enhanced in response to these stresses. Pretreatment of actinomvcin D prior to heat shock completely inhibited the induction of fish HSP70, indicating the transcriptional regulation of fish HSP70 gene expression. In HeLa and CHSE-214 cells either recovering from heat shock or experiencing prolonged heat shock, attenuation in the HSP90 a'nd HSP70 induction occurred but both induction and repression of HSP70 synthesis appear 19 precede those of HSP90. Moreover, attenuation did not occur in the syntheses of 40 kDa and 42 kOto proteins which were only induced in CHSE-214 cells. The enhanced syntheses of these he proteins continued as long as CHSE-214 cells were Siven heat shock. These results suggest that down-regulation of HSP syntheses during prolonged heat shock may be controlled by several different. as vet undefined, mechanisms.

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Salicylic Acid and Wounding Induce Defense-Related Proteins in Chinese Cabbage

  • Kim, Hong-Nam;Cha, Jae-Soon;Cho, Tae-Ju;Kim, Hak-Yong
    • Animal cells and systems
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    • v.7 no.3
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    • pp.213-219
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    • 2003
  • The response of plants to pathogens and wounding is dependent upon very sensitive perception mechanisms. Although genetic approaches have revealed a variety of resistance genes that activate common defense responses, defense-related proteins are not well characterized in plants. Therefore, we used a proteomic approach to determine which defense-related proteins are induced by salicylic acid (SA) and wounding in Chinese cabbage. We found that SA and wounding induce pathogenesis-related protein 1a (PR1a) at both protein and mRNA levels using proteomics and Northern blot analysis, respectively. This indicates that our proteomic approach is useful for identifying defense-related proteins. We also identified several other proteins that are induced by SA or wounding. Among the seven SA-induced proteins identified, four may be defense-related, including defense-related protein, phospholipase D (PLD), resistance protein RPS2 homolog, and L-ascorbate peroxidase. Out of the six wounding-induced proteins identified, three may be defense-related: heat shock cognate protein 70 (HSC70), polygalacturonase, and peroxidase P7. The precise functions of these proteins in plant defense responses await further study. However, identification of the defense-related proteins described in this study should allow us to better understand the mechanisms and signal transduction pathways involved in defense responses in Chinese cabbage.

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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Proteomic Evaluation of Cellular Responses of Saccharomyces cerevisiae to Formic Acid Stress

  • Lee, Sung-Eun;Park, Byeoung-Soo;Yoon, Jeong-Jun
    • Mycobiology
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    • v.38 no.4
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    • pp.302-309
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    • 2010
  • Formic acid is a representative carboxylic acid that inhibits bacterial cell growth, and thus it is generally considered to constitute an obstacle to the reuse of renewable biomass. In this study, Saccharomyces cerevisiae was used to elucidate changes in protein levels in response to formic acid. Fifty-seven differentially expressed proteins in response to formic acid toxicity in S. cerevisiae were identified by 1D-PAGE and nano-liquid chromatography-tandem mass spectrometry (nano-LC-MS/MS) analyses. Among the 28 proteins increased in expression, four were involved in the MAP kinase signal transduction pathway and one in the oxidative stress-induced pathway. A dramatic increase was observed in the number of ion transporters related to maintenance of acid-base balance. Regarding the 29 proteins decreased in expression, they were found to participate in transcription during cell division. Heat shock protein 70, glutathione reductase, and cytochrome c oxidase were measured by LC-MS/MS analysis. Taken together, the inhibitory action of formic acid on S. cerevisiae cells might disrupt the acidbase balance across the cell membrane and generate oxidative stress, leading to repressed cell division and death. S. cerevisiae also induced expression of ion transporters, which may be required to maintain the acid-base balance when yeast cells are exposed to high concentrations of formic acid in growth medium.

Contribution of HSP90 Cleavage to the Cytotoxic Effect of Suberoylanilide Hydroxamic Acid In Vivo and the Involvement of TXNIP in HSP90 Cleavage

  • Sangkyu Park;Dongbum Kim;Haiyoung Jung;In Pyo Choi;Hyung-Joo Kwon;Younghee Lee
    • Biomolecules & Therapeutics
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    • v.32 no.1
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    • pp.115-122
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    • 2024
  • Heat shock protein (HSP) 90 is expressed in most living organisms, and several client proteins of HSP90 are necessary for cancer cell survival and growth. Previously, we found that HSP90 was cleaved by histone deacetylase (HDAC) inhibitors and proteasome inhibitors, and the cleavage of HSP90 contributes to their cytotoxicity in K562 leukemia cells. In this study, we first established mouse xenograft models with K562 cells expressing the wild-type or cleavage-resistant mutant HSP90β and found that the suppression of tumor growth by the HDAC inhibitor suberoylanilide hydroxamic acid (SAHA) was interrupted by the mutation inhibiting the HSP90 cleavage in vivo. Next, we investigated the possible function of thioredoxin interacting protein (TXNIP) in the HSP90 cleavage induced by SAHA. TXNIP is a negative regulator for thioredoxin, an antioxidant protein. SAHA transcriptionally induced the expression of TXNIP in K562 cells. HSP90 cleavage was induced by SAHA also in the thymocytes of normal mice and suppressed by an anti-oxidant and pan-caspase inhibitor. When the thymocytes from the TXNIP knockout mice and their wild-type littermate control mice were treated with SAHA, the HSP90 cleavage was detected in the thymocytes of the littermate controls but suppressed in those of the TXNIP knockout mice suggesting the requirement of TXNIP for HSP90 cleavage. We additionally found that HSP90 cleavage was induced by actinomycin D, β-mercaptoethanol, and p38 MAPK inhibitor PD169316 suggesting its prevalence. Taken together, we suggest that HSP90 cleavage occurs also in vivo and contributes to the anti-cancer activity of various drugs in a TXNIP-dependent manner.

Differentiation and upregulation of heat shock protein 70 induced by a subset of histone deacetylase inhibitors in mouse and human embryonic stem cells

  • Park, Jeong-A;Kim, Young-Eun;Seok, Hyun-Jeong;Park, Woo-Youn;Kwon, Hyung-Joo;Lee, Young-Hee
    • BMB Reports
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    • v.44 no.3
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    • pp.176-181
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    • 2011
  • Inhibiting histone deacetylase (HDAC) activity modulates the epigenetic status of cells, resulting in an alteration of gene expression and cellular function. Here, we investigated the effects of HDAC inhibitors on mouse embryonic stem (ES) cells. The HDAC inhibitors trichostatin A, suberoylanilide hydroxamic acid, sodium butyrate, and valproic acid induced early differentiation of mouse ES cells and triggered induction of heat-shock protein (HSP)70. In contrast, class III HDAC inhibitors failed to induce differentiation or HSP70 expression. Transcriptional upregulation of HSP70 was confirmed by mRNA expression analysis, an inhibitor study, and chromatin immunoprecipitation. HSP70 induction was dependent on the SAPK/JNK, p38, and PI3K/Akt pathways. Differentiation and induction of HSP70 by a subset of HDAC inhibitors was also examined in human ES cells, which suggests that the phenomenon generally occurs in ES cells. A better understanding of the effects of HDAC inhibitors may give more insight into their application in stem cell biology.