• Title/Summary/Keyword: stress protein

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Transcript Analysis of Wheat WAS-2 Gene Family under High Temperature Stress during Ripening Period

  • Ko, Chan Seop;Kim, Jin-Baek;Hong, Min Jeong;Kim, Kyeong Hoon;Seo, Yong Weon
    • Plant Breeding and Biotechnology
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    • v.6 no.4
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    • pp.363-380
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    • 2018
  • Wheat is frequently exposed to high temperature during anthesis and ripening period, which resulted in yield loss and detrimental end-use-quality. The transcriptome analysis of wheat under high temperature stress during the early stage of the grain filling period was undertaken. Three expression patterns of differentially expressed genes (DEGs) during grain filling period were identified. The DEGs of seed storage protein and starch-branching enzyme showed continuous increases in their expressions during high temperature stress, as well as during the recovery period. The activities of the enzymes responsible for the elimination of antioxidants were significantly affected by exposure to high temperature stress. Only the WAS-2 family genes showed increased transcription levels under high temperature stress in dehulled spikelets. The relative transcription levels for sub-genome specific WAS-2 genes suggested that WAS-2 genes reacted with over-expression under high temperature stress and decreased back to normal expression during recovery. We propose the role of WAS-2 as a protective mechanism during the stage of grain development under high temperature in spikelets.

Characterization of T-DNA Insertional Mutant of Formaldehyde-Responsive Protein1 (T-DNA 삽입에 의한 Formaldehyde-Responsive Protein1 기능파괴 돌연변이체의 특성연구)

  • Seo, Jae-Hyun;Woo, Su-Young;Kim, Wook;Kwon, Mi
    • Journal of Korean Society of Forest Science
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    • v.99 no.4
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    • pp.501-507
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    • 2010
  • Formaldehyde responsive protein(FRP) 1 belongs to the family of universal stress protein(USP) and is known to respond to stress caused by fumigation of gaseous volatile organic compounds(VOCs) such as formaldehyde and toluene. However, the molecular function of this protein is not well understood at cellular and molecular level. In this study, loss of function mutant of FRP1 generated by T-DNA insertion(frp1-4) has been isolated from Arabidopsis thaliana and the function of FRP1 was characterized. The loss-of-function mutant of FRP1 appeared slight growth defects with shorter stem and rosette leaves compared to wild type. In addition, the damage caused by exogenous VOCs was more severe in frp1-4 than in control. Therefore, Arabidopsis FRP1 seems to be the protein involved not only in the growth and development of plant but also the stress resistance against toxic volatile organic compounds.

Metallothioneins and Oxidative Stress

  • Beattie, John H.;Trayhurn, Paul
    • Nutritional Sciences
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    • v.5 no.4
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    • pp.228-233
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    • 2002
  • The low molecular weight zinc-binding protein metallothionein(MT) contains 32% cysteine and has been shown to efficiently scavenge hydroxyl radicals in vitro. MT expression is induced by oxidative stress and an antioxidant role for this protein has therefore been proposed. This review mainly focuses on the evidence for this role arising from studies using genetically modified animals and cells which either over- or under-express MT. Despite some considerable disparity of results in the literature, reported studies do generally support an antioxidant role. Nevertheless, oxidant stress at non-physiological treatment levels has been the preferred experimental model and there is little information about the role of MT in physiological oxidative stress. Although it is presumed that the mechanism by which MT has an antioxidant effect involves oxidation of cysteinal thiols, it is possible that zinc release from MT is in itself an important signalling factor.

Metallothioneins and Oxidative Stress

  • Beattie, John H.;Trayhurn, Paul
    • Proceedings of the Korean Nutrition Society Conference
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    • 2002.11b
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    • pp.1171-1177
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    • 2002
  • The low molecular weight zinc-binding protein metallothionein (MT) contains 32% cysteine and has been shown to efficiently scavenge hydroxyl radicals in vitro. MT expression is induced by oxidative stress and an antioxidant role for this protein has therefore been proposed. This review mainly focuses on the evidence for this role arising from studies using genetically modified animals and cells which either over-or under-express MT. Despite some considerable disparity of results in the literature, reported studies do generally support an antioxidant role. Nevertheless, oxidant stress at non-physiological treatment levels has been the preferred experimental model and there is little information about the role of MT in physiological oxidative stress Although it is presumed that the mechanism by which MT has an antioxidant effect involves oxidation of cysteinal thiols, it is possible that zinc release from MT is in itself an important signalling factor.

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Metallothioneins and oxidative stress

  • Beattie, John H.;Trayhurn, Paul
    • Proceedings of the Korean Nutrition Society Conference
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    • 2002.11a
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    • pp.73-82
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    • 2002
  • The low molecular weight zinc-binding protein metallothionein (U) contains 32% cysteine and has been shown to efficiently scavenge hydroxyl radicals in vitro. MT expression is induced by oxidative stress and an antioxidant role for this protein has therefore been proposed. This review mainly focuses on the evidence for this role arising from studies using genetically modified animals and cells which either over- or under-express MT. Despite some considerable disparity of results in the literature, reported studies do generally support an antioxidant role. Nevertheless, oxidant stress at non-physiological treatment levels has been the preferred experimental model and there is little information about the role of MT in physiological oxidative stress. Although it is presumed that the mechanism by which MT has an antioxidant effect involves oxidation of cysteinal thiols, it is possible that zinc release from MT is in itself an important signalling factor.

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New Insights into the Role of Endoplasmic Reticulum Stress in Breast Cancer Metastasis

  • Han, Chang-chang;Wan, Fu-sheng
    • Journal of Breast Cancer
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    • v.21 no.4
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    • pp.354-362
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    • 2018
  • Cellular stress severely disrupts endoplasmic reticulum (ER) function, leading to the abnormal accumulation of unfolded or misfolded proteins in the ER and subsequent development of endoplasmic reticulum stress (ERS). To accommodate the occurrence of ERS, cells have evolved a highly conserved, selfprotecting signal transduction pathway called the unfolded protein response. Notably, ERS signaling is involved in the development of a variety of diseases and is closely related to tumor development, particularly in breast cancer. This review discusses recent research regarding associations between ERS and tumor metastasis. The information presented here will help researchers elucidate the precise mechanisms underlying ERS-mediated tumor metastasis and provide new directions for tumor therapies.

Effect of Cold Stress on Activities of Protein kinase C Subspecies in Rat Brain Regions

  • 이재란;최명언
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1994.04a
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    • pp.259-259
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    • 1994
  • Protein kinase C (PKC) participates in many cellular signal transduction. Previously we found that PKC activity of whole rat brain was altered after an exposure to cold temperature of 4 $^{\circ}C$ (Lee and Choi, Exp. Neurobiol., 2, 6, 1993). In this time PKC activity in each region of rat brain was investigated in order to know each regions is affected mostly by the stress.

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Expression of Thiol-Dependent Protector Protein from Yeast Enhances the Resistance of Escherichia coli to Menadione

  • Park, Jeen-Woo;Ahn, Soo-Mi;Kim, Eun-Ju;Lee, Soo-Min
    • BMB Reports
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    • v.29 no.6
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    • pp.513-518
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    • 1996
  • A soluble protein from Saccharomyces cerevisiae specifically provides protection against a thiolcontaining oxidation system but not against an oxidation system without thiol. This 25-kDa protein was thus named thiol-dependent protector protein (TPP). The role of TPP in the cellular defense against oxidative stress was investigated in Escherichia coli containing an expression vector with a yeast genomic DNA fragment that encodes TPP (strain YP) and a mutant in which the catalytically essential amino acid in the active site of TPP (Cys-47) has been replaced with alanine by site-directed mutagenesis (strain YPC47A). There was a distinct difference between these two strains in regard to viability, modulation of activities of superoxide dismutase and catalase, and the oxidative damage of DNA upon exposure to menadione. These results suggest that TPP may play a direct role in the cellular defense against oxidative stress by functioning as an antioxidant protein.

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