National Tsing Hua University Institutional Repository:Activation of p38 mitogen-activated protein kinase and mitochondrial Ca2+-mediated oxidative stress are essential for the enhanced expression of grp78 induced by the protein phosphatase inhibitors okadaic acid and calyculin A
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    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  Activation of p38 mitogen-activated protein kinase and mitochondrial Ca2+-mediated oxidative stress are essential for the enhanced expression of grp78 induced by the protein phosphatase inhibitors okadaic acid and calyculin A


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    题名: Activation of p38 mitogen-activated protein kinase and mitochondrial Ca2+-mediated oxidative stress are essential for the enhanced expression of grp78 induced by the protein phosphatase inhibitors okadaic acid and calyculin A
    作者: Chen KD;Lai MT;Cho JH;Chen LY;Lai YK
    教師: 黎耀基
    日期: 2000
    出版者: Wiley-Blackwell
    關聯: JOURNAL OF CELLULAR BIOCHEMISTRY,Wiley-Blackwell,Volume 76,Issue 4,2000,Pages 585-595
    关键词: GLUCOSE-REGULATED PROTEIN
    RAT-BRAIN TUMOR
    NF-KAPPA-B
    HETEROLOGOUS FUSION GENES
    摘要: We have reported that treatment with okadaic acid, a potent protein phosphatase inhibitor, has the ability to enhance the synthesis of the 78-kDa glucose-regulated protein (GRP78). This article reports our investigation of another protein phosphatase inhibitor, calyculin A, demonstrating the signaling pathways elicited by the protein phosphatase inhibitors that lead to the induction of grp78. Our data showed that the induction process is abolished by SB203580, a specific inhibitor of p38 mitogen-activated protein kinase (p38(MAPK)). Phosphorylation-activation of p38(MAPK) in the treated cells was indicated by its own phosphorylation, as shown by double Western blotting analyses and directly confirmed by the in vitro kinase assay using MAPK-activated protein kinase-2, a well-known downstream effector of p38(MAPK), as a substrate. The involvement of p38(MAPK) in this process is further substantiated by using transient transfection assays with a plasmid, pGRP78-Luc, which contains a 0.72-kbp stretch of the grp78 promoter. By exploiting the same transfection assay, we demonstrated that the up-regulation of the grp78 promoter by the protein phosphatase inhibitors is suppressed in the presence of the cytoplasmic calcium chelator bis(aminophenoxy)ethane N,N'-tetraacetic acid, the mitochondria calcium uniporter inhibitor ruthenium red as well as the antioxidants N-acetyl cysteine and pyrrolidinedithiocarbamate. Taken together, our results lead us to conclude that treatment with the protein phosphatase inhibitors would activate the signaling pathways involving p38(MAPK) and mitochondrial calcium-mediated oxidative stress and that these pathways must act in concert in order to confer the induction of grp78 by okadaic acid and calyculin A.
    URI: http://www3.interscience.wiley.com/journal/69501938/abstract?CRETRY=1&SRETRY=0
    http://eu.wiley.com/WileyCDA/Brand/id-35.html
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/49577
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