Okadaic acid markedly potentiates the heat-induced hsp 70 promoter activity.

Chang, Nien-Tze; Huang, Lanqing; Liu, A. Y.-C.

doi:10.1016/s0021-9258(18)54094-1

Cited by 35 publications

(1 citation statement)

References 45 publications

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“…Thus, for these studies, we employed the phosphatase inhibitors vanadate and okadaic acid. These inhibitors have been successfully used to identify critical phosphorylation events stimulated by receptor activation in normal cells in cases where the increase in phosphorylation of signaling proteins contributes to downstream events but is otherwise relatively small and transient. − Many changes in protein phosphorylation induced by Ox-PAPC are presented here for the first time. We also identify specific sites of phosphorylation in proteins known to be activated by Ox-PAPC.…”

Section: Introductionmentioning

confidence: 99%

Activation of Aortic Endothelial Cells by Oxidized Phospholipids: A Phosphoproteomic Analysis

et al. 2010

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Previous studies have shown that oxidized products of the phospholipid PAPC (Ox-PAPC) are strong activators of aortic endothelial cells and play an important role in atherosclerosis and other inflammatory diseases. We and others have demonstrated that Ox-PAPC activates specific signaling pathways and regulates a large number of genes. Using a phosphoproteomic approach based on phosphopeptide enrichment and mass spectrometry analysis, we identified candidate changes in Ox-PAPC-induced protein phosphorylation of 228 proteins. Functional annotation of these proteins showed an enrichment of the regulation of cytoskeleton, junctional components, and tyrosine kinases, all of which may contribute to the phenotypic and molecular changes observed in endothelial cells treated with Ox-PAPC. Many changes in protein phosphorylation induced by Ox-PAPC are reported here for the first time and provide new insights into the mechanism of activation by oxidized lipids, including phosphorylation-based signal transduction.

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Section: Introductionmentioning

confidence: 99%

Activation of Aortic Endothelial Cells by Oxidized Phospholipids: A Phosphoproteomic Analysis

et al. 2010

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Okadaic acid, sphingosine, and phorbol ester reversibly modulate heat induction on protein kinase F a /GSK‐3α in A431 cells

Yang¹,

Chang²,

Lee³

1996

J of Cellular Biochemistry

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Exposure of A431 cells to a rapid and sudden increase from 37 degrees C to 46 degrees C for 30 min could induce an increase in protein level and cellular activity of protein (kinase FA/GSK-3 alpha) up to approximately 200% of control level. However, when cells were first treated with 500 nM tumor promoter phorbol ester TPA at 37 degrees C for 30 min to activate cellular protein kinase C (PKC) or with 400 nM okadaic acid at 37 degrees C for 30 min to inhibit cellular protein phosphatases followed by heat shock at 46 degrees C for another 30 min, the heat induction on kinase FA/GSK-3 alpha was found to be completed blocked. In sharp contrast, when cells were first treated with 1 microM TPA at 37 degrees C for 24 h or with 5 microM sphingosine at 37 degrees C for 30 min to down-regulate cellular PKC, the heat induction on kinase FA/GSK-3 alpha was found to be reversely promoted up to approximately 250% of control level, demonstrating that kinase FA/GSK-3 alpha may not represent a constitutively active/mitogen-inactivated protein kinase as previously conceived. Taken together, the results provide initial evidence that TPA/sphingosine and okadaic acid could reversibly modulate the heat induction on kinase FA/GSK-3 alpha in A431 cells, suggesting that phosphorylation/dephosphorylation mechanisms are involved in the regulation of the heat-shock induction of kinase FA/GSK-3 alpha, representing a new mode of signal transduction for the regulation of this multisubstrate protein kinase and a new mode of signaling pathway modulating the heat-induction process.

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Modulation of protein phosphorylation and stress protein expression by okadaic acid on heat shock cells

1996

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Okadaic acid markedly potentiates the heat-induced hsp 70 promoter activity.

Cited by 35 publications

References 45 publications

Activation of Aortic Endothelial Cells by Oxidized Phospholipids: A Phosphoproteomic Analysis

Activation of Aortic Endothelial Cells by Oxidized Phospholipids: A Phosphoproteomic Analysis

Okadaic acid, sphingosine, and phorbol ester reversibly modulate heat induction on protein kinase F a /GSK‐3α in A431 cells

Modulation of protein phosphorylation and stress protein expression by okadaic acid on heat shock cells

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