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• W2012094853 startingPage "e0116410" @default.
• W2012094853 abstract "Reactive oxygen species (ROS) primarily produced via NADPH oxidase play an important role for killing microorganisms in neutrophils. In this study we examined if ROS production in Human promyelocytic leukemia cells (HL60) differentiated into neutrophil-like cells (dHL60) induces ER stress and activates the unfolded protein response (UPR). To cause ROS production cells were treated with PMA or by chronic hyperglycemia. Chronic hyperglycemia failed to induce ROS production and did not cause activation of the UPR in dHL60 cells. PMA, a pharmacologic NADPH oxidase activator, induced ER stress in dHL60 cells as monitored by IRE-1 and PERK pathway activation, and this was independent of calcium signaling. The NADPH oxidase inhibitor, DPI, abolished both ROS production and UPR activation. These results show that ROS produced by NADPH oxidase induces ER stress and suggests a close association between the redox state of the cell and the activation of the UPR in neutrophil-like HL60 cells." @default.
• W2012094853 created "2016-06-24" @default.
• W2012094853 creator A5004080311 @default.
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• W2012094853 creator A5034694073 @default.
• W2012094853 creator A5072487969 @default.
• W2012094853 date "2015-02-10" @default.
• W2012094853 modified "2023-10-16" @default.
• W2012094853 title "NADPH Oxidase-Dependent Production of Reactive Oxygen Species Induces Endoplasmatic Reticulum Stress in Neutrophil-Like HL60 Cells" @default.
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• W2012094853 doi "https://doi.org/10.1371/journal.pone.0116410" @default.
• W2012094853 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4323339" @default.
• W2012094853 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25668518" @default.
• W2012094853 hasPublicationYear "2015" @default.
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