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• W1973019265 abstract "Heme oxygenase-1 (HO-1) is a key cytoprotective enzyme and an established marker of oxidative stress. Increased HO-1 expression has been found in the resident macrophages in the alveolar spaces of smokers. The lipid peroxidation product 4-hydroxynonenal (HNE) is also increased in the bronchial and alveolar epithelium in response to cigarette smoke. This suggests a link between a chronic environmental stress, HNE formation, and HO-1 induction. HNE is both an agent of oxidative stress in vivo and a potent cell signaling molecule. We hypothesize that HNE acts as an endogenously produced pulmonary signaling molecule that elicits an adaptive response culminating in the induction of HO-1. Here we demonstrate that HNE increases HO-1 mRNA, protein, and activity in pulmonary epithelial cells and identify ERK as a key pathway involved. Treatment with HNE increased ERK phosphorylation, c-Fos protein, JNK phosphorylation, c-Jun phosphorylation, and AP-1 binding. Whereas inhibiting the ERK pathway with the MEK inhibitor PD98059 significantly decreased HNE-mediated ERK phosphorylation, c-Fos protein induction, AP-1 binding, and HO-1 protein induction, inhibition of the ERK pathway had no effect on HNE-induced HO-1 mRNA. This suggests that ERK is involved in the increase in HO-1 through regulation of translation rather than transcription." @default.
• W1973019265 created "2016-06-24" @default.
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• W1973019265 date "2005-08-01" @default.
• W1973019265 modified "2023-10-15" @default.
• W1973019265 title "HNE increases HO-1 through activation of the ERK pathway in pulmonary epithelial cells" @default.
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• W1973019265 doi "https://doi.org/10.1016/j.freeradbiomed.2005.03.026" @default.
• W1973019265 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2798573" @default.
• W1973019265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15993334" @default.
• W1973019265 hasPublicationYear "2005" @default.
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