ArticleBritish journal of pharmacology2001
Platelet-activating factor and endotoxin activate CCAAT/enhancer binding protein in rat small intestine.
Article in British journal of pharmacology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Exfoliated epithelial cell transcriptome reflects both small and large intestinal cell signatures in piglets.American journal of physiology. Gastrointestinal and liver physiology · 2021Article
- Regulation of platelet-activating factor-induced interleukin-8 expression by protein tyrosine phosphatase 1B.Cell communication and signaling : CCS · 2019Article
- Regulation of platelet-activating factor-mediated interleukin-6 promoter activation by the 48 kDa but not the 45 kDa isoform of protein tyrosine phosphatase non-receptor type 2.Cell & bioscience · 2019Article
- Regulation of platelet-activating factor-mediated protein tyrosine phosphatase 1B activation by a Janus kinase 2/calpain pathway.PloS one · 2017Article
- Menadione Suppresses Benzo(α)pyrene-Induced Activation of Cytochromes P450 1A: Insights into a Possible Molecular Mechanism.PloS one · 2016Article
- The p50-p50 NF-kappaB complex as a stimulus-specific repressor of gene activation.Molecular and cellular biochemistry · 2004Article
- Regulatory region variability in the human presenilin-2 (PSEN2) gene: potential contribution to the gene activity and risk for AD.Molecular psychiatry · 2002Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The transcription factor family CCAAT/enhancer binding proteins (C/EBP) is involved in inflammation via the regulation of the gene expression of various pro-inflammatory cytokines and proteins. PAF and endotoxin (lipopolysaccharide, LPS) are known agents causing intestinal inflammation and injury. In this study, we examined the binding activity of C/EBP isoforms in rat small intestine in response to PAF (1.5 microg kg(-1), i.v.) or LPS (5 mg kg(-1), i.v.). We found that C/EBP is constitutively active in normal small intestine, mainly as C/EBP-alpha and beta (C/EBP-beta>alpha). Both C/EBP-alpha and beta are localized in the intestinal epithelial cells: C/EBP-alpha mainly in the crypts, and C/EBP-beta in both villi and crypts, as well as in some lamina propria cells. Only minute amounts of C/EBP-delta were found. PAF rapidly upregulates the binding activity of C/EBP-alpha and beta within 30 min. The increase in C/EBP-alpha is prominent in the crypt cells, whereas the change of C/EBP-beta is more widespread. LPS also increases the binding activity of C/EBP-alpha and beta, and the response is slower than PAF. PAF synergizes with LPS to markedly activate all three subunits. The increase in C/EBP-alpha is transient, whereas the other two have a sustained elevation until 120 min. After challenge with PAF (but not LPS), small amounts of nuclear factor -kappaB (NF-kappaB) p50 and p65 subunits are found in the C/EBP-DNA binding complex, indicating cross-dimerization of the two transcription families. Pretreatment of rats with pyrrolidine dithiocarbamate (PDTC) suppresses LPS-, but not PAF-, induced NF-kappaB and C/EBP binding activity, and significantly increases the C/EBP-delta subunit in LPS- or PAF-induced C/EBP complex. These results suggest that PAF and LPS activate intestinal C/EBP in vivo, probably via different pathways.
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