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Biochim Biophys Acta. 1998 Jun 15;1392(2-3):185-92.

Intestinal NF-kappaB is activated, mainly as p50 homodimers, by platelet-activating factor.

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Department of Pediatrics (Neonatology), Children's Memorial Hospital, Northwestern University Medical School, 2300 Children's Plaza, Chicago, IL 60614, USA.


NF-kappaB, a transcription factor, upregulates gene transcription of many inflammatory mediators. Here, we examined the activity of NF-kappaB in the rat small intestine, and how it may be affected by platelet-activating factor (PAF), an important mediator for intestinal injury and inflammation. Ileal nuclear extracts from sham-operated and PAF (1.5 microg/kg)-injected rats were prepared for the assessment of NF-kappaB DNA-binding activity, and the identification of NF-kappaB subunits. The experiment was also performed on neutrophil-depleted rats to examine whether the PAF effect is neutrophil-dependent. Cellular NF-kappaB was localized by immunohistochemistry. We found that: (a) NF-kappaB is constitutively active in rat small intestine; (b) PAF at a dose below that causing shock and bowel necrosis enhances DNA-binding activity of NF-kappaB within 30 min after injection; activated NF-kappaB contains predominantly p50 subunits; (c) immunohistochemistry showed that PAF induced translocation of p50 into the nucleus of cells of the lamina propria, as well as of the epithelium; and (d) the effect of PAF is abrogated by neutrophil depletion, suggesting a role of neutrophils in NF-kappaB activation. Our study suggests that NF-kappaB is weakly active constitutively in the intestine, and inflammatory stimuli such as PAF activate NF-kappaB and enhance its DNA-binding activity in the intestine, which contains predominantly p50 subunits.

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