Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 277, Issue 9, Pages 6838-6845Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M106908200
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Funding
- NCI NIH HHS [CA 25917] Funding Source: Medline
- NIDDK NIH HHS [T32 DK 07115, DK 55491] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R37CA025917, R01CA025917] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [T32DK007115, R01DK055491] Funding Source: NIH RePORTER
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Peroxisome proliferator-activated receptors (PPARs) are transcription factors that belong to the nuclear hormone receptor superfamily. PPARalpha and PPARgamma ligands have been demonstrated to exert anti-inflammatory activities in macrophages by repressing the activities of several transcription factors. PPARgamma is expressed in T lymphocytes and may play a role in cytokine production, cellular proliferation, and susceptibility to apoptosis. Herein, we demonstrate that T and B lymphocytes constitutively express PPARalpha. PPARalpha represents the predominant isoform expressed in lymphocytes, whereas PPARgamma dominates in all cell types of the myeloid lineage. PPARalpha expression was down-regulated following T-cell activation while PPARgamma expression increased under the same activating conditions. PPARalpha expression in T cells may be regulated by microenvironmental factors, because Peyer's patch T cells expressed far greater levels of PPARalpha than T cells isolated from peripheral lymphoid organs. Exposure to specific ligand determined that PPARalpha in lymphocytes can effectively transactivate a peroxisome proliferator response element reporter construct. PPARalpha's ability to regulate endogenous genes, however, required treatment with histone deacetylase inhibitors. Finally, ligand activation of lymphocyte PPARalpha antagonized NF-kappaB. Our observation that a functional PPARalpha exists within T cells and B lymphocytes suggests an expanding role for this nuclear receptor in cells of the immune system.
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