TY - JOUR
T1 - 15-Deoxy-Δ12,14-prostaglandin J2 inhibits multiple steps in the NF-κB signaling pathway
AU - Straus, Daniel S.
AU - Pascual, Gabriel
AU - Li, Mei
AU - Welch, John S.
AU - Ricote, Mercedes
AU - Hsiang, Chin Hui
AU - Sengchanthalangsy, Lei Lei
AU - Ghosh, Gourisankar
AU - Glass, Christopher K.
PY - 2000/4/25
Y1 - 2000/4/25
N2 - Prostaglandin J2 (PGJ2) and its metabolites Δ12-PGJ2 and 15-deoxy-Δ12,14-PGJ2 (15d-PGJ2) are naturally occurring derivatives of prostaglandin D2 that have been suggested to exert antiinflammatory effects in vivo. 15d-PGJ2 is a high-affinity ligand for the peroxisome proliferator-activated receptor γ (PPARγ) and has been demonstrated to inhibit the induction of inflammatory response genes, including inducible NO synthase and tumor necrosis factor α, in a PPARγ-dependent manner. We report here that 15d-PGJ2 potently inhibits NK-κB-dependent transcription by two additional PPARγ-independent mechanisms. Several lines of evidence suggest that 15d-PGJ2 directly inhibits NF-κB-dependent gene expression through covalent modifications of critical cysteine residues in lκB kinase and the DNA-binding domains of NF-κB subunits. These mechanisms act in combination to inhibit transactivation of the NF-κB target gene cyclooxygenase 2. Direct inhibition of NF-κB signaling by 15d-PGJ2 may contribute to negative regulation of prostaglandin biosynthesis and inflammation, suggesting additional approaches to the development of antiinflammatory drugs.
AB - Prostaglandin J2 (PGJ2) and its metabolites Δ12-PGJ2 and 15-deoxy-Δ12,14-PGJ2 (15d-PGJ2) are naturally occurring derivatives of prostaglandin D2 that have been suggested to exert antiinflammatory effects in vivo. 15d-PGJ2 is a high-affinity ligand for the peroxisome proliferator-activated receptor γ (PPARγ) and has been demonstrated to inhibit the induction of inflammatory response genes, including inducible NO synthase and tumor necrosis factor α, in a PPARγ-dependent manner. We report here that 15d-PGJ2 potently inhibits NK-κB-dependent transcription by two additional PPARγ-independent mechanisms. Several lines of evidence suggest that 15d-PGJ2 directly inhibits NF-κB-dependent gene expression through covalent modifications of critical cysteine residues in lκB kinase and the DNA-binding domains of NF-κB subunits. These mechanisms act in combination to inhibit transactivation of the NF-κB target gene cyclooxygenase 2. Direct inhibition of NF-κB signaling by 15d-PGJ2 may contribute to negative regulation of prostaglandin biosynthesis and inflammation, suggesting additional approaches to the development of antiinflammatory drugs.
UR - http://www.scopus.com/inward/record.url?scp=0034712933&partnerID=8YFLogxK
U2 - 10.1073/pnas.97.9.4844
DO - 10.1073/pnas.97.9.4844
M3 - Article
C2 - 10781090
AN - SCOPUS:0034712933
SN - 0027-8424
VL - 97
SP - 4844
EP - 4849
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 9
ER -