Curcumin inhibits phorbol ester-induced expression of cyclooxygenase-2 in mouse skin through suppression of extracellular signal-regulated kinase activity and NF- B activation

Chun, Kyung Soo; Keum, Young‐Soo; Han, Seong‐Su; Song, Yong Sang; Kim, Su Hyeong; Surh, Young Joon

doi:10.1093/carcin/bgg107

Cited by 282 publications

(236 citation statements)

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“…Curcumin was found to suppress COX-2 expression by inhibiting extracellular signal-regulated kinase (ERK) activity and NF-κB in phorbol ester-induced mouse skin tumorigenesis [26]. Curcumin has also been shown to induce growth arrest and apoptosis in various cancer cell lines [67,80,154,169].…”

Section: Pre-clinical and Clinical Trials Of Nf-κb Inhibitorsmentioning

confidence: 99%

NF‐κB as a potential molecular target for cancer therapy

et al. 2007

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Abstract. Nuclear factor κB (NF-κB), a transcription factor, plays an important role in carcinogenesis as well as in the regulation of immune and inflammatory responses. NF-κB induces the expression of diverse target genes that promote cell proliferation, regulate apoptosis, facilitate angiogenesis and stimulate invasion and metastasis. Furthermore, many cancer cells show aberrant or constitutive NF-κB activation which mediates resistance to chemo-and radio-therapy. Therefore, the inhibition of NF-κB activation and its signaling pathway offers a potential cancer therapy strategy. In addition, recent studies have shown that NF-κB can also play a tumor suppressor role in certain settings. In this review, we focus on the role of NF-κB in carcinogenesis and the therapeutic potential of targeting NF-κB in cancer therapy.Keywords: NF-κB, NF-κB inhibitor, carcinogenesis, cancer therapy Structure, function and regulation of NF-κBNuclear factor-κB (NF-κB) was first identified in 1986 as a transcription factor that binds to a 10 bp DNA element in kappa immunoglobulin light-chain enhancer in B cells [128]. The mammalian NF-κB family consists of 5 members: NF-κB1 (p50/p105), NF-κB2 (p52/p100), c-Rel, RelA (p65) and RelB (Fig. 1). RelA, c-Rel and RelB are synthesized in their mature forms and contain a transactivation domain that interacts with the transcriptional apparatus. On the other hand, NF-κB1 (p50/p105) and NF-κB2 (p52/p100) are synthesized in precursor forms (p100 and p105) which contain C-terminal ankyrin repeats that are proteolysed by the proteasome resulting in the production of mature proteins (p50 and p52). Both p50 and p52 contain a DNA binding domain but lack a transactivation domain. NF-κB proteins exist in unstimulated cells as homo-or heterodimers bound to IκB proteins. Whereas RelB forms only heterodimers, all the other proteins can form both homo-and heterodimers. NF-κB proteins are characterized by the presence of a highly conserved 300 amino acid Rel homology domain that is located toward the N terminus of the protein, and which is responsible for DNA binding, dimerization, and interaction with specific inhibitory factors known as IκB proteins [7,36].

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Section: Pre-clinical and Clinical Trials Of Nf-κb Inhibitorsmentioning

confidence: 99%

NF‐κB as a potential molecular target for cancer therapy

et al. 2007

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“…7,21 Equal amounts of protein extracts in RIPA lysis buffer [150 mM NaCl, 0.5% Triton X-100, 50 mM Tris-HCl (pH 7.4), 25 mM NaF, 20 mM EGTA, 1 mM DTT, 1 mM Na 3 VO 4 , and a protease-inhibitor-cocktail tablet] were subjected to 12% SDS-PAGE and electrophoretically transferred to nitrocellulose membrane. Protein bands were detected using an enhanced chemiluminescence detection kit.…”

Section: Immunoblot Analysismentioning

confidence: 99%

Section: Electrophoretic Mobility Shift Assaymentioning

confidence: 99%

“…21 An electrophoretic mobility shift assay (EMSA) was performed using a DNA-protein-binding detection kit (GIBCO BRL) for NFjB binding according to the Manufacturer's protocol as described previously. 21 Briefly, the NF-jB oligonucleotide probe (5 0 -AGT TGA GGG GAC TTT CCC AGG C-3 0 ) was labeled with [a-32 P]ATP by T4 polynucleotide kinase and purified on a Nick column. The binding reaction was performed in 25 ll of the mixture containing 5 ll of incubation buffer [10 mM Tris-HCl (pH 7.5), 100 mM NaCl, 1 mM DTT, 1 mM EDTA, 4% (v/v) glycerol and 0.1 mg/ml sonicated salmon sperm DNA], 10 lg of nuclear extracts and the labeled probe at 100,000 cpm.…”

Section: Electrophoretic Mobility Shift Assaymentioning

confidence: 99%

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H‐Ras selectively up‐regulates MMP‐9 and COX‐2 through activation of ERK1/2 and NF‐κB: An implication for invasive phenotype in rat liver epithelial cells

Lee

Kim

Kang

et al. 2006

Intl Journal of Cancer

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One of the most frequent events in carcinogenesis is uncontrolled activation of Ras signaling pathway. A previous study demonstrated that the introduction of H-Ras into the normal WB-F344 rat liver epithelial (WB) cell line and adult male F344 rats resulted in tumorigenicity. The present study investigated whether H-Ras induced the invasive and migrative phenotypes in WB cells, and subsequently aimed at characterizing the underlying mechanisms. H-Ras induced the invasive and migrative phenotypes of WB cells with a selective up-regulation of matrix metalloproteinase (MMP)-9, but not MMP-2. Cyclooxygenase (COX)-2 and the subsequent production of prostaglandin E 2 (PGE 2 ) were also induced by H-Ras. Treatment of H-Ras WB cells with GM6001 and NS398, the inhibitors of MMPs and COX-2, respectively, significantly inhibited the H-Ras-induced invasive and migrative phenotypes. DNA binding activity of nuclear factor (NF)-jB, but not that of activator protein (AP)-1, was increased by H-Ras. Caffeic acid phenethyl ester and Bay 11-7082, specific inhibitors of NF-jB and IKK, respectively, significantly inhibited the expression of MMP-9 and COX-2, invasion and migration of H-Ras WB cells, revealing NF-jB as a transcriptional factor responsible for HRas-induced malignant phenotypic conversion of WB cells. Activation of ERKs pathway was critical for H-Ras-induced invasive and migrative phenotypes, up-regulation of MMP-9 and COX-2 as well as enhanced DNA binding activity of NF-jB in WB cells. Taken together, these results demonstrate that H-Ras up-regulates MMP-9 and COX-2 through activation of ERKs and IKK-IjBa-NF-jB signal pathway which may contribute to the malignant progression of WB rat liver epithelial cells. ' 2006 Wiley-Liss, Inc.

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“…Recently, it has been reported that curcumin-treated cells show the decreased expressions of COX-2 in various cell lines by inhibition of MAPKs signaling pathways (Chun et al, 2003;Hong et al, 2004;Kang et al, 2004). Currently, it is unknown whether curcumin modulates the expression of COX-2 in UVB-irradiated HaCaT cells.…”

Section: Introductionmentioning

confidence: 99%