HUVEC cells were transiently transfected with 6X DBE-luciferase and pRL-TK plasmids for 24 h 69

After transfection, HUVEC cells were pretreated with AKT inhibitor IV (1 μM) and/or MEK1/2 inhibitor PD98059 (10 μM) for 2 h, followed by treatment with or without EGCG (40 μM) for 24 h. Cells were harvested for firefly/Renilla luciferase assays using the Dual-Luciferase Reporter Assay System (Promega). Luciferase counts were normalized using luciferase transfection control. Data represent the mean ± S.D. *, #, ** = significantly different from respective controls, P < 0.05.<p><b>Copyright information:</b></p><p>Taken from "Inhibition of PI3K/AKT and MEK/ERK pathways act synergistically to enhance antiangiogenic effects of EGCG through activation of FOXO transcription factor"</p><p>http://www.jmolecularsignaling.com/content/3/1/7</p><p>Journal of Molecular Signaling 2008;3():7-7.</p><p>Published online 20 Mar 2008</p><p>PMCID:PMC2278143.</p><p></p

HUVEC cells were transiently transfected with empty vector or constructs encoding FOXO1-TM, FOXO3a-TM, or FOXO4-TM together with 6X DBE-luciferase and pRL-TK plasmids for 24 h 69

Luciferase counts were normalized using luciferase transfection control. After transfection, cells were washed, treated with EGCG (20 μM) for 24 h, and harvested for firefly/Renilla luciferase assays using the Dual-Luciferase Reporter Assay System (Promega). Data represent the mean ± S.D. *, #, ** = significantly different from respective controls, P < 0.05.<p><b>Copyright information:</b></p><p>Taken from "Inhibition of PI3K/AKT and MEK/ERK pathways act synergistically to enhance antiangiogenic effects of EGCG through activation of FOXO transcription factor"</p><p>http://www.jmolecularsignaling.com/content/3/1/7</p><p>Journal of Molecular Signaling 2008;3():7-7.</p><p>Published online 20 Mar 2008</p><p>PMCID:PMC2278143.</p><p></p

Human umbilical vein endothelial cells (HUVECs) were pretreated with AKT inhibitor-IV (1 μM) or MEK1/2 inhibitor PD98059 (10 μM) for 4 h, followed by treatment with EGCG (40 μM) for 2 h

Cells were harvested and TUNEL assay was performed as per manufacturer's instructions (Promega). Data represent mean ± SD. * = significantly different from control, P < 0.05.<p><b>Copyright information:</b></p><p>Taken from "Inhibition of PI3K/AKT and MEK/ERK pathways act synergistically to enhance antiangiogenic effects of EGCG through activation of FOXO transcription factor"</p><p>http://www.jmolecularsignaling.com/content/3/1/7</p><p>Journal of Molecular Signaling 2008;3():7-7.</p><p>Published online 20 Mar 2008</p><p>PMCID:PMC2278143.</p><p></p

Immunohistochemical examination of Bcl-2 family members and death receptors

<p><b>Copyright information:</b></p><p>Taken from "Curcumin sensitizes TRAIL-resistant xenografts: molecular mechanisms of apoptosis, metastasis and angiogenesis"</p><p>http://www.molecular-cancer.com/content/7/1/16</p><p>Molecular Cancer 2008;7():16-16.</p><p>Published online 29 Jan 2008</p><p>PMCID:PMC2249593.</p><p></p> Immunohistochemistry was performed to measure the expression of Bak, Bax, Bcl-2, Bcl-X, TRAIL-R1/DR4 and TRAIL-R2/DR5 in tumor tissues derived from control and/or treated mice on week 6

Effects of curcumin and/TRAIL on markers of phospho-p65NFκB, Cox-2, and IL-8

<p><b>Copyright information:</b></p><p>Taken from "Curcumin sensitizes TRAIL-resistant xenografts: molecular mechanisms of apoptosis, metastasis and angiogenesis"</p><p>http://www.molecular-cancer.com/content/7/1/16</p><p>Molecular Cancer 2008;7():16-16.</p><p>Published online 29 Jan 2008</p><p>PMCID:PMC2249593.</p><p></p> (A), Immunohistochemistry was performed to measure the expression of phospho-p65NFκB, Cox-2 and IL-8 in tumor tissues derived from control and/or treated mice on week 6. (B), Expression of phospho-p65NFκB, Cox-2, IL-8 and β-actin in tumor tissues derived on week 6 were measured by the Western blot analysis. (C), NFκB-DNA binding activity. Nuclear extracts were prepared from tumor tissues derived from different treatment groups on week 6. NFκB-DNA binding activity was measured by Gelshift assay as described in Materials and Methods. The relative nuclear NFκB-DNA binding activities were quantified by scanning densitometry

Curcumin enhances the apoptosis-inducing potential of TRAIL in prostate cancer cells: molecular mechanisms of apoptosis, migration and angiogenesis-2

<p><b>Copyright information:</b></p><p>Taken from "Curcumin enhances the apoptosis-inducing potential of TRAIL in prostate cancer cells: molecular mechanisms of apoptosis, migration and angiogenesis"</p><p>http://www.jmolecularsignaling.com/content/2/1/10</p><p>Journal of Molecular Signaling 2007;2():10-10.</p><p>Published online 4 Oct 2007</p><p>PMCID:PMC2082014.</p><p></p>alysis

Curcumin enhances the apoptosis-inducing potential of TRAIL in prostate cancer cells: molecular mechanisms of apoptosis, migration and angiogenesis-5

<p><b>Copyright information:</b></p><p>Taken from "Curcumin enhances the apoptosis-inducing potential of TRAIL in prostate cancer cells: molecular mechanisms of apoptosis, migration and angiogenesis"</p><p>http://www.jmolecularsignaling.com/content/2/1/10</p><p>Journal of Molecular Signaling 2007;2():10-10.</p><p>Published online 4 Oct 2007</p><p>PMCID:PMC2082014.</p><p></p> fluorometric assay as per manufacturer's instructions. (C and D), PC-3 and LNCaP cells were treated with curcumin (0–40 μM), in the presence or absence of TRAIL, and caspase-8 activity was measured by fluorometric assay as per manufacturer's instructions. (E and F), PC-3 and LNCaP cells were treated with curcumin (0, 10 or 20 μM), in the presence or absence of TRAIL (25 nM for PC-3, and 50 nM for LNCaP), and the cleavage of caspase-3, caspase-9, caspase-8 and PARP was measured by the Western blot analysis. β-actin was used as a loading control

Interactive effects of resveratrol and TRAIL on caspase activation and PARP cleavage

<p><b>Copyright information:</b></p><p>Taken from "Sensitization of TRAIL-resistant LNCaP cells by resveratrol (3, 4', 5 tri-hydroxystilbene): molecular mechanisms and therapeutic potential"</p><p>http://www.jmolecularsignaling.com/content/2/1/7</p><p>Journal of Molecular Signaling 2007;2():7-7.</p><p>Published online 24 Aug 2007</p><p>PMCID:PMC2018690.</p><p></p> (A), Effects of resveratrol and/or TRAIL on caspase-3 activity in LNCaP cells. Cells were treated with resveratrol (0–30 μM) in the presence or absence of TRAIL (50 nM) for 24 h. At the end of incubation period, caspase-3 activity was measured by flurometric assay. (B), Effects of resveratrol and/or TRAIL on caspase-8 activity. LNCaP cells were treated with resveratrol (0–30 μM) in the presence or absence of TRAIL (50 nM) for 24 h. At the end of incubation period, caspase-8 activity was measured by flurometric assay. (C), Effects of resveratrol and/or TRAIL on cleavage of pro-caspase-8, pro-caspase-3, pro-caspase-9 and PARP. LNCaP cells were pretreated with resveratrol (0, 10 or 20 μM) for 24 h followed by treatment with or without TRAIL (50 nM) for 24 h. At the end of incubation period, cells were harvested, and the Western blot analysis was performed to measure the expression of pro-caspase-8, cleaved-caspase-3, cleaved-caspase-9 and PARP. β-actin was used as a loading control

Curcumin enhances the apoptosis-inducing potential of TRAIL in prostate cancer cells: molecular mechanisms of apoptosis, migration and angiogenesis-0

<p><b>Copyright information:</b></p><p>Taken from "Curcumin enhances the apoptosis-inducing potential of TRAIL in prostate cancer cells: molecular mechanisms of apoptosis, migration and angiogenesis"</p><p>http://www.jmolecularsignaling.com/content/2/1/10</p><p>Journal of Molecular Signaling 2007;2():10-10.</p><p>Published online 4 Oct 2007</p><p>PMCID:PMC2082014.</p><p></p>h. Cell viability was measured at the end of 48 h by XTT assay. (B), LNCaP cells were treated with various concentrations of curcumin (0–30 μM) for 24 h, followed by treatment with TRAIL (50 nM) for another 24 h. Cell viability was measured at the end of 48 h by XTT assay. (C), PC-3 cells were seeded in soft agar and treated with curcumin (5–40 μM) in the presence or absence of TRAIL (25 nM). After three weeks, no of colonies were counted. Data represent mean ± SE. (D), LNCaP cells were seeded in soft agar and treated with curcumin (5–40 μM) in the presence or absence of TRAIL (50 nM). After three weeks, no of colonies were counted. Data represent mean ± SE. (E and F), Effects of dominant negative FADD on curcumin and/or TRAIL-induced apoptosis. PC-3 and LNCaP cells were transiently transfected with either control plasmid or plasmid expressing dominant negative FADD (DN-FADD) along with plasmid (pCMV-LacZ) encoding the β-galactosidase (β-Gal) enzyme. There was no difference in transfection efficiency among groups. Transfected cells were treated with curcumin (0, 10 or 20 μM) in the presence or absence of TRAIL (25 nM for PC-3 cells or 50 nM for LNCaP) for 48 h. Apoptosis was measured by DAPI staining. Data represent mean ± SE. * = significantly different from respective control; # and % = treatment groups were significantly different, P < 0.05

Effects of resveratrol and/or TRAIL on mitochondrial membrane potential (Δψ)

<p><b>Copyright information:</b></p><p>Taken from "Sensitization of TRAIL-resistant LNCaP cells by resveratrol (3, 4', 5 tri-hydroxystilbene): molecular mechanisms and therapeutic potential"</p><p>http://www.jmolecularsignaling.com/content/2/1/7</p><p>Journal of Molecular Signaling 2007;2():7-7.</p><p>Published online 24 Aug 2007</p><p>PMCID:PMC2018690.</p><p></p> (A), Resveratrol induces drop in Δψ. LNCaP cells were treated with or without resveratrol (20 μM) for 0–24 h. Cells were stained with JC1 dye, and Δψwas measured by a fluorometer as per manufacturer's instructions. (B), Interactive effects of resveratrol and TRAIL on Δψ. LNCaP cells were treated with resveratrol (20 μM) in the presence or absence of TRAIL (50 nM) for 1, 2, 8 and 16 h. Cells were stained with JC1 dye, and Δψwas measured