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EICC-1: First EuCheMS Inorganic Chemistry Conference
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11 - 14 April 2011 University of Manchester, UK
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The Dalton Division of the RSC is joining together with the EuCheMS Inorganic Division (EID) to host the first edition in a new European conference series in Inorganic Chemistry.
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Volume 2 | Number 2 | February 2011 | Pages 93–144
Inorganic Chemistry is a buoyant subject area with major developments being seen in all branches of the subject and common themes emerging; this timely conference arranged across parallel sessions brings all these themes together.
Themes and Plenary Speakers Supramolecular and co-ordination chemistry Paul Beer University of Oxford, UK Organometallic and catalysis Sylviane Sabo-Etienne Laboratoire de Chimie de Coordination du CNRS, Toulouse, France Reaction mechanisms Pablo Espinet University of Valladolid, Spain Inorganic materials Reshef Tenne Weizmann Institute of Science, Israel
Energy and photochemistry Leif Hammarström Uppsala University, Sweden Bioinorganic and metallic enzymes Claudio Luchinat University of Florence, Italy Main group Markku Räsänen University of Helsinki, Finland Solid state chemistry Martin Jansen Max Planck Institute for Solid State Research, Germany
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COVER ARTICLE Vincenzo Fogliano and Francisco J. Morales Estimation of dietary intake of melanoidins from coffee and bread
2042-6496(2011)2:2;1-A
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COVER ARTICLE Joshua D. Lambert et al. (−)-Epigallocatechin-3-gallate increases the expression of genes related to fat oxidation in the skeletal muscle of high fat-fed mice
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IN THIS ISSUE
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ISSN 2042-6496 CODEN FFOUAI 2(2) 93–144 (2011) Cover See Vincenzo Fogliano and Francisco J. Morales, pp. 117–123. Image reproduced by permission of Laura Gennaro from Food Funct., 2011, 2, 117.
Inside cover See Sudathip Sae-tan, Kimberly A. Grove, Mary J. Kennett and Joshua D. Lambert, pp. 111–116. Image reproduced by permission of Joshua D. Lambert from Food Funct., 2011, 2, 111.
REVIEW 101 Multistage carcinogenesis process as molecular targets in cancer chemoprevention by epicatechin-3-gallate Min-Hsiung Pan,* Yi-Siou Chiou, Yin-Jen Wang, Chi-Tang Ho and Jen-Kun Lin* ECG may block multiple stages carcinogenesis via regulating intracellular signaling transduction pathways.
PAPERS 111 ( )-Epigallocatechin-3-gallate increases the expression of genes related to fat oxidation in the skeletal muscle of high fat-fed mice Sudathip Sae-tan, Kimberly A. Grove, Mary J. Kennett and Joshua D. Lambert* ( )-Epigallocatechin-3-gallate (EGCG) enhances skeletal muscle expression of genes related to b-oxidation in high fat-fed mice.
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Food Funct., 2011, 2, 95–100 | 95
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Food & Function provides a dedicated venue for research relating to the chemical and physical properties of food components and their nutritional and health benefits in humans.
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ADVISORY BOARD Hitoshi Ashida, Kobe University, Japan Junshi Chen, Chinese Centre of Disease Control & Prevention, China E. Allen Foegeding, North Carolina State University, USA Vincenzo Fogliano, University of Napoli Federico II, Italy Mike Gidley, University of Queensland, Australia Chi-Tang Ho, Rutgers University, USA Richard Hurrell, ETH Zurich, Switzerland Peter Lillford, University of York, UK Rui Hai Liu, Cornell University, USA
Julian McClements, University of Massachusetts, USA Clare Mills, Institute of Food Research, UK John A. Milner, National Cancer Institute, National Institutes of Health, USA Brent Murray, University of Leeds, UK Patricia Oteiza, University of California at Davis, USA Augustin Scalbert, INRA, France Helmut Sies, University of Dusseldorf, Germany Leif Skibsted, University of Copenhagen, Denmark
David Stuart, The Hershey Company, USA Arthur Tatham, University of Wales Institute, Cardiff, UK Junji Terao, University of Tokushima, Japan George van Aken, NIZO Food Research, The Netherlands Erik van der Linden, TI Food & Nutrition, The Netherlands Jose Vina, University of Valencia, Spain Peter Wood, Agriculture and Agri-Food Canada, Canada
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PAPERS 117 Estimation of dietary intake of melanoidins from coffee and bread Vincenzo Fogliano and Francisco J. Morales*
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Melanoidins are widely distributed in the human diet and daily intake was calculated from its main contributors (coffee and cereals).
124 Normalization genes for quantitative RT-PCR in differentiated Caco-2 cells used for food exposure studies Robert A. M. Vreeburg,* Shanna Bastiaan-Net and Jurriaan J. Mes A set of normalization genes for Caco-2 cells is validated, and is used to detect changes in gene expression upon exposure to apple, tomato, broccoli and mushroom.
130 Function of Plectranthus barbatus herbal tea as neuronal acetylcholinesterase inhibitor Pedro L. V. Fale, Paulo J. Amorim Madeira, M. Helena Flor^encio, Lia Ascensa˜o and Maria Luısa M. Serralheiro* Herbal tea containing rosmarinic acid and other phenolic acid derivatives can reach the brain and act as low acetylcholinesterase inhibitors.
137 Interaction of dietary flavonoids with gamma-globulin: molecular property-binding affinity relationship aspect Fan Yang, Yaru Zhao, Guoyin Kai and Jianbo Xiao* The quenching effects of flavonoids on gamma-globulin fluorescence depended on the structures of the flavonoids.
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Food Funct., 2011, 2, 95–100 | 97
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MC10 2011 Downloaded on 09 February 2011 Published on 09 February 2011 on http://pubs.rsc.org | doi:10.1039/C1FO90003J
Tenth International Conference on Materials Chemistry (MC10) | 4 - 7 July 2011 | Manchester, UK
Poster and early bird deadline – 6 May 2011 The ‘MC’ conference series has provided a showcase for materials chemistry for almost two decades, and is the flagship event of the RSC’s Materials Chemistry Division. Recent editions of the MC series have been very successful: MC7, held in Edinburgh in 2005, attracted over 450 delegates; and MC8 saw 500 scientists present their work and network in central London. In 2009, the RSC was proud to incorporate MC9 into the scientific programme of the 42nd IUPAC World Congress (IUPAC 2009). Comprising 16 symposia across 5 of the congress’ 17 parallel sessions, MC9 reached an audience of over 2000 delegates. The series returns in 2011 to its traditional format as a standalone conference over four days, beginning at lunchtime on Monday 4 July and ending at lunchtime on Thursday 7 July. MC10 will appeal to academic and industrial scientists working on the chemistry, physics and materials science of functional materials.
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Food & Function
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C
Dynamic Article Links
ECG
BEAS-2B cells; 2C5 cells; HL-60 cells, A427, RTE
0.0001–1 mM
35
EGCG ¼ ECG
H2O2-treated human bladder urothelial cells UVA-induced HaCaT keratinocyte
10–40 mg ml1
36
ECG > EGCG
1–100 mM
37
ECG > EGCG
t-BOOH-treated HepG2 cells
10–25 mM
39
EGCG > ECG
Colon mucosa and tumor from human
30 mg ml1
46
ECG > EGCG
H2O2–induced Passage-2 NHNE cells
100 mM
47
ECG
IL-6-stimulated HepG2 cells TPA-treated mouse ear IL-17A-stimulated HGF cells
25 mM 1 mmol 50 mg ml1
50 49 48
EGCG > ECG EGCG > ECG EGCG > ECG
HCT-116 cells A549 cells 30.7b Ras 12 cells B[a]P-induced lung carcinogenesis
50 mM IC50 ¼ 50 mM IC50 ¼ 15 mM 4 mg
64 65 79 62
EGCG > ECG EGCG > ECG EGCG > ECG EGCG ¼ ECG
BEL-7404/DOX; CHRC5 cells; KB-C2 cells SCC7 cells
50–100 mM
80–82
EGCG > ECG
50 mM
63
ECG > EGCG
A172 glioblastoma cells
50 mM
76
ECG S EGCG
MCF-7, C57BL/6 mice
1 mM
75
ECG S EGCG
Rat liver and rat-1A cells chicken liver FAS
IC50 ¼ 12 mM IC50 ¼ 42 mM
66 67,68
EGCG > ECG ECG > EGCG
NCI-H460 cells HSC-2 cells
125 mM
87 103
ECG > EGCG
HCT-116 cells
50 mM
100
EGCG ¼ ECG
HCT-116 cells
50 mM
93
ECG > EGCG
DU145 cells
100 mM
102
ECG > EGCG
KATO III cells
26–500 mM
104
ECG > EGCG
HT1080 cells Thrombin-induced VSMCs
100 mg ml1 30 mM
109 110
ECG > EGCG ECG > EGCG
This journal is ª The Royal Society of Chemistry 2011
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Table 1 (Contd. ) Experimental models Molecular targets
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YMMP-7 activity YYphosphorylation of Met, ERK and Akt YPhosphorylation of ERK and Akt YNDP kinase activity YAdhesion and/or spreading YRibonuclease A (RNase A) enzymatic activity YCollagenase activity
Studied type
Dose
Reference
f Outcomes
MCF10A cells
IC50 ¼ 0.47 mM 0.65 mM
132 116
ECG > EGCG EGCG > ECG
DU145 cells MDA-MB-435 cells 3LL or B16F10 cells Cu(II)-ECG complex
110 mM 3.5 log M
EGCG ¼ ECG EGCG > ECG
46.7 mM
117 118 122,123 119
Prokaryotic and eukaryotic cell
100 mg ml1
111
ECG > EGCG
proliferation and growth than ECG via decreasing the proliferative gene NUDT6 level in HCT116 cells. However, ECG showed more effective in inducing apoptosis of DU145 and KATO III cells than EGCG by increasing ROS formation and TNFa release, respectively. Besides, ECG seems to better inhibit cell growth by blocking b-catenin, PDGF-Rb, ERb and FAS activity in different experimental systems. In HCT116 cells, ECG showed stronger antitumorigenic activity than EGCG by activating transcription factors (e.g. Egr-1, ATF-3) mediated anti-cancer gene expression, including TSP-1 and NAG-1. Nevertheless, EGCG-induced NAG-1 expression is regulated by p53. Recently studies also indicate that ECG had the strongest anti-invasion activity by reducing MMP-2 and MMP-9 activity and their activation by a direct inhibition of MT1-MMP.
EGCG > ECG
These studies suggest that ECG may be biologically more active than EGCG, and EGCG was not always the most potent chemopreventive agent among green tea catechins. While EGCG has been well studied and is known to have chemopreventive property in several cancer cells, but molecular mechanisms of ECG have not been well investigated. Therefore, research on the function of ECG is important for understanding its anti-tumor effect. Previous studies found that ECG more effective than EGCG induced apoptosis and increased cell cycle arrest by inhibiting bcatenin signaling and cyclin D1 expression in SSC-7 cells.63 Interestingly, EGCG may affect anti-tumorigenic activity in a cyclin D1-independent manner.126 EGCG induced apoptosis through increasing H2O2 generation, but not found in ECGinduced apoptosis in HSC-2 cells.103 It has been found that
Fig. 3 Schematic representation of ECG mediated intracellular signaling transduction pathways on carcinogenesis processes. : Induction of signaling cascades by ECG-regulated; ; inhibition of signaling cascades by ECG-regulated.
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Food Funct., 2011, 2, 101–110 | 107
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treatment with EGCG caused G1 arrest and apoptosis in LoVo cells, whereas ECG triggers just the former process.127 Another study displayed that ECG induced apoptosis of HCT116 cells by mediating NAG-1 expression via ATF3 in a p53-independent manner, but EGCG is involved in p53-induced NAG-1 expression.93 These are suggested by resent results, ECG seems to better modulate cell apoptosis in p53 mutant tumor cells. Therefore, these results suggest that ECG and EGCG display differences in anti-tumor mechanisms.
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7. Conclusions In green tea extract, the percentages of the main catechins are EGCG 10–15%, EGC 6–10%, and ECG 2–3%.128 However, high ECG (537.14 mg mL1) occurs in some pu-erh tea129 and pu-erh green tea (EGCG 7.689% and ECG 9.890%, respectively).130 It is clear that ECG can interfere with multiple cell signaling pathways and has multiple targets within the cells, which are likely to interact together to reduce the risk of carcinogenesis (initiation, promotion and progression stages). These mechanisms include (a) inhibition of phase 1 CYP enzymes, (b) induction of phase II detoxification and antioxidant enzymes, (c) anti-inflammatory efficacy (d) arrest of cell cycle progression, (e) regulation of proapoptotic properties and (f) mediation of metastasis processes (Fig. 2 and 3). Many of the anti-carcinogenic affects of ECG may be due to its direct and/or indirect interaction with numerous molecular targets,131 such as NAG-1, AP-1, 5a-reductase and PDGF. Importantly, these growth inhibitions of ECG have been shown to sensitize cancer cells, but not in normal cells. Despite the regulation of intracellular signaling pathways, ECG may also inhibit RNase A and MMPs enzymatic activity via chelating copper and zinc metals, which are important cofactors for angiogenesis and metastasis. Furthermore, structure function analysis revealed that the gallate moiety of ECG is important for mediating these inhibitory effects which these acts may enhance chemoprevention ability.
Abbreviations AP-1 ATF3 BMDCs CAMs CDK CDKIs Chk COX-2 EC ECG EGCG EGC EGF EGFR EGR-1 ER ERK FAS FGF-2
Activator protein-1 Activating transcription factor 3 Bone marrow-derived cells Cell adhesion molecules Cyclin-dependent kinase Cdk inhibitors Check point kinases Cyclooxygenase-2 ()-Epicatechin Epicatechin-3-gallate ()-Epigallocatechin-3-gallate ()-Epigallocatechin Epidermal growth factor Epidermal growth factor receptor Early growth response gene-1 Estrogen receptor Extracellular-signal-regulated kinase Fatty acid synthase Fibroblast growth factor-2
108 | Food Funct., 2011, 2, 101–110
GSH-Px GST HGF hnRNPB1 HO-1 H2O2 IL iNOS JNK MAPK MCT MMP MT1-MMP NAG-1
Glutathione peroxidase Glutathione-S-transferase Hepatocyte growth factor Heterogeneous nuclear ribonucleoprotein B1 Heme oxygenase-1 Hydrogen peroxide Interleukin Inducible nitric oxide synthase Jun amino-terminal kinase Mitogen activated protein kinase Monocarboxylate transporter Matrix metalloproteinase Membrane-type matrix metalloproteinases-1 Non-steroidal anti-inflammatory drug (NSAID) activated gene-1 Nucleoside diphosphate kinase Nuclear factor-kB Nitric oxide NAD(P)H:quinone oxidoreductase 1 Nuclear factor erythroid 2 p45 (NF-E2)related factor 2 Nudix (nucleoside diphosphate linked moiety X)-type motif 6 Platelet-derived growth factor Phosphatidylinositol-3-kinase Prostaglandins P-Glycoprotein Poly(ADP-ribose) polymerase Phosphatase and tensin homolog Retinol binding protein Reactive oxygen species Reactive nitrogen species Ribonuclease A Superoxide dismutase Thiobarbituric acid reactive substances tert-Butylated hydroperoxide T-cell factor Transforming growth factor- b Tissue inhibitor of metalloproteinase Tumor necrosis factor- a 12-O-Tetradecanoyl-phorbol-acetate Transthyretin Vascular endothelial growth factor Vascular smooth muscle cells
NDPK-B NF-kB NO NQO1 Nrf2 NUDT6 PDGF PI3K PGs P-gp PARP PTEN RBP ROS RNS RNase A SOD TBARS t-BOOH TCF TGF-b TIMP TNF-a TPA TTR VEGF VSMCs
References 1 D. L. McKay and J. B. Blumberg, J. Am. Coll. Nutr., 2002, 21, 1. 2 J. Ju, G. Lu, J. D. Lambert and C. S. Yang, Semin. Cancer Biol., 2007, 17, 395. 3 C. Han and Y. Gong, Wei Sheng Yan Jiu, 1999, 28, 343. 4 M. H. Ravindranath, V. Ramasamy, S. Moon, C. Ruiz and S. Muthugounder, Evid. Based. Complement Alternat. Med., 2009, 6, 523. 5 T. Ohe, K. Marutani and S. Nakase, Mutat. Res., Genet. Toxicol. Environ. Mutagen., 2001, 496, 75. 6 K. M. Ku, J. Kim, H. J. Park, K. H. Liu and C. H. Lee, J. Agric. Food Chem., 2010, 58, 345. 7 T. D. Way, H. Y. Lin, D. H. Kuo, S. J. Tsai, J. C. Shieh, J. C. Wu, M. R. Lee and J. K. Lin, J. Agric. Food Chem., 2009, 57, 5257.
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