Document Detail


Enhanced anti-tumor activity by the combination of the natural compounds (-)-epigallocatechin-3-gallate and luteolin: potential role of p53.
MedLine Citation:
PMID:  20826787     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Natural dietary agents have drawn a great deal of attention toward cancer prevention because of their wide safety margin. However, single agent intervention has failed to bring the expected outcome in clinical trials; therefore, combinations of chemopreventive agents are gaining increasingly popularity. In the present study, we investigated a combinatorial approach using two natural dietary polyphenols, luteolin and EGCG, and found that their combination at low doses (at which single agents induce minimal apoptosis) synergistically increased apoptosis (3-5-fold more than the additive level of apoptosis) in both head and neck and lung cancer cell lines. This combination also significantly inhibited growth of xenografted tumors in nude mice. The in vivo findings also were supported by significant inhibition of Ki-67 expression and increase in TUNEL-positive cells in xenografted tissues. Mechanistic studies revealed that the combination induced mitochondria-dependent apoptosis in some cell lines and mitochondria-independent apoptosis in others. Moreover, we found more efficient stabilization and ATM-dependent Ser(15) phosphorylation of p53 due to DNA damage by the combination, and ablation of p53 using shRNA strongly inhibited apoptosis as evidenced by decreased poly(ADP-ribose) polymerase and caspase-3 cleavage. In addition, we observed mitochondrial translocation of p53 after treatment with luteolin or the combination of EGCG and luteolin. Taken together, our results for the first time suggest that the combination of luteolin and EGCG has synergistic/additive growth inhibitory effects and provides an important rationale for future chemoprevention trials of head and neck and lung cancers.
Authors:
A R M Ruhul Amin; Dongsheng Wang; Hongzheng Zhang; Shifang Peng; Hyung Ju C Shin; Johann C Brandes; Mourad Tighiouart; Fadlo R Khuri; Zhuo Georgia Chen; Dong M Shin
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-09-08
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  285     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-11-01     Completed Date:  2010-11-30     Revised Date:  2011-11-07    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  34557-65     Citation Subset:  IM    
Affiliation:
Department of Hematology and Medical Oncology, Winship Cancer Institute of Emory University, Atlanta, Georgia 30322, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Anticarcinogenic Agents / agonists,  pharmacology*
Apoptosis / drug effects
Caspase 3 / metabolism
Catechin / agonists,  analogs & derivatives*,  pharmacology
Cell Cycle Proteins / pharmacology
Cell Line, Tumor
DNA Damage / drug effects
DNA-Binding Proteins / pharmacology
Drug Synergism
Gene Expression Regulation, Neoplastic / drug effects
Head and Neck Neoplasms / metabolism*,  prevention & control*
Humans
Ki-67 Antigen / biosynthesis
Luteolin / agonists,  pharmacology*
Mice
Mice, Nude
Mitochondria / metabolism
Neoplasm Transplantation
Phosphorylation / drug effects
Protein Stability / drug effects
Protein-Serine-Threonine Kinases / pharmacology
Tumor Suppressor Protein p53 / metabolism*
Tumor Suppressor Proteins / pharmacology
Xenograft Model Antitumor Assays
Grant Support
ID/Acronym/Agency:
P50 CA128613/CA/NCI NIH HHS; R01 CA112643/CA/NCI NIH HHS; U01 CA101244/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Anticarcinogenic Agents; 0/Cell Cycle Proteins; 0/DNA-Binding Proteins; 0/Ki-67 Antigen; 0/TP53 protein, human; 0/Tumor Suppressor Protein p53; 0/Tumor Suppressor Proteins; 154-23-4/Catechin; 491-70-3/Luteolin; 989-51-5/epigallocatechin gallate; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/ataxia telangiectasia mutated protein; EC 3.4.22.-/Casp3 protein, mouse; EC 3.4.22.-/Caspase 3

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