Diallyl trisulfide inhibits angiogenic features of human umbilical vein endothelial cells by causing Akt inactivation and down-regulation of VEGF and VEGF-R2

Nutrition and Cancer

Volumn 55, Issue 1, 2006, Pages 94-107

  Xiao, Dong ^a   Li, Mengfeng ^a   Herman Antosiewicz, Anna ^a   Antosiewicz, Jedrzej ^a   Xiao, Hui ^a   Lew, Karen L ^a   Zeug, Yan ^a   Marynowski, Stanley W ^a   Singh, Shivendra V ^a  

^a UNIVERSITY OF PITTSBURGH CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ALLYL SULFIDE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; BENZYLOXYCARBONYLISOLEUCYLGLUTAMYLTHREONYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLLEUCYLGLUTAMYLHISTIDYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE 3; CASPASE 9; CASPASE INHIBITOR; DIALLYL DISULFIDE; DIALLYL TRISULFIDE; DNA FRAGMENT; HISTONE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN BAD; PROTEIN KINASE B; STRESS ACTIVATED PROTEIN KINASE; VASCULOTROPIN; VASCULOTROPIN RECEPTOR 2;

ANGIOGENESIS; APOPTOSIS; ARTICLE; CAPILLARY; CELL MIGRATION; CELL SURVIVAL; CONTROLLED STUDY; CYTOPLASM; DIPLOIDY; DRUG RECEPTOR BINDING; ENDOTHELIUM CELL; ENZYME DEGRADATION; ENZYME INACTIVATION; ENZYME INHIBITION; GARLIC; HUMAN; HUMAN CELL; IC 50; MITOCHONDRION; PROTEIN LOCALIZATION; PROTEIN SECRETION; RECEPTOR DOWN REGULATION;

ALLYL COMPOUNDS; ANGIOGENESIS INHIBITORS; APOPTOSIS; CASPASES; CELL SURVIVAL; CELLS, CULTURED; DNA FRAGMENTATION; DOSE-RESPONSE RELATIONSHIP, DRUG; DOWN-REGULATION; ENDOTHELIAL CELLS; GARLIC; HUMANS; INHIBITORY CONCENTRATION 50; PROTO-ONCOGENE PROTEINS C-AKT; SULFIDES; UMBILICAL VEINS; VASCULAR ENDOTHELIAL GROWTH FACTOR A; VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR-2;

ALLIUM SATIVUM;

EID: 33749183133     PISSN: 01635581     EISSN: None     Source Type: Journal    
DOI: 10.1207/s15327914nc5501_12     Document Type: Article

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