Disease relevance of butein

• The antinephritic effects of butein (3,4,2',4'-tetrahydroxychalcone) on original-type anti-glomerular basement membrane antibody-associated glomerulonephritis in rats were investigated [1].
• Butein was given to anti-glomerular basement membrane antibody-associated glomerulonephritic rats for 15 days after the induction of nephritis [1].
• Butein prevented proteinuria and histological alterations [1].
• The aim of this work was to investigate the effects of butein on liver fibrosis induced by carbon tetrachloride (CCl4) in rats, and to explore its antifibrogenic mechanism [2].
• The plant polyphenol butein inhibits testosterone-induced proliferation in breast cancer cells expressing aromatase [3].

High impact information on butein

• Among the polyphenols examined for their action on DNP-SG export, butein was the most potent inhibitor with an IC50 value of 15 microM [4].
• Taken together, these results suggest that butein inhibits iNOS gene expression, providing possible mechanisms for its anti-inflammatory action [5].
• Butein also inhibited the induction of tumor necrosis factor-alpha and cyclooxygenase 2 by LPS [5].
• The LPS-induced DNA binding activity of NF-kappaB was significantly inhibited by butein, and this effect was mediated through inhibition of the degradation of inhibitory factor-kappaB and phosphorylation of Erk1/2 MAP kinase [5].
• Furthermore, increased binding of the osteopontin alphavbeta3 integrin receptor by butein may explain its inhibitory effect on LPS-mediated NO production [5].

Chemical compound and disease context of butein

• The chalcone butein from Rhus verniciflua Stokes inhibits clonogenic growth of human breast cancer cells co-cultured with fibroblasts [6].
• These results demonstrate that isoliquiritigenin and butein inhibit cell proliferation and induce apoptosis in B16 melanoma cells [7].

Biological context of butein

• These data suggest that the antinephritic action of butein is due to inhibition of intraglomerular accumulation of leukocytes through the prevention of the up-regulation of ICAM-1 and the inhibition of a function of adhesion molecules on the surface of leukocytes [1].
• These data suggest the potential of butein to serve as an antifibrogenic agent by inhibition of collagen accumulation and lipid peroxidation, and by down-regulation of the expression of both alpha1(I) collagen and TIMP-1 mRNA [2].
• Cytotoxic effect of butein on human colon adenocarcinoma cell proliferation [8].
• Butein, at a concentration of 1 microg mL(-1), reduced DNA synthesis without affecting cell viability, and downregulated smooth muscle alpha-actin and type-I collagen expression, and alpha1(I) collagen and tissue inhibitor of metalloproteinase-1 mRNA expression, while treatment with butein induced metalloproteinase-13 mRNA expression [9].
• The caspase-3 activity was increased during butein-induced apoptosis [10].

Anatomical context of butein

• When human umbilical vein endothelial cells or neutrophils were treated with butein, the adhesion of neutrophils to human umbilical vein endothelial cells was suppressed [1].
• These results indicate that the vasorelaxant effect of butein depended on the endothelium and was mediated by endothelium-derived relaxing factor (EDRF) [11].
• Butein, (10 microM), the most potent anti-proliferative agent, exerted 30% growth inhibition and was more effective on HeLa cells [12].
• In a subsequent experiment, we measured the dose-response effect on the clonogenic growth of UACC-812 breast cancer cells by pre-incubating the fibroblasts with varying concentrations of butein (10 microg/ml-1.25 microg/mL) [6].
• Apoptotic DNA fragments in the butein-treated HL-60 cells were increased gradually as determined by flow cytometric analysis [10].

Associations of butein with other chemical compounds

• The chalcone butein from Rhus verniciflua shows antifibrogenic activity [2].
• Biocatalytic synthesis of butein and sulfuretin by Aspergillus alliaceus [13].
• Finally, EI-MS, 1H-NMR, and 13C-NMR spectra confirmed that RCMF contained flavonoid derivatives, including protocatechuic acid, fustin, fisetin, sulfuretin, and butein, suggesting that these flavonoid derivatives are the main active compounds responsible for the antioxidant and antiproliferative activities of RCMF [14].
• The mode of cytotoxic action of butein was different from 5-FU but may be similar to colchicine, a known HeLa cell inhibitor [8].
• Cell proliferation assay indicated that the cell number increased by 10 nM-testosterone treatment was significantly reduced by 5 microM butein, and the administration of flutamide could not reverse the effect [3].

Gene context of butein

• Molecular modelling suggests that butein, marein and phloretin can be docked into the ATP binding pocket of EGFR [15].
• On the other hand, it was suggested that butein induces apoptosis via down-regulation of Bcl-2 expression and promotion of Bax expression [7].
• Butein prevented the up-regulation of ICAM-1 expression mediated by TNF-alpha or PMA on human umbilical vein endothelial cells in a dose-dependent manner [1].
• Inhibition of lipopolysaccharide-induced expression of inducible nitric oxide synthase by butein in RAW 264.7 cells [5].
• Butein, a specific protein tyrosine kinase inhibitor [16].

Analytical, diagnostic and therapeutic context of butein

• This method was applied to a pharmacokinetic study after intravenous injection of butein (5mg/kg) to rats [17].
• Determination of butein in rat serum by high performance liquid chromatography [17].
• The effects of butein on alpha1(I) collagen, tissue inhibitor of metalloproteinase-1, and metalloproteinase-13 gene expression in activated stellate cells were investigated by measuring mRNA levels using reverse transcription polymerase chain reaction [9].
• The effects of butein on the production of collagen and smooth muscle alpha-actin proteins were examined at the same concentration, by western blot [9].
• The present study illustrated that butein was an aromatase inhibitor and a potential natural alternative for the chemoprevention or therapy of breast cancer [3].

References