Changes of the stability and bioactivity of quercetin and myricetin in BGC-823 cells in response to heat treatment and Fe2+/Cu2+ addition
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Two flavonols quercetin and myricetin with heat treatment and Fe2+/Cu2+ addition were assessed for stability and bioactivity changes. Quercetin and myricetin at 37 °C showed higher degradation rate constants than those at 20 °C (0.133 − 1.025 vs. 0.299 − 1.803 h−1). Due to the chelation of flavonol and metals, Fe/Cu addition at the two temperatures (except Cu addition at 37 °C) mostly led to enhanced stability via decreasing the constant values to 0.064 − 0.675 h−1. Cell counting kit-8 assaying results showed that myricetin and quercetin heated at 37 °C and 100 °C received decreased growth inhibition in human gastric cancer BGC-823 cells, because they at 80 μmol/L showed decreased inhibition percentages (from 41.1 − 45.6 to 23.9 − 43.3%, cell treatment of 24 h; or from 46.6 − 51.9 to 28.8 − 46.5%, cell treatment of 48 h). The assaying results of Hoechst 33,258staining, DCFH-DA fluorescence probe, and flow cytometry also proved that the heated flavonols in the cells had less reactive oxygen species generation, lower DNA damage, and weakened apoptosis induction, compared with the unheated flavonols. Fe addition decreased these flavonol bioactivities in the cells because of decreased flavonol–Fe chelation and enhanced flavonol degradation; however, Cu addition induced oxidative stress and thus led to less bioactivity decrease than Fe addition. Correlation analysis results indicated that decreased reactive oxygen species generation of the two flavonols was correlated with decreased apoptosis induction (p < 0.05). Overall, these used treatments brought about stability and bioactivity changes for the two flavonols, suggesting reasonable consideration should be paid on processing conditions and some components of foods when studying food bioactivities.
KeywordsFlavonols Metal ions Heat treatment Stability Bioactivity Gastric cancer cells
This work was funded by the Specialized Research Fund for the Doctoral Program of Higher Education (Project No. 200802240002). The authors thank the anonymous referees for their valuable advice.
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Conflicts of interest
The authors declare that they have no competing interests.
- 1.J.P.E. Spencer, A. Crozier, Flavonoids and Related Compounds: Bioavailability and Function (CRC Press, Boca Raton, 2013)Google Scholar
- 9.Batra P, Sharma AK (2013) Anti-cancer potential of flavonoids: recent trends and future perspectives. 3 Biotech 3:439–459Google Scholar
- 12.S. Settharaksa, A. Jongjareonrak, P. Hmadhlu, W. Chansuwan, S. Siripongvutikorn, Flavonoid, phenolic contents and antioxidant properties of Thai hot curry paste extract and its ingredients as affected of pH, solvent types and high temperature. Int. Food Res. J. 4, 1581–1587 (2012)Google Scholar
- 24.J.L. Lou, G.H. Chu, G.J. Zhou, J. Jiang, F.F. Huang, J.J. Xu, S. Zheng, W. Jiang, Y.Z. Lu, X.X. Li, Z.J. Chen, J.L. He, Comparison between two kinds of cigarette smoke condensates (CSCs) of the cytogenotoxicity and protein expression in a human B-cell lymphoblastoid cell line using CCK-8 assay, comet assay and protein microarray. Mutat. Res. Genet. Toxicol. Environ. Mutagen. 697, 55–59 (2010)CrossRefGoogle Scholar
- 36.J. Fu, H. Zhang, Y. Zhang, T. Zhang, AG1031 induces apoptosis through suppressing SIRT1/p53 pathway in human neuroblastoma cells. Mol. Cell. Biochem. 1–2, 165–175 (2018)Google Scholar
- 37.Y. Peng, Z.Z. Fu, C.S. Guo, Y.X. Zhang, Q.W. Li, Effects and mechanism of baicalin on apoptosis of cervical cancer HeLa cells in-vitro. Iran. J. Pharm. Res. 1, 251–261 (2015)Google Scholar
- 38.M. Mitsis, G.A. Alexiou, E. Vartholomatos, G. Markopoulos, D. Lazari, E. Hodaj, D. Nastos, P. Zagorianakou, V. Galani, A.P. Kyritsis, N-(p-coumaroyl) serotonin induces cell cycle arrest and apoptosis in breast cancer cells. J. BUON 1, 129–133 (2018)Google Scholar
- 42.J.H. Seo, Y. Ahn, S.R. Lee, C.Y. Yeo, K.C. Hur, The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 Kinase) in the PI-3 kinase/AKT pathway. Mol. Biol. Cell 16, 348–357 (2005)CrossRefGoogle Scholar