Though the chemical structure of chrysin with only two hydroxyls at place 5 and 7 of A ring showed lower cytotoxicity activity in particular human cancer cells, the prospective apoptotic result of chrysin has been reported in human cervical cancer, leukemia, esophageal squamous carcinoma, malignant glioma, breast carcinoma, prostate cancer, non modest cell lung cancer and colon cancer in vitro, as outlined in Table 1. The Natural products has been implicated in the regulation of a broad spectrum of cellular processes, including cell customized peptide price cycle arrest and apoptosis. Besides, it has been regarded as a likely phosphate donor for the p65 subunit of NFkappaB. According to the study, treatment method of HeLa cells with 30 uM chrysin for 24 h induced a important improve of NFkappaB/p65 levels in the cells, as demonstrated by EMSA.

The signals could be suppressed by a specific p38 or p65 inhibitor indicating that the p38 or p65 could be useful therapeutic targets of chrysin to manage gene expression in HeLa cells. Nevertheless, no correlation of pro apoptotic or apoptotic activity induced by chrysin in this phenomenon was plainly stated in the study. Though, chrysin was identified to substantially sensitize the TNFalpha induced apoptosis in human colorectal cancer cell line HCT 116, human liver cancer cell line HepG2, and the human nasopharyngeal carcinoma cell line CNE 1, in which this kind of sensitization is closely linked with inhibitory impact on NFkappaB activation, the phenomenon could take place in different ways in HeLa cells. Therefore, the NFkappaB stays a prospective target to examine the mechanism of apoptosis induced by chrysin in HeLa cells.

Although each chrysin peptide calculator and phosphorylated chrysin could inhibit proliferation and induced apoptosis in HeLa cells, as talked about above, the effects of the phosphorylated chrysins had been probably more potent than that of non phosphorylated chrysin, where the estimated IC50 for chrysin was 14. 2 uM, followed by CPE and CP, assessed by the cell viability assays. Phosphorylated chrysin, which could very easily form non covalent compound with lysozyme, are thus concluded as much more efficient in inhibiting cancer cell growth and inducing apoptosis than non phosphorylated chrysin in HeLa cells. 3In 1 examine, different flavonoids and relevant compounds had been screened in human leukemia cells, how to dissolve peptide. Amongst the flavonoids examined, genistein, apigenin, alpha naphto flavone, chrysin, quercetin, galangin, luteolin, fisetin and 3,7 dihydroxyflavone were discovered to substantially lessen the cellular viability of the U937 cells.

However, only apigenin, chrysin, quercetin, galangin, luteolin and fisetin had been discovered to plainly induce the oligonucleosomal DNA fragmentation at 50 ?M right after 6 h of treatment method. Chrysin was the most productive flavonoid in terms of decreasing the viability of the U937 cells with an IC50 of 16 uM. Chrysin also potentiated the effects of TNFalpha in triggering apoptosis in the cells. On the other hand, Woo et al. showed that chrysin induced apoptosis in association with activation of caspase 3, involving inactivation of Akt or Protein Kinases B signaling and down regulation of X linked inhibitor of apoptosis protein in the U937 cells.

This research provided the first proof of a much more comprehensive molecular mechanism whereby chrysin induces the apoptosis in leukemia cells namely through Akt dephosphorylation of the phosphoinositide 3 kinase signaling pathway. The Akt signaling pathway, from PARP PI3K to phosphoinositide dependent kinase 1 and from PDK1 to Akt, mediates apoptosis in human cancer cells.