The Experts below are selected from a list of 5709 Experts worldwide ranked by ideXlab platform
Taeg Kyu Kwon - One of the best experts on this subject based on the ideXlab platform.
-
Chrysin suppresses lipopolysaccharide induced cyclooxygenase 2 expression through the inhibition of nuclear factor for il 6 nf il6 dna binding activity
FEBS Letters, 2005Co-Authors: Yongjin Jeong, Jongwook Park, Hiroyasu Inoue, Taeg Kyu KwonAbstract:Chrysin is a natural, biologically active compound extracted from many plants, honey and propolis. It possesses potent anti-inflammation, anti-cancer and anti-oxidation properties. The mechanism by which Chrysin suppresses COX-2 expression remains poorly understood. In the present report, we investigated the effect of Chrysin on the expression of COX-2 in lipopolysaccharide (LPS)-activated Raw 264.7 cells. Chrysin significantly suppressed the LPS-induced COX-2 protein and mRNA expression in a dose-dependent manner. The ability of Chrysin to suppress the expression of the COX-2 was investigated using luciferase reporters controlled by various cis-elements in COX-2 promoter region. Mutational analysis and electrophoretic mobility shift assay verified that nuclear factor for IL-6 was identified as responsible for the Chrysin-mediated COX-2 downregulation. These results will provide new insights into the anti-inflammatory and anti-carcinogenic properties of Chrysin.
-
Chrysin induced apoptosis is mediated through caspase activation and akt inactivation in u937 leukemia cells
Biochemical and Biophysical Research Communications, 2004Co-Authors: Yongjin Jeong, Jongwook Park, Taeg Kyu KwonAbstract:Chrysin is a natural, biologically active compound extracted from many plants, honey, and propolis. It possesses potent anti-inflammation, anti-cancer, and anti-oxidation properties. The mechanism by which Chrysin initiates apoptosis remains poorly understood. In the present report, we investigated the effect of Chrysin on the apoptotic pathway in U937 human promonocytic cells. We show that Chrysin induces apoptosis in association with the activation of caspase 3 and that Akt signal pathway plays a crucial role in Chrysin-induced apoptosis in U937 cells. Furthermore, we have shown that inhibition of Akt phosphorylation in U937 cells by the specific PI3K inhibitor, LY294002 significantly, enhanced apoptosis. Overexpression of a constitutively active Akt (myr-Akt) in U937 cells inhibited the induction of apoptosis, activation of caspase 3, and PLC-γ1 cleavage by Chrysin. Together, these findings suggest that the Akt pathway plays a major role in regulating the apoptotic response of human leukemia cells to Chrysin and raise the possibility that combined interruption of Chrysin and PI3K/Akt-related pathways may represent a novel therapeutic strategy in hematological malignancies.
Jing Fang - One of the best experts on this subject based on the ideXlab platform.
-
Chrysin inhibits expression of hypoxia inducible factor 1α through reducing hypoxia inducible factor 1α stability and inhibiting its protein synthesis
Molecular Cancer Therapeutics, 2007Co-Authors: Beibei Fu, Zhaodong Li, Binghua Jiang, Jing FangAbstract:Chrysin is a natural flavonoid and has been shown recently to have anticancer effects. However, the mechanisms that Chrysin inhibits cancers are not well known. In this study, we investigated the effects of Chrysin on expression of hypoxia-inducible factor-1α (HIF-1α) and vascular endothelial growth factor in human prostate cancer DU145 cells. Chrysin inhibited insulin-induced expression of HIF-1α by reducing its stability. Chrysin increases ubiquitination and degradation of HIF-1α by increasing its prolyl hydroxylation. In addition, Chrysin interfered with interaction between HIF-1α and heat shock protein 90. Chrysin was also found to inhibit HIF-1α expression through AKT signaling. Inhibition of HIF-1α by Chrysin resulted in abrogation of vascular endothelial growth factor expression. Finally, we showed that Chrysin inhibited DU145 xenograft-induced angiogenesis in nude mice. Taken together, these results suggest that Chrysin is a potent inhibitor of HIF-1α and provide a new sight into the mechanisms of Chrysin against cancers. [Mol Cancer Ther 2007;6(1):220–6]
Gwonhwa Song - One of the best experts on this subject based on the ideXlab platform.
-
Chrysin attenuates progression of ovarian cancer cells by regulating signaling cascades and mitochondrial dysfunction
Journal of Cellular Physiology, 2018Co-Authors: Fuller W Bazer, Gwonhwa SongAbstract:Chrysin is mainly found in passion flowers, honey, and propolis acts as a potential therapeutic and preventive agent to inhibit proliferation and invasion of various human cancer cells. Although Chrysin has anti-carcinogenic effects in several cancers, little is known about its functional roles in ovarian cancer which shows poor prognosis and chemoresistance to traditional therapeutic agents. In the present study, we investigated functional roles of Chrysin in progression of ovarian cancer cells using ES2 and OV90 (clear cell and serous carcinoma, respectively) cell lines. Results of the current study demonstrated that Chrysin inhibited ovarian cancer cell proliferation and induced cell death by increasing reactive oxygen species (ROS) production and cytoplasmic Ca2+ levels as well as inducing loss of mitochondrial membrane potential (MMP). Moreover, Chrysin activated mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K)/AKT pathways in ES2 and OV90 cells in concentration-response experiments. Collectively, our results led us to propose that Chrysin-induced apoptotic events are mediated by the activation of PI3K and MAPK pathways in human ovarian cancer cells.
-
Chrysin induces death of prostate cancer cells by inducing ros and er stress
Journal of Cellular Physiology, 2017Co-Authors: Fuller W Bazer, Gwonhwa SongAbstract:Chrysin is a natural flavone found in numerous plant extracts, honey, and propolis that has multiple biological activities including anti-cancer effects. Understanding of biological mechanisms mediated in response to Chrysin in cancerous cells may provide novel insight into chemotherapeutic approaches with reduced side effects in cancers. In the present study, we investigated functional roles of Chrysin in progression of prostate cancer cells using DU145 and PC-3 cell lines. The results showed that Chrysin induced apoptosis of cells evidenced by DNA fragmentation and increasing the population of both DU145 and PC-3 cells in the sub-G1 phase of the cell cycle. In addition, Chrysin reduced expression of proliferating cell nuclear antigen in the prostate cancer cell lines compared to untreated prostate cancer cells. Moreover, Chrysin induced loss of mitochondria membrane potential (MMP), while increasing production of reactive oxygen species (ROS) and lipid peroxidation in a dose-dependent manner. Also, it induced endoplasmic reticulum (ER) stress through activation of unfolded protein response (UPR) proteins including PRKR-like ER kinase (PERK), eukaryotic translation initiation factor 2α (eIF2α), and 78 kDa glucose-regulated protein (GRP78) in DU145 and PC-3 cells. The Chrysin-mediated intracellular signaling pathways suppressed phosphoinositide 3-kinase (PI3K) and the abundance of AKT, P70S6K, S6, and P90RSK proteins, but stimulated mitogen-activated protein kinases (MAPK) and activation of ERK1/2 and P38 proteins in the prostate cancer cells. Collectively, these results indicate that Chrysin initiates cell death through induction of mitochondrial-mediated apoptosis and ER stress, and regulation of signaling pathways responsible for proliferation of prostate cancer cells.
Yongjin Jeong - One of the best experts on this subject based on the ideXlab platform.
-
Chrysin suppresses lipopolysaccharide induced cyclooxygenase 2 expression through the inhibition of nuclear factor for il 6 nf il6 dna binding activity
FEBS Letters, 2005Co-Authors: Yongjin Jeong, Jongwook Park, Hiroyasu Inoue, Taeg Kyu KwonAbstract:Chrysin is a natural, biologically active compound extracted from many plants, honey and propolis. It possesses potent anti-inflammation, anti-cancer and anti-oxidation properties. The mechanism by which Chrysin suppresses COX-2 expression remains poorly understood. In the present report, we investigated the effect of Chrysin on the expression of COX-2 in lipopolysaccharide (LPS)-activated Raw 264.7 cells. Chrysin significantly suppressed the LPS-induced COX-2 protein and mRNA expression in a dose-dependent manner. The ability of Chrysin to suppress the expression of the COX-2 was investigated using luciferase reporters controlled by various cis-elements in COX-2 promoter region. Mutational analysis and electrophoretic mobility shift assay verified that nuclear factor for IL-6 was identified as responsible for the Chrysin-mediated COX-2 downregulation. These results will provide new insights into the anti-inflammatory and anti-carcinogenic properties of Chrysin.
-
Chrysin induced apoptosis is mediated through caspase activation and akt inactivation in u937 leukemia cells
Biochemical and Biophysical Research Communications, 2004Co-Authors: Yongjin Jeong, Jongwook Park, Taeg Kyu KwonAbstract:Chrysin is a natural, biologically active compound extracted from many plants, honey, and propolis. It possesses potent anti-inflammation, anti-cancer, and anti-oxidation properties. The mechanism by which Chrysin initiates apoptosis remains poorly understood. In the present report, we investigated the effect of Chrysin on the apoptotic pathway in U937 human promonocytic cells. We show that Chrysin induces apoptosis in association with the activation of caspase 3 and that Akt signal pathway plays a crucial role in Chrysin-induced apoptosis in U937 cells. Furthermore, we have shown that inhibition of Akt phosphorylation in U937 cells by the specific PI3K inhibitor, LY294002 significantly, enhanced apoptosis. Overexpression of a constitutively active Akt (myr-Akt) in U937 cells inhibited the induction of apoptosis, activation of caspase 3, and PLC-γ1 cleavage by Chrysin. Together, these findings suggest that the Akt pathway plays a major role in regulating the apoptotic response of human leukemia cells to Chrysin and raise the possibility that combined interruption of Chrysin and PI3K/Akt-related pathways may represent a novel therapeutic strategy in hematological malignancies.
Wei Liang - One of the best experts on this subject based on the ideXlab platform.
-
Chrysin promotes osteogenic differentiation via erk mapk activation
Protein & Cell, 2013Co-Authors: Wenfeng Zeng, Fayun Zhang, Chunling Zhang, Wei LiangAbstract:The effect of the anti-inflammatory flavonoid Chrysin on osteogenesis was determined in preosteoblast MC3T3-E1 cells. Results demonstrated that Chrysin could induce osteogenic differentiation in the absence of other osteogenic agents. Chrysin treatment promoted the expression of transcription factors (Runx2 and Osx) and bone formation marker genes (Col1A1, OCN, and OPN) as well as enhanced the formation of mineralized nodules. During osteogenic differentiation, Chrysin preferentially activated ERK1/2, but not JNK nor the p38 MAPKs. Further experiments with inhibitors revealed the co-treatment of U0126, PD98059, or ICI182780 (a general ER antagonist) with Chrysin effectively abrogated the Chrysin-induced osteogenesis and ERK1/2 activation. Thus, the effect of Chrysin on osteogenesis is ERK1/2-dependent and involves ER. Therefore, Chrysin has the significant potential to enhance osteogenesis for osteoporosis prevention and treatment.
-
Chrysin promotes osteogenic differentiation via ERK/MAPK activation
Protein & Cell, 2013Co-Authors: Wenfeng Zeng, Fayun Zhang, Chunling Zhang, Wei LiangAbstract:The effect of the anti-inflammatory flavonoid Chrysin on osteogenesis was determined in preosteoblast MC3T3-E1 cells. Results demonstrated that Chrysin could induce osteogenic differentiation in the absence of other osteogenic agents. Chrysin treatment promoted the expression of transcription factors (Runx2 and Osx) and bone formation marker genes (Col1A1, OCN, and OPN) as well as enhanced the formation of mineralized nodules. During osteogenic differentiation, Chrysin preferentially activated ERK1/2, but not JNK nor the p38 MAPKs. Further experiments with inhibitors revealed the co-treatment of U0126, PD98059, or ICI182780 (a general ER antagonist) with Chrysin effectively abrogated the Chrysin-induced osteogenesis and ERK1/2 activation. Thus, the effect of Chrysin on osteogenesis is ERK1/2-dependent and involves ER. Therefore, Chrysin has the significant potential to enhance osteogenesis for osteoporosis prevention and treatment.