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Rhapontigenin

$143

  • Brand : BIOFRON

  • Catalogue Number : BF-R3003

  • Specification : 98%

  • CAS number : 500-65-2

  • Formula : C15H14O4

  • Molecular Weight : 258.272

  • PUBCHEM ID : 5320954

  • Volume : 25mg

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Catalogue Number

BF-R3003

Analysis Method

HPLC,NMR,MS

Specification

98%

Storage

2-8°C

Molecular Weight

258.272

Appearance

Yellow crystalline powder

Botanical Source

Trigonella foenum-graecum,Rumex nepalensis,Rheum hotaoense,Gnetum cleistostachyum

Structure Type

Stilbenes

Category

Standards;Natural Pytochemical;API

SMILES

COC1=C(C=C(C=C1)C=CC2=CC(=CC(=C2)O)O)O

Synonyms

trans-1-(3,5-Dihydroxyphenyl)-2-(3-hydroxy-4-methoxyphenyl)ethylene/5-[(E)-2-(3-Hydroxy-4-methoxyphenyl)vinyl]-1,3-benzenediol/rhapontigenin/5-[(E)-2-(3-Hydroxy-4-methoxyphenyl)vinyl]benzene-1,3-diol/(E)-5-(3-Hydroxy-4-methoxystyryl)benzene-1,3-diol/1,3-Benzenediol, 5-[(E)-2-(3-hydroxy-4-methoxyphenyl)ethenyl]-/3,3',5-Trihydroxy-4'-methoxy-trans-stilbene/5-[(E)-2-(3-hydroxy-4-methoxyphenyl)ethenyl]benzene-1,3-diol

IUPAC Name

5-[(E)-2-(3-hydroxy-4-methoxyphenyl)ethenyl]benzene-1,3-diol

Density

1.3±0.1 g/cm3

Solubility

Methanol

Flash Point

258.4±26.8 °C

Boiling Point

503.6±38.0 °C at 760 mmHg

Melting Point

186-187ºC

InChl

InChl Key

WGK Germany

RID/ADR

HS Code Reference

2938900000

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:500-65-2) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

PMID

30820014

Abstract

BACKGROUND/AIMS:
Rhapontigenin (RPG) is a stilben derivative and is known to bear several effects such as antiallergic, anticoagulative, hypoglycemic, antiangiogenic, and purgative. The investigation was conducted to evaluate the cardioprotective efficacy of RPG in rats having acute myocardial infarction (MI) induced by isoproterenol (ISO).

METHODS:
Animals were divided into 6 groups: group I (control group), group II (ISO-treated), group III (1.0 mg/kg/day RPG and ISO-treated), group IV (2.5 mg/kg/day RPG and ISO-treated), group V (5.0 mg/kg/day RPG and ISO-treated), and group VI (treated with RPG 5.0 mg/kg/day). Various cardiac stress markers, including infarct size and heart/body weight index, were investigated in animals with ISO-induced MI, such as inducible nitric oxide synthase (iNOS), creatinine kinase (CK), lactate dehydrogenase (LD), cardiac troponin-T (CTT), superoxide dismutase (SOD), and malondialdehyde. INOS, p38, caspase-3, and connexin 43 expressions were analyzed in animals. Inflammatory mediators, tissue necrosis factor-α (TNF-α) and interleukin-6 (IL-6), were detected in serum of experimental animals.

RESULTS:
Group I animals indicated normal levels of biochemical parameters, whereas group II animals indicated high levels of these parameters and successful induction of MI. Pretreatment of animal groups III, IV, and V with RPG revealed amelioration of infarct size, heart/body weight index, CK, LD, CTT in rats, whereas group VI animals were treated only with RPG (5.0 mg/kg/day) and not with ISO. Levels of TNF-α, IL-6, MD, SOD, p38, and iNOS expressions were significantly downregulated by RPG administration (5.0 mg/kg/day).

CONCLUSION:
RPG ameliorates MI caused by ISO in rats and provides cardioprotective effect, via anti-inflammatory, antioxidant, and antiapoptotic effect.

© 2019 S. Karger AG, Basel.

KEYWORDS

Cardioprotective; Isoproterenol; Myocardial infarction; Oxidative stress; Rhapontigenin

Title

Cardioprotective Effect of Rhapontigenin in Isoproterenol-Induced Myocardial Infarction in a Rat Model.

Author

Fan Y1.

Publish date

2019

PMID

21628883

Abstract

Hypoxia inducible factor 1 alpha (HIF-1α) is frequently over-expressed in the numerous types of cancer and plays an important role in angiogenesis. In the present study, the inhibitory mechanism of rhapontigenin isolated from Vitis coignetiae was investigated on HIF-1α stability and angiogenesis in human prostate cancer PC-3 cells. Rhapontigenin significantly suppressed HIF-1α accumulation at protein level but not at mRNA level in PC-3 cells under hypoxia. Also, rhapontigenin suppressed hypoxia-induced HIF-1α activation in various cancer cells, such as colorectal adenocarcinoma (SW620), breast adenocarcinoma (MCF-7), fibrosarcoma (HT-1080) and prostate carcinoma (LNCaP). Interestingly, rhapontigenin had more potency in inhibition of hypoxia-induced HIF-1α expression than that of resveratrol, a known HIF-1α inhibitor. In addition, rhapontigenin promoted hypoxia-induced HIF-1α degradation and cycloheximide (CHX) blocked protein synthesis. A prolyl hydroxylase (PHD) inhibitor dimethyloxalylglycine (DMOG) is usually utilized to examine whether prolyl hydroxylation is involved in inhibition of HIF-1α accumulation. Here, DMOG recovered HIF-1α accumulation inhibited by rhapontigenin. Immunoprecipitation assay also revealed that rhapotigenin enhanced the binding of hydroxylated HIF-1α to von Hippel-Lindau (VHL) tumor suppressor protein. Furthermore, rhapontigenin reduced vascular endothelial growth factor (VEGF) secretion in hypoxic PC-3 cells as well as suppressed tube formation in human umbilical vein endothelial cells (HUVECs) treated by the conditioned media of hypoxic PC-3 cells. However, anti-angiogenic effect of rhapontigenin in hypoxic PC-3 cells was reversed by DMOG. Taken together, these findings suggest that rhapontigenin inhibits HIF-1α accumulation and angiogenesis in PC-3 prostate cancer cells.

Title

Rhapontigenin inhibited hypoxia inducible factor 1 alpha accumulation and angiogenesis in hypoxic PC-3 prostate cancer cells.

Author

Jung DB1, Lee HJ, Jeong SJ, Lee HJ, Lee EO, Kim YC, Ahn KS, Chen CY, Kim SH.

Publish date

2011

PMID

26986649

Abstract

The epithelial-mesenchymal transition (EMT) is a pivotal event in cancer cell invasion and metastasis. Emerging evidence suggests that rhapontigenin (Rha) may impede the progression of cancer by disrupting angiogenesis and the EMT. However, the underlying mechanism of Rha has not yet been clarified. In this study, we used transforming growth factor β (TGF-β) to trigger EMT in diverse types of cancer cells and revealed that Rha inhibited TGF-β-induced EMT and derived‑cell invasiveness. The effects of TGF-β were blocked by Rha via interference with the PI3K/AKT/mTOR/GSK3β/β‑catenin signaling pathway. Furthermore, Rha also inhibited TGF-β‑induced expression of transcription regulators Snail and hypoxia-inducible factor 1α (HIF-1α) by causing their degradation by the 26S proteasome. Surprisingly, although HIF-1α was degraded with Snail as a result of Rha exposure, HIF-1α was not a key factor involved in TGF-β-mediated EMT induced by Rha. Knocking-down Snail expression, but not HIF-1α expression, by RNA interference dramatically reversed TGF-β-mediated EMT. Moreover, Rha abolished TGF-β-triggered cell invasiveness. Our results demonstrate that Rha inhibits TGF-β-induced EMT in cancer cells by suppressing the activity of the PI3K/AKT/mTOR pathway. Therefore, Rha may represent a new route for therapeutic intervention in cancer patients and merits future studies to assess its potential.

Title

Rhapontigenin inhibits TGF-β-mediated epithelial‑mesenchymal transition via the PI3K/AKT/mTOR pathway and is not associated with HIF-1α degradation.

Author

Yeh YH1, Wang SW2, Yeh YC3, Hsiao HF4, Li TK1.

Publish date

2016 May


Description :

Antihyperlipidemic effects of rhapontin and rhapontigenin from rheum undulatum in rats fed a high-cholesterol diet PUMID/DOI:25127020 Planta Med. 2014 Aug;80(13):1067-71. Rhapontin was purified from a methanol extract from the roots of Rheum undulatum, and Rhapontigenin was produced by an enzymatic transformation of rhapontin. Rats were fed a high-cholesterol diet to induce hyperlipidemia, followed by oral treatment with rhapontin or Rhapontigenin (1-5 mg/kg/day). Rhapontin and Rhapontigenin treatment resulted in a significant (p<0.05) dose-dependent decrease in the serum lipid level, while the high-density lipoprotein cholesterol level increased slightly compared with the experimental control. Furthermore, rhapontin and Rhapontigenin treatment improved the pathological characteristics of the degenerating fatty liver in high-cholesterol diet-induced hyperlipidemic rats dose-dependently. Aspartate aminotransferase and alanine aminotransferase levels in rhapontin- and Rhapontigenin-treated hyperlipidemic rats were not significantly different from those in the control. These results indicate that rhapontin and Rhapontigenin can be used as potent antihyperlipidemic agents. The possible mechanism of rhapontigenin influencing antifungal activity on Candida albicans. PUMID/DOI:22662760 ]Med Mycol. 2013 Jan;51(1):45-52. Rhapontigenin, an aglycone of rhapontin, was produced by biotransformation and we investigated its antifungal activity against Candida albicans, one of the most important opportunistic fungal pathogens. Rhapontigenin is found to have, in vitro, inhibitory activity with a minimal inhibitory concentration (MIC) value against all test isolates of 128-256 μg/ml. We detected increased reactive oxygen species (ROS) levels in yeast cultures treated with Rhapontigenin at the MIC. Rhapontigenin inhibited DNA, RNA, and protein synthesis, especially RNA synthesis, and induced morphological changes and apoptosis of C. albicans. The apoptotic effect of Rhapontigenin on C. albicans at subinhibitory concentrations was higher in the stationary growth phase than in the exponential phase, while the opposite results were noted with amphotericin B. The mechanism of antifungal activity of Rhapontigenin may be associated with the generation of ROS that might induce apoptosis and it may also involve the inhibition of ergosterol biosynthesis. Rhapontigenin suppresses cell migration and invasion by inhibiting the PI3K-dependent Rac1 signaling pathway in MDA-MB-231 human breast cancer cells. PUMID/DOI: J Nat Prod. 2014 May 23;77(5):1135-9. Rhapontigenin (1) has various biological activities including anticancer activities. However, whether and how Rhapontigenin affects cancer invasion has never been explored. Here, we examined the anti-invasive effects of Rhapontigenin and its underlying molecular mechanisms in the highly invasive human breast cancer cell line designated MDA-MB-231. At noncytotoxic concentrations, Rhapontigenin strongly suppressed serum-induced cell migration and invasion as judged by Boyden chamber analysis and wound-healing assays, respectively. Rhapontigenin strikingly reduced Rac1 activity as judged by both absorbance-based and pull-down assays. In addition, its downstream effectors such as WASP-family verprolin homologous proteins 2 (WAVE-2) and p21-activated kinase Rhapontigenin (PAK1) signaling cascades were attenuated after treatment with Rhapontigenin. Immunofluorescence staining showed that Rhapontigenin diminished lamellipodia formation at the leading edge of cells. Finally, Rhapontigenin decreased the phosphorylation of phosphoinisitide-3-kinase (PI3K) and AKT. Rac1 activity was inhibited by the PI3K inhibitor wortmannin. Taken together, these results suggest that Rhapontigenin suppresses breast cancer cell migration and invasion, which is involved in inhibiting the PI3K-dependent Rac1 signaling pathway. Rhapontigenin converted from rhapontin purified from Rheum undulatum enhances the inhibition of melanin synthesis. PUMID/DOI:23221688 Biosci Biotechnol Biochem. 2012;76(12):2307-9. Rhapontigenin was produced from rhapontin isolated from a methanol extract of Rheum undulatum roots by enzymatic transformation. Rhapontin and Rhapontigenin exhibited dose-dependent inhibition of tyrosinase activity and melanin synthesis in B16F10 melanoma cells, but the inhibitory activity of Rhapontigenin was greater than that of rhapontin. Thus the bioconversion of rhapontin enhanced its ability to inhibit cellular tyrosinase activity and melanin synthesis. Rhapontigenin inhibited hypoxia inducible factor 1 alpha accumulation and angiogenesis in hypoxic PC-3 prostate cancer cells PUMID/DOI:21628883 Biol Pharm Bull. 2011;34(6):850-5. The inhibitory mechanism of Rhapontigenin isolated from Vitis coignetiae was investigated on HIF-1α stability and angiogenesis in human prostate cancer PC-3 cells. Rhapontigenin significantly suppressed HIF-1α accumulation at protein level but not at mRNA level in PC-3 cells under hypoxia. Also, Rhapontigenin suppressed hypoxia-induced HIF-1α activation in various cancer cells, such as colorectal adenocarcinoma (SW620), breast adenocarcinoma (MCF-7), fibrosarcoma (HT-1080) and prostate carcinoma (LNCaP). Interestingly, Rhapontigenin had more potency in inhibition of hypoxia-induced HIF-1α expression than that of resveratrol, a known HIF-1α inhibitor. In addition, Rhapontigenin promoted hypoxia-induced HIF-1α degradation and cycloheximide (CHX) blocked protein synthesis. A prolyl hydroxylase (PHD) inhibitor dimethyloxalylglycine (DMOG) is usually utilized to examine whether prolyl hydroxylation is involved in inhibition of HIF-1α accumulation. Here, DMOG recovered HIF-1α accumulation inhibited by Rhapontigenin. Immunoprecipitation assay also revealed that rhapotigenin enhanced the binding of hydroxylated HIF-1α to von Hippel-Lindau (VHL) tumor suppressor protein. Furthermore, Rhapontigenin reduced vascular endothelial growth factor (VEGF) secretion in hypoxic PC-3 cells as well as suppressed tube formation in human umbilical vein endothelial cells (HUVECs) treated by the conditioned media of hypoxic PC-3 cells. However, anti-angiogenic effect of Rhapontigenin in hypoxic PC-3 cells was reversed by DMOG. Taken together, these findings suggest that Rhapontigenin inhibits HIF-1α accumulation and angiogenesis in PC-3 prostate cancer cells.