Emodin / ROS Cancer Research Results

EMD, Emodin: Click to Expand ⟱
Features:
Organic compound isolated from rhubarb, buckthorn, knotweed. It has laxative, anticancer, antibacterial, antiinflammatory, and antiviral activities, and is used in traditional Chinese medicine.
Emodin, an anthraquinone derivative found in various plants (e.g., rhubarb, Polygonum cuspidatum).

Pathways:
- Generation of Reactive Oxygen Species (ROS)
- Upregulation Bax downregulation of Bcl‑2, caspase activation and cyt_c release.
- Induce cell cycle arrest at various checkpoints (commonly G0/G1 or G2/M phases.
- Can inhibit NF‑κB activation
– MAPK Pathways
– PI3K/Akt Pathway
- Metalloproteinases (MMPs)

-ic50 cancer cells 10-50uM, normal cells higher(supports a therapeutic window)

Rhubarb species Common name Plant part analyzed Emodin content Aloe-emodin content Interpretation
Rheum palmatum Chinese rhubarb Dried root and rhizome Approximately 1.1–2.0 mg/g Approximately 0.65–1.0 mg/g Major medicinal source; concentrations vary considerably with origin, plant age, processing, and extraction method.
Rheum officinale Medicinal rhubarb Dried root and rhizome Usually approximately 0.5–2 mg/g Usually approximately 0.5–2 mg/g Composition broadly resembles R. palmatum; some samples contain more aloe-emodin than emodin.
Rheum tanguticum Tangut rhubarb Root and rhizome; smaller amounts occur in aerial tissues Moderate to high; commonly approximately 1–3 mg/g in underground tissues Moderate; commonly below emodin One of the three principal Chinese medicinal rhubarb species. Tissue distribution differs, and some aerial tissues may contain appreciable emodin.
Rheum australe
syn. Rheum emodi		 Himalayan or Indian rhubarb Root and rhizome Present and frequently a major anthraquinone Present, generally lower and more variable Reported concentrations vary widely among wild populations; quantitative results are not directly comparable across extraction methods.
Rheum rhabarbarum / Rheum × hybridum Garden or culinary rhubarb Root and rhizome; edible petiole contains much less Low to moderate in roots; usually trace or low in petioles Low or trace in petioles; variable in roots Edible stalks are not compositionally equivalent to medicinal rhubarb roots. Most anthraquinones occur in underground tissues.

In rhubarb, the medicinal material described as “root and rhizome” includes both the true roots and the thick underground stem base from which the leaf stalks emerge.



Emodin — Emodin is a naturally occurring hydroxyanthraquinone and plant secondary metabolite, chemically identified as 1,3,8-trihydroxy-6-methylanthraquinone. It is a small-molecule natural product rather than an approved anticancer drug. Major sources include rhubarb species, Japanese knotweed, buckthorn, Polygonum multiflorum, Polygonum cuspidatum, Rheum palmatum, and several fungi. Emodin is pharmacologically pleiotropic, with redox-active, kinase-modulating, anti-inflammatory, cytotoxic, laxative, and antimicrobial properties. Its anticancer effects remain predominantly preclinical, and emodin should be distinguished from the related compounds aloe-emodin and rhein.

Primary mechanisms (ranked):

  1. Induction of oxidative stress and mitochondrial dysfunction, producing ROS accumulation, mitochondrial membrane depolarization, cytochrome-c release, and caspase-dependent apoptosis.
  2. Suppression of PI3K/AKT/mTOR and related survival signaling, frequently accompanied by AMPK activation, reduced protein synthesis, metabolic stress, and apoptosis.
  3. Modulation of BAX/BCL-2-family proteins and activation of intrinsic and, in some models, extrinsic apoptotic pathways.
  4. Cell-cycle arrest through context-dependent modulation of p53, p21, ATM, cyclins, CDKs, and checkpoint proteins.
  5. Inhibition of NF-κB, STAT3, TLR4, JAK, MAPK, HER2, CK2, and other pro-survival or inflammatory signaling pathways.
  6. Suppression of glycolysis and anabolic metabolism through reduced GLUT1, HK2, PKM2, LDHA, FASN, and AKT/mTOR activity in selected cancer models.
  7. Inhibition of invasion, epithelial–mesenchymal transition, angiogenesis, and cancer-stem-cell phenotypes through reduced MMPs, HIF-1α, VEGF, TGF-β, CXCR4, and mesenchymal signaling.
  8. Induction of autophagy, ER stress, DNA-damage responses, or necroptosis in model-dependent settings.
  9. NRF2/HO-1 activation as a secondary, context-dependent antioxidant response that may protect normal cells but can also oppose emodin-induced cytotoxic oxidative stress.
  10. Chemosensitization through inhibition of survival, resistance, stemness, cholesterol-metabolism, or drug-efflux pathways; the interaction is drug- and tumor-dependent.

Bioavailability / PK relevance: Native emodin has very poor oral bioavailability, estimated at approximately 3% in rat studies. It has low aqueous solubility, incomplete intestinal absorption, extensive intestinal and hepatic glucuronidation and sulfation, and rapid systemic clearance. Circulating exposure is therefore dominated by conjugated metabolites rather than sustained concentrations of free emodin. Nanoparticles, liposomes, phospholipid complexes, prodrugs, and other delivery systems are being investigated but are not established clinical formulations.

In-vitro vs systemic exposure relevance: Most anticancer experiments use approximately 10–100 µM emodin, commonly 20–50 µM. These free-drug concentrations are unlikely to be maintained systemically after conventional oral administration because of poor absorption and rapid conjugation. In-vitro findings therefore substantially overstate the exposure achievable with unformulated oral emodin. Local gastrointestinal exposure may be higher, but this does not establish therapeutically useful tumor exposure.

Clinical evidence status: Preclinical. Evidence consists primarily of cancer-cell studies and rodent xenograft or chemically induced tumor models. Emodin has shown experimental adjunct and chemosensitizing effects with agents including paclitaxel, sorafenib, cisplatin, gemcitabine, and other therapies, but there is no established randomized clinical evidence supporting emodin as a cancer treatment. Emodin is not an FDA-, EMA-, or Health Canada-approved anticancer agent.

Safety: Emodin is not necessarily tumor-selective and can produce ROS, mitochondrial injury, apoptosis, and genotoxic signals in nonmalignant cells at sufficient concentrations. Preclinical literature reports possible hepatotoxicity, nephrotoxicity, reproductive toxicity, gastrointestinal irritation, laxative effects, and complex mutagenicity findings, particularly with high doses or prolonged exposure. It may also affect CYP enzymes, conjugating enzymes, transporters, and the pharmacokinetics of co-administered drugs. Long-term concentrated supplementation should not be considered equivalent to ordinary dietary exposure from rhubarb or other foods.


Mechanistic Profile of Emodin

Rank Pathway / Axis Cancer Cells Normal Cells TSF Primary Effect Notes / Interpretation
1 ROS-driven mitochondrial injury ↑ ROS
↓ mitochondrial membrane potential
↓ ATP		 ↑ ROS and mitochondrial injury at cytotoxic exposure P–R Upstream cytotoxic stress A central mechanism in many cancer models, but not intrinsically cancer-specific. Redox outcome varies with dose, cell type, antioxidant capacity, and exposure duration.
2 Intrinsic mitochondrial apoptosis ↑ BAX
↓ BCL-2 and BCL-XL
↑ cytochrome-c
↑ caspase-9 and caspase-3
↑ PARP cleavage		 ↑ apoptosis at high concentration or prolonged exposure R–G Programmed cell death Frequently follows ROS accumulation and mitochondrial depolarization. Extrinsic Fas and caspase-8 signaling also contributes in some models.
3 PI3K AKT mTOR and AMPK signaling ↓ PI3K
↓ AKT
↓ mTOR
↑ AMPK (context-dependent)		 Mixed or tissue-protective modulation (context-dependent) R–G Reduced survival and anabolic signaling Mechanistically important across several tumor types, although AMPK activation is not universal and may differ by metabolic state.
4 Cell-cycle checkpoints and DNA-damage response ↑ ATM
↑ p53
↑ p21
↓ cyclin D1, cyclin E, or cyclin B1
↓ CDK activity		 Cell-cycle disturbance possible at cytotoxic exposure G G0/G1, S-phase, or G2/M arrest The arrest point is cell-line and dose-dependent. Emodin should not be assigned to one universal checkpoint.
5 NF-κB TLR4 inflammatory survival signaling ↓ TLR4
↓ IKK activation
↓ IκBα degradation
↓ NF-κB nuclear activity		 ↓ inflammatory signaling in many injury models R–G Reduced survival, inflammation, and treatment resistance This axis contributes to both anticancer and anti-inflammatory effects and may reduce cytokine-driven tumor support.
6 JAK STAT3 and receptor kinase signaling ↓ JAK1 and JAK2
↓ STAT3
↓ HER2
↓ CK2 or Src signaling (model-dependent)		 Mixed; possible inhibition of physiological kinase signaling R–G Reduced proliferation and anti-apoptotic transcription Direct and indirect kinase effects have been reported, but target dominance varies substantially among tumor models.
7 Glycolysis and metabolic dependency ↓ GLUT1
↓ HK2
↓ PKM2
↓ LDHA
↓ ECAR
↓ glycolysis		 PKM2 and metabolic modulation reported (context-dependent) R–G Energy stress and reduced biosynthetic capacity Prominent in selected renal and hepatic cancer models but not yet established as a universal primary mechanism.
8 HIF-1α VEGF angiogenic program ↓ HIF-1α biosynthesis
↓ VEGF
↓ angiogenesis		 Potential impairment of physiological hypoxic adaptation at sufficient exposure G Reduced hypoxia tolerance and vascular support Evidence includes reduced HIF-1α protein synthesis rather than exclusively altered transcription or degradation.
9 EMT invasion and extracellular-matrix remodeling ↑ E-cadherin
↓ N-cadherin
↓ vimentin
↓ MMP2 and MMP9
↓ TGF-β signaling		 Possible modulation of wound repair and fibrosis pathways G Reduced migration, invasion, and metastatic phenotype Effects may involve tumor cells, macrophages, stromal signaling, and cancer-stem-cell maintenance.
10 Cancer stemness and differentiation state ↓ CD133
↓ OCT4
↓ NOTCH1
↓ stem-cell formation		 Effects on normal progenitor populations are insufficiently characterized G Reduced tumor initiation and recurrence-associated phenotype Supported primarily by cell and animal models; clinically meaningful selectivity has not been established.
11 Autophagy ER stress and necroptosis ↑ autophagy
↑ ER stress or ↓ ER stress (model-dependent)
↑ RIP1 and MLKL signaling in selected models		 Protective or toxic depending on tissue and exposure R–G Alternative stress-response and death pathways Autophagy can facilitate death or survival. Necroptosis has been demonstrated in selected renal cancer models but should not be generalized.
12 NRF2 HO-1 antioxidant response ↑ NRF2
↑ HO-1 (secondary; context-dependent)		 ↑ NRF2-mediated antioxidant and cytoprotective signaling R–G Compensatory antioxidant response NRF2 activation may limit oxidative injury in normal tissues but could also reduce emodin cytotoxicity or support resistant cancer cells. It is not consistently the primary anticancer mechanism.
13 HDAC and chromatin regulation ↓ HDAC activity
↑ histone acetylation		 Epigenetic modulation possible R–G Altered transcriptional state Biochemical HDAC inhibition is reported, but the free concentrations required and its contribution in vivo remain uncertain.
14 Chemosensitization ↑ chemotherapy sensitivity
↓ survival and resistance pathways		 Potential ↑ normal-tissue toxicity or altered drug disposition G Enhanced response to selected anticancer agents Reported combinations are promising preclinically, but interactions cannot be assumed beneficial because emodin also affects metabolism, transport, redox balance, and normal-cell viability.
15 Clinical Translation Constraint ↓ free systemic exposure
↑ conjugated metabolites
heterogeneous tumor response		 Dose-limiting gastrointestinal and organ toxicity concerns G Limited translation of in-vitro activity Approximately 3% oral bioavailability in rat studies, extensive glucuronidation and sulfation, poor solubility, short exposure, absence of validated clinical dosing, and lack of randomized oncology trials are major limitations.

P: 0–30 min    R: 30 min–3 hr    G: >3 hr
ROS, Reactive Oxygen Species: Click to Expand ⟱
Source: HalifaxProj (inhibit)
Type:
Reactive oxygen species (ROS) are highly reactive molecules that contain oxygen and can lead to oxidative stress in cells. They play a dual role in cancer biology, acting as both promoters and suppressors of cancer.
ROS can cause oxidative damage to DNA, leading to mutations that may contribute to cancer initiation and progression. So normally you want to inhibit ROS to prevent cell mutations.
However excessive ROS can induce apoptosis (programmed cell death) in cancer cells, potentially limiting tumor growth. Chemotherapy typically raises ROS.
-mitochondria is the main source of reactive oxygen species (ROS) (and the ETC is heavily related)
ROS Homeostasis in Cancer Cells and Its Potential as a Therapeutic Target

"Reactive oxygen species (ROS) are two electron reduction products of oxygen, including superoxide anion, hydrogen peroxide, hydroxyl radical, lipid peroxides, protein peroxides and peroxides formed in nucleic acids 1. They are maintained in a dynamic balance by a series of reduction-oxidation (redox) reactions in biological systems and act as signaling molecules to drive cellular regulatory pathways."
"During different stages of cancer formation, abnormal ROS levels play paradoxical roles in cell growth and death 8. A physiological concentration of ROS that maintained in equilibrium is necessary for normal cell survival. Ectopic ROS accumulation promotes cell proliferation and consequently induces malignant transformation of normal cells by initiating pathological conversion of physiological signaling networks. Excessive ROS levels lead to cell death by damaging cellular components, including proteins, lipid bilayers, and chromosomes. Therefore, both scavenging abnormally elevated ROS to prevent early neoplasia and facilitating ROS production to specifically kill cancer cells are promising anticancer therapeutic strategies, in spite of their contradictoriness and complexity."
"ROS are the collection of derivatives of molecular oxygen that occur in biology, which can be categorized into two types, free radicals and non-radical species. The non-radical species are hydrogen peroxide (H 2O 2 ), organic hydroperoxides (ROOH), singlet molecular oxygen ( 1 O 2 ), electronically excited carbonyl, ozone (O3 ), hypochlorous acid (HOCl, and hypobromous acid HOBr). Free radical species are super-oxide anion radical (O 2•−), hydroxyl radical (•OH), peroxyl radical (ROO•) and alkoxyl radical (RO•) [130]. Any imbalance of ROS can lead to adverse effects. H2 O 2 and O 2 •− are the main redox signalling agents. The cellular concentration of H2 O 2 is about 10−8 M, which is almost a thousand times more than that of O2 •−".
"Radicals are molecules with an odd number of electrons in the outer shell [393,394]. A pair of radicals can be formed by breaking a chemical bond or electron transfer between two molecules."

Recent investigations have documented that polyphenols with good antioxidant activity may exhibit pro-oxidant activity in the presence of copper ions, which can induce apoptosis in various cancer cell lines but not in normal cells. "We have shown that such cell growth inhibition by polyphenols in cancer cells is reversed by copper-specific sequestering agent neocuproine to a significant extent whereas iron and zinc chelators are relatively ineffective, thus confirming the role of endogenous copper in the cytotoxic action of polyphenols against cancer cells. Therefore, this mechanism of mobilization of endogenous copper." > Ions could be one of the important mechanisms for the cytotoxic action of plant polyphenols against cancer cells and is possibly a common mechanism for all plant polyphenols. In fact, similar results obtained with four different polyphenolic compounds in this study, namely apigenin, luteolin, EGCG, and resveratrol, strengthen this idea.
Interestingly, the normal breast epithelial MCF10A cells have earlier been shown to possess no detectable copper as opposed to breast cancer cells [24], which may explain their resistance to polyphenols apigenin- and luteolin-induced growth inhibition as observed here (Fig. 1). We have earlier proposed [25] that this preferential cytotoxicity of plant polyphenols toward cancer cells is explained by the observation made several years earlier, which showed that copper levels in cancer cells are significantly elevated in various malignancies. Thus, because of higher intracellular copper levels in cancer cells, it may be predicted that the cytotoxic concentrations of polyphenols required would be lower in these cells as compared to normal cells."

Majority of ROS are produced as a by-product of oxidative phosphorylation, high levels of ROS are detected in almost all cancers.
-It is well established that during ER stress, cytosolic calcium released from the ER is taken up by the mitochondrion to stimulate ROS overgeneration and the release of cytochrome c, both of which lead to apoptosis.

Note: Products that may raise ROS can be found using this database, by:
Filtering on the target of ROS, and selecting the Effect Direction of ↑

Targets to raise ROS (to kill cancer cells):
• NADPH oxidases (NOX): NOX enzymes are involved in the production of ROS.
    -Targeting NOX enzymes can increase ROS levels and induce cancer cell death.
    -eNOX2 inhibition leads to a high NADH/NAD⁺ ratio which can lead to increased ROS
• Mitochondrial complex I: Inhibiting can increase ROS production
• P53: Activating p53 can increase ROS levels(by inducing the expression of pro-oxidant genes)
• Nrf2 inhibition: regulates the expression of antioxidant genes. Inhibiting Nrf2 can increase ROS levels
• Glutathione (GSH): an antioxidant. Depleting GSH can increase ROS levels
• Catalase: Catalase converts H2O2 into H2O+O. Inhibiting catalase can increase ROS levels
• SOD1: converts superoxide into hydrogen peroxide. Inhibiting SOD1 can increase ROS levels
• PI3K/AKT pathway: regulates cell survival and metabolism. Inhibiting can increase ROS levels
• HIF-1α inhibition: regulates genes involved in metabolism and angiogenesis. Inhibiting HIF-1α can increase ROS
• Glycolysis: Inhibiting glycolysis can increase ROS levels • Fatty acid oxidation: Cancer cells often rely on fatty acid oxidation for energy production.
-Inhibiting fatty acid oxidation can increase ROS levels
• ER stress: Endoplasmic reticulum (ER) stress can increase ROS levels
• Autophagy: process by which cells recycle damaged organelles and proteins.
-Inhibiting autophagy can increase ROS levels and induce cancer cell death.
• KEAP1/Nrf2 pathway: regulates the expression of antioxidant genes.
    -Inhibiting KEAP1 or activating Nrf2 can increase ROS levels and induce cancer cell death.
• DJ-1: regulates the expression of antioxidant genes. Inhibiting DJ-1 can increase ROS levels
• PARK2: regulates the expression of antioxidant genes. Inhibiting PARK2 can increase ROS levels
• SIRT1 inhibition:regulates the expression of antioxidant genes. Inhibiting SIRT1 can increase ROS levels
• AMPK activation: regulates energy metabolism and can increase ROS levels when activated.
• mTOR inhibition: regulates cell growth and metabolism. Inhibiting mTOR can increase ROS levels
• HSP90 inhibition: regulates protein folding and can increase ROS levels when inhibited.
• Proteasome: degrades damaged proteins. Inhibiting the proteasome can increase ROS levels
• Lipid peroxidation: a process by which lipids are oxidized, leading to the production of ROS.
    -Increasing lipid peroxidation can increase ROS levels
• Ferroptosis: form of cell death that is regulated by iron and lipid peroxidation.
    -Increasing ferroptosis can increase ROS levels
• Mitochondrial permeability transition pore (mPTP): regulates mitochondrial permeability.
    -Opening the mPTP can increase ROS levels
• BCL-2 family proteins: regulate apoptosis and can increase ROS levels when inhibited.
• Caspase-independent cell death: a form of cell death that is regulated by ROS.
    -Increasing caspase-independent cell death can increase ROS levels
• DNA damage response: regulates the repair of DNA damage. Increasing DNA damage can increase ROS
• Epigenetic regulation: process by which gene expression is regulated.
    -Increasing epigenetic regulation can increase ROS levels

-PKM2, but not PKM1, can be inhibited by direct oxidation of cysteine 358 as an adaptive response to increased intracellular reactive oxygen species (ROS)

ProOxidant Strategy:(inhibit the Mevalonate Pathway (likely will also inhibit GPx)
-HydroxyCitrate (HCA) found as supplement online and typically used in a dose of about 1.5g/day or more
-Atorvastatin typically 40-80mg/day, -Dipyridamole typically 200mg 2x/day Combined effect research
-Lycopene typically 100mg/day range (note debatable as it mainly lowers NRF2)

Dual Role of Reactive Oxygen Species and their Application in Cancer Therapy 
ROS-Inducing Interventions in Cancer — Canonical + Mechanistic Reference
-generated from AI and Cancer database
ROS rating:  +++ strong | ++ moderate | + weak | ± mixed | 0 none
NRF2:        ↓ suppressed | ↑ activated | ± mixed | 0 none
Conditions:  [D] dose  [Fe] metal  [M] metabolic  [O₂] oxygen
             [L] light [F] formulation [T] tumor-type [C] combination




Item ROS↑ NRF2 Condition Mechanism Class Remarks 



ROS">Piperlongumine
+++ ↓ [D][T] ROS-dominant






ROS">Shikonin
+++↓/±[D][T]ROS-dominant






ROS">Vitamin K3 (menadione)
+++↓[D]ROS-dominant






ROS">Copper (ionic / nano)
+++↓[Fe][F]ROS-dominant






ROS">Sodium Selenite
+++↓[D]ROS-dominant






ROS">Juglone
+++↓[D]ROS-dominant






ROS">Auranofin
+++↓[D]ROS-dominant






ROS">Photodynamic Therapy (PDT)
+++0[L][O₂]ROS-dominant






ROS">Radiotherapy / Radiation
+++0[O₂]ROS-dominant






ROS">Doxorubicin
+++↓[D]ROS-dominant






ROS">Cisplatin
++↓[D][T]ROS-dominant






ROS">Salinomycin
++↓[D][T]ROS-dominant






ROS">Artemisinin / DHA
++↓[Fe][T]ROS-dominant






ROS">Sulfasalazine
++↓[C][T]ROS-dominant






ROS">FMD / fasting
++↓[M][C][O₂]ROS-dominant






ROS">Vitamin C (pharmacologic)
++↓[Fe][D]ROS-dominant






ROS">Silver nanoparticles
++±[F][D]ROS-dominant






ROS">Gambogic acid
++↓[D][T]ROS-dominant






ROS">Parthenolide
++↓[D][T]ROS-dominant






ROS">Plumbagin
++↓[D]ROS-dominant






ROS">Allicin
++↓[D]ROS-dominant






ROS">Ashwagandha (Withaferin A)
++↓[D][T]ROS-dominant






ROS">Berberine
++↓[D][M]ROS-dominant






ROS">PEITC
++↓[D][C]ROS-dominant






ROS">Methionine restriction
+↓[M][C][T]ROS-secondary






ROS">DCA
+±[M][T]ROS-secondary






ROS">Capsaicin
+±[D][T]ROS-secondary






ROS">Galloflavin
+0[D]ROS-secondary






ROS">Piperine
+±[D][F]ROS-secondary






ROS">Propyl gallate
+↓[D]ROS-secondary






ROS">Scoulerine
+?[D][T]ROS-secondary






ROS">Thymoquinone
±±[D][T]Dual redox






ROS">Emodin
±±[D][T]Dual redox






ROS">Alpha-lipoic acid (ALA)
±↑[D][M]NRF2-dominant






ROS">Curcumin
±↑/↓[D][F]NRF2-dominant






ROS">EGCG
±↑/↓[D][O₂]NRF2-dominant






ROS">Quercetin
±↑/↓[D][Fe]NRF2-dominant






ROS">Resveratrol
±↑[D][M]NRF2-dominant






ROS">Sulforaphane
±↑↑[D]NRF2-dominant






ROS">Lycopene
0↑—Antioxidant






ROS">Rosmarinic acid
0↑—Antioxidant






ROS">Citrate
00—Neutral


Scientific Papers found: Click to Expand⟱
6816- EMD,    Emodin attenuates Alzheimer's disease by activating the protein kinase C signaling pathway
- in-vivo, AD, NA
*cognitive↑, *Aβ↓, *p‑PKCδ↑, *ROS↓,
6817- EMD,    Emodin inhibits aggregation of amyloid-β peptide 1–42 and improves cognitive deficits in Alzheimer's disease transgenic mice
- in-vivo, AD, NA
*Aβ↓, *tau↓, *ROS↓, *Inflam↓, *cognitive↑,
6818- EMD,    Emodin Rescued Hyperhomocysteinemia-Induced Dementia and Alzheimer's Disease-Like Features in Rats
- in-vivo, AD, NA
*Aβ↓, *p‑tau↓, *PP2A↑, *cAMP↑, *5LO↓, *IL6↓, *TNF-α↓, *ROS↓, *DNMT1↓,
6819- EMD,    Recent advances in the therapeutic potential of emodin for human health
- Review, Nor, NA
AntiCan↑, *AntiDiabetic↑, *neuroP↑, *Inflam↓, *antiOx↑, *BioAv↓, *BioAv↑, *SOD↑, *GPx↑, *GSH↑, *NRF2↑, *ROS↓, *lipid-P↓, *Cyt‑c↓, *BAX↓, *Bcl-2↓, *iNOS↓, *NO↓, *IL6↓, *IL10↓, *IL17↓, *IFN-γ↓, *NF-kB↓, *LC3II↓, *Akt↓, *Beclin-1↓, *AMPK↓, *TNF-α↓, *PGE2↓, *Apoptosis↓, *Casp3↓, *Casp9↓, *P53↓, *P21↓, *NAD↓, *ATP↓, *CHOP/DDIT3↓, *GADD34↓, *ATF4↓, tumCV↓, Apoptosis↑, TumCG↓, TumCI↓, TumMeta↓, CSCs↓, NOTCH1↓, STAT3↓, eff↑, miR-34a↓, *neuroP↑, *BDNF↓, *hepatoP↑, *ALAT↓, *AST↓, TG/TAG↓, ROS↑, Slug↓, EMT↓, Glycolysis↓, ChemoSen↑, P-gp↓, Ki-67↓, PCNA↓, ER Stress↑, TRIB3↑, NF-kB↑, TumMeta↑, *Imm↓, *toxicity↝,
6820- EMD,    The Health Benefits of Emodin, a Natural Anthraquinone Derived from Rhubarb—A Summary Update
- Review, Nor, NA - Review, Arthritis, NA - Review, AD, NA
*diuretic↑, *Bacteria↓, *Inflam↓, AntiCan↑, TumCP↓, TumCI↓, angioG↓, *toxicity↓, IFN-γ↑, IL12↑, ROS↑, TNF-α↓, TNF-α↓, TGF-β↓, MAPK↓, PKCδ↓, NF-kB↓, HER2/EBBR2↓, VEGF↓, DNAdam↑, Necroptosis↑, Glycolysis↓, GLUT1↓, PI3K↓, Akt↓, Casp9↑, Casp3↑, BAX↑, Bcl-2↓, eff↑, MMP2↓, MMP9↓, eff↑, ChemoSen↑, P-gp↓, SREBP2↓, eff↑, *other↝, *COX2↓, *Hif1a↓, *HDAC↓, *tau↓, *PKCδ↑, *ROS↓, *Inflam↓, AntiAg?,
6821- EMD,    Emodin derivatives as promising multi-aspect intervention agents for amyloid aggregation: molecular docking/dynamics simulation, bioactivities evaluation, and cytoprotection
- Study, AD, NA
*ROS↓, *Aβ↓,
6824- EMD,    Neuroprotective, Anti-Inflammatory and Antifibrillogenic Offerings by Emodin against Alzheimer’s Dementia: A Systematic Review
- Review, AD, NA
*Inflam?, *antiOx↑, *tau↓, *Aβ↓, *neuroP↑, *ROS↓, *memory↑, *cognitive↑, *other↝, *AChE↓, *BACE↓, *LC3II↓, *Beclin-1↓, *p‑tau↓, *CREB↑, *HNE↓, *BioAv↓, *BioAv↝, *BioAv↑, *BioAv↑, *BioAv↑, *BioAv↑, BioAv↑, *HO-1↑, *PKCδ↑, *Akt↑, *NLRP3↓, *NF-kB↓, *TLR3↓,
6827- EMD,    Mechanism of Emodin in the Treatment of Rheumatoid Arthritis
- Review, Arthritis, NA
*ALAT↓, *AST↓, *ROS↓, *cardioP↑, *TNF-α↓, *NF-kB↓, *Inflam↓, *AntiArt↑, *PGE2↓, *MMP3↓, *MMP13↓, *COX2↓, *AntiCan↑, *neuroP↑, *hepatoP↑,
6828- EMD,    Neuroprotective effect of emodin against Alzheimer's disease via Nrf2 signaling in U251 cells and APP/PS1 mice
- in-vitro, AD, U251
*MMP↑, *ROS↓, *NRF2↑, *HO-1↑, *SOD↑, *Bcl-2↑, *Catalase↑, *BAX↓, *memory↑, *ANXi↓, *Aβ↓, *antiOx↑, *MDA↓,
6836- EMD,    Emodin and the Anthraquinone Scaffold: Therapeutic Promise and Strategies to Overcome Translational Barriers
- Review, Nor, NA
*antiOx↑, *neuroP↑, *Inflam↓, *hepatoP↑, AntiTum↑, *Bacteria↓, *diuretic↑, *AntiDiabetic↑, *BioAv↝, *NF-kB↓, *AMPK↑, *JAK↓, *STAT3↓, *ROS↓, *lipid-P↓, ROS↑, TumCCA↑, CycB/CCNB1↓, BAX↑, Bcl-2↓, MOMP↑, Cyt‑c↑, Casp9↑, Casp3↑, Casp7↑, Apoptosis↑, P53↑,
2422- EMD,    Anti-Cancer Effects of Emodin on HepG2 Cells as Revealed by 1H NMR Based Metabolic Profiling
- in-vitro, HCC, HepG2
HK2↓, PKM2↓, LDHA↓, Glycolysis↓, TumCCA↑, ROS↓, glut↓, Hif1a↓,

Showing Research Papers: 1 to 11 of 11

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 11

Pathway results for Effect on Cancer / Diseased Cells:


Redox & Oxidative Stress(tgid=1) ⓘ

ROS↓, 1,   ROS↑, 3,  

Core Metabolism/Glycolysis(tgid=4) ⓘ

glut↓, 1,   Glycolysis↓, 3,   HK2↓, 1,   LDHA↓, 1,   PKM2↓, 1,   SREBP2↓, 1,  

Cell Death(tgid=5) ⓘ

Akt↓, 1,   Apoptosis↑, 2,   BAX↑, 2,   Bcl-2↓, 2,   Casp3↑, 2,   Casp7↑, 1,   Casp9↑, 2,   Cyt‑c↑, 1,   MAPK↓, 1,   MOMP↑, 1,   Necroptosis↑, 1,  

Kinase & Signal Transduction(tgid=6) ⓘ

HER2/EBBR2↓, 1,  

Transcription & Epigenetics(tgid=7) ⓘ

tumCV↓, 1,  

Protein Folding & ER Stress(tgid=8) ⓘ

ER Stress↑, 1,  

DNA Damage & Repair(tgid=10) ⓘ

DNAdam↑, 1,   P53↑, 1,   PCNA↓, 1,  

Cell Cycle & Senescence(tgid=11) ⓘ

CycB/CCNB1↓, 1,   TumCCA↑, 2,  

Proliferation, Differentiation & Cell State(tgid=12) ⓘ

CSCs↓, 1,   EMT↓, 1,   miR-34a↓, 1,   NOTCH1↓, 1,   PI3K↓, 1,   STAT3↓, 1,   TumCG↓, 1,  

Migration(tgid=13) ⓘ

AntiAg?, 1,   Ki-67↓, 1,   MMP2↓, 1,   MMP9↓, 1,   PKCδ↓, 1,   Slug↓, 1,   TGF-β↓, 1,   TRIB3↑, 1,   TumCI↓, 2,   TumCP↓, 1,   TumMeta↓, 1,   TumMeta↑, 1,  

Angiogenesis & Vasculature(tgid=14) ⓘ

angioG↓, 1,   Hif1a↓, 1,   VEGF↓, 1,  

Barriers & Transport(tgid=15) ⓘ

GLUT1↓, 1,   P-gp↓, 2,  

Immune & Inflammatory Signaling(tgid=16) ⓘ

IFN-γ↑, 1,   IL12↑, 1,   NF-kB↓, 1,   NF-kB↑, 1,   TNF-α↓, 2,  

Drug Metabolism & Resistance(tgid=21) ⓘ

BioAv↑, 1,   ChemoSen↑, 2,   eff↑, 4,  

Clinical Biomarkers(tgid=22) ⓘ

HER2/EBBR2↓, 1,   Ki-67↓, 1,   TG/TAG↓, 1,   TRIB3↑, 1,  

Functional Outcomes(tgid=23) ⓘ

AntiCan↑, 2,   AntiTum↑, 1,  
Total Targets: 65

Pathway results for Effect on Normal Cells:


NA, unassigned(tgid=0) ⓘ

AntiArt↑, 1,   diuretic↑, 2,  

Redox & Oxidative Stress(tgid=1) ⓘ

antiOx↑, 4,   Catalase↑, 1,   GPx↑, 1,   GSH↑, 1,   HNE↓, 1,   HO-1↑, 2,   lipid-P↓, 2,   MDA↓, 1,   NRF2↑, 2,   ROS↓, 10,   SOD↑, 2,  

Mitochondria & Bioenergetics(tgid=3) ⓘ

ATP↓, 1,   MMP↑, 1,  

Core Metabolism/Glycolysis(tgid=4) ⓘ

ALAT↓, 2,   AMPK↓, 1,   AMPK↑, 1,   cAMP↑, 1,   CREB↑, 1,   NAD↓, 1,  

Cell Death(tgid=5) ⓘ

Akt↓, 1,   Akt↑, 1,   Apoptosis↓, 1,   BAX↓, 2,   Bcl-2↓, 1,   Bcl-2↑, 1,   Casp3↓, 1,   Casp9↓, 1,   Cyt‑c↓, 1,   GADD34↓, 1,   iNOS↓, 1,  

Transcription & Epigenetics(tgid=7) ⓘ

other↝, 2,  

Protein Folding & ER Stress(tgid=8) ⓘ

CHOP/DDIT3↓, 1,  

Autophagy & Lysosomes(tgid=9) ⓘ

Beclin-1↓, 2,   LC3II↓, 2,  

DNA Damage & Repair(tgid=10) ⓘ

DNMT1↓, 1,   P53↓, 1,  

Cell Cycle & Senescence(tgid=11) ⓘ

P21↓, 1,  

Proliferation, Differentiation & Cell State(tgid=12) ⓘ

HDAC↓, 1,   STAT3↓, 1,  

Migration(tgid=13) ⓘ

5LO↓, 1,   MMP13↓, 1,   MMP3↓, 1,   PKCδ↑, 2,   p‑PKCδ↑, 1,  

Angiogenesis & Vasculature(tgid=14) ⓘ

ATF4↓, 1,   Hif1a↓, 1,   NO↓, 1,  

Immune & Inflammatory Signaling(tgid=16) ⓘ

COX2↓, 2,   IFN-γ↓, 1,   IL10↓, 1,   IL17↓, 1,   IL6↓, 2,   Imm↓, 1,   Inflam?, 1,   Inflam↓, 6,   JAK↓, 1,   NF-kB↓, 4,   PGE2↓, 2,   TLR3↓, 1,   TNF-α↓, 3,  

Synaptic & Neurotransmission(tgid=18) ⓘ

AChE↓, 1,   BDNF↓, 1,   tau↓, 3,   p‑tau↓, 2,  

Protein Aggregation(tgid=19) ⓘ

Aβ↓, 6,   BACE↓, 1,   NLRP3↓, 1,   PP2A↑, 1,  

Drug Metabolism & Resistance(tgid=21) ⓘ

BioAv↓, 2,   BioAv↑, 5,   BioAv↝, 2,  

Clinical Biomarkers(tgid=22) ⓘ

ALAT↓, 2,   AST↓, 2,   IL6↓, 2,  

Functional Outcomes(tgid=23) ⓘ

AntiCan↑, 1,   AntiDiabetic↑, 2,   ANXi↓, 1,   cardioP↑, 1,   cognitive↑, 3,   hepatoP↑, 3,   memory↑, 2,   neuroP↑, 5,   toxicity↓, 1,   toxicity↝, 1,  

Infection & Microbiome(tgid=24) ⓘ

Bacteria↓, 2,  
Total Targets: 87

Scientific Paper Hit Count for: ROS, Reactive Oxygen Species
11 Emodin
Query results interpretion may depend on "conditions" listed in the research papers.
Such Conditions may include : 
  -low or high Dose
  -format for product, such as nano of lipid formations
  -different cell line effects
  -synergies with other products 
  -if effect was for normal or cancerous cells

Filter Conditions: Pro/AntiFlg:%  IllCat:%  CanType:%  Cells:%  prod#:75  Target#:275  State#:%  Dir#:1
  wNotes=0  sortOrder:rid,rpid

 

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