Emodin / TumCI 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)

Rank Pathway / Target Axis Direction Label Primary Effect Notes / Cancer Relevance Ref
1 Reactive oxygen species (ROS) ↑ ROS Driver Upstream cytotoxic trigger Emodin induces ROS in cancer cells; ROS increase is positioned upstream of mitochondrial dysfunction and death signaling. (ref)
2 Mitochondrial integrity (ΔΨm) ↓ ΔΨm Driver Mitochondrial dysfunction Emodin decreases mitochondrial membrane potential (ΔΨm), consistent with mitochondria-dependent killing. (ref)
3 Intrinsic apoptosis (caspase cascade) ↑ apoptosis (↑ caspases / ↑ PARP cleavage) Driver Execution-phase cell death Emodin activates caspase-dependent apoptosis with mitochondrial involvement in colon cancer models. (ref)
4 AMPK → AKT/mTOR axis ↑ AMPK / ↓ AKT-mTOR signaling Secondary Growth/metabolic suppression NSCLC study reports AMPK activation with inhibition of AKT/mTOR alongside apoptosis and ROS increase (consistent directionality). (ref)
5 NF-κB signaling ↓ NF-κB activation (↓ p65 nuclear translocation; ↓ IκBα phosphorylation/degradation) Secondary Reduced pro-survival/inflammatory transcription Emodin inhibits TNF-α–induced NF-κB activation by blocking IκBα phosphorylation/degradation and p65 nuclear activity. (ref)
6 STAT3 signaling ↓ STAT3 activation (↓ phosphorylation) Secondary Reduced survival/proliferation signaling HCC study shows emodin suppresses STAT3 activation (and discusses upstream kinase modulation), supporting directionality as STAT3↓. (ref)
7 HIF-1α hypoxia program ↓ HIF-1α (↓ biosynthesis; not via transcription/stability) Adaptive Reduced hypoxia tolerance Pancreatic cancer study: emodin decreases HIF-1α by decreasing biosynthesis (explicit mechanism stated). (ref)
8 Aerobic glycolysis (Warburg output) ↓ glycolysis (↓ ECAR / ↓ glycolytic dependence) Phenotypic Metabolic suppression Renal cancer paper reports emodin inhibits aerobic glycolysis (and links killing to a non-apoptotic death mode in that model). (ref)
9 HDAC inhibition (epigenetic enzyme activity) ↓ HDAC activity Secondary Epigenetic modulation Direct biochemical evidence: emodin inhibits HDAC activity in vitro (fast-on/slow-off kinetics reported). (ref)
10 NRF2 / HO-1 antioxidant response ↑ NRF2 / ↑ HO-1 (context-dependent stress response) Adaptive Counter-response to redox stress HCC model reports emodin increases NRF2 and HO-1 expression; interpret as adaptive/compensatory (not necessarily the cytotoxic driver). (ref)


TumCI, Tumor Cell invasion: Click to Expand ⟱
Source:
Type:
Tumor cell invasion is a critical process in cancer progression and metastasis, where cancer cells spread from the primary tumor to surrounding tissues and distant organs. This process involves several key steps and mechanisms:

1.Epithelial-Mesenchymal Transition (EMT): Many tumors originate from epithelial cells, which are typically organized in layers. During EMT, these cells lose their epithelial characteristics (such as cell-cell adhesion) and gain mesenchymal traits (such as increased motility). This transition is crucial for invasion.

2.Degradation of Extracellular Matrix (ECM): Tumor cells secrete enzymes, such as matrix metalloproteinases (MMPs), that degrade the ECM, allowing cancer cells to invade surrounding tissues. This degradation facilitates the movement of cancer cells through the tissue.

3.Cell Migration: Once the ECM is degraded, cancer cells can migrate. They often use various mechanisms, including amoeboid movement and mesenchymal migration, to move through the tissue. This migration is influenced by various signaling pathways and the tumor microenvironment.

4.Angiogenesis: As tumors grow, they require a blood supply to provide nutrients and oxygen. Tumor cells can stimulate the formation of new blood vessels (angiogenesis) through the release of growth factors like vascular endothelial growth factor (VEGF). This not only supports tumor growth but also provides a route for cancer cells to enter the bloodstream.

5.Invasion into Blood Vessels (Intravasation): Cancer cells can invade nearby blood vessels, allowing them to enter the circulatory system. This step is crucial for metastasis, as it enables cancer cells to travel to distant sites in the body.

6.Survival in Circulation: Once in the bloodstream, cancer cells must survive the immune response and the shear stress of blood flow. They can form clusters with platelets or other cells to evade detection.

7.Extravasation and Colonization: After traveling through the bloodstream, cancer cells can exit the circulation (extravasation) and invade new tissues. They may then establish secondary tumors (metastases) in distant organs.

8.Tumor Microenvironment: The surrounding microenvironment plays a significant role in tumor invasion. Factors such as immune cells, fibroblasts, and signaling molecules can either promote or inhibit invasion and metastasis.
Scientific Papers found: Click to Expand⟱
1319- EMD,    Emodin treatment of papillary thyroid cancer cell lines in vitro inhibits proliferation and enhances apoptosis via downregulation of NF‑κB and its upstream TLR4 signaling
- in-vitro, Thyroid, TPC-1 - in-vitro, Thyroid, IHH4
NF-kB↓, TLR4↓, TumCI↓, TumCMig↓,
1247- EMD,    Emodin exerts antitumor effects in ovarian cancer cell lines by preventing the development of cancer stem cells via epithelial mesenchymal transition
- vitro+vivo, Ovarian, SKOV3 - in-vitro, Ovarian, A2780S
TumCP↓, TumCMig↓, TumCI↓, EMT↓, N-cadherin↓, Vim↓, E-cadherin↑, TumCG↓, CD133↓, OCT4↓, CSCs↓,

Showing Research Papers: 1 to 2 of 2

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 2

Pathway results for Effect on Cancer / Diseased Cells:


Proliferation, Differentiation & Cell State ⓘ

CD133↓, 1,   CSCs↓, 1,   EMT↓, 1,   OCT4↓, 1,   TumCG↓, 1,  

Migration ⓘ

E-cadherin↑, 1,   N-cadherin↓, 1,   TumCI↓, 2,   TumCMig↓, 2,   TumCP↓, 1,   Vim↓, 1,  

Immune & Inflammatory Signaling ⓘ

NF-kB↓, 1,   TLR4↓, 1,  
Total Targets: 13

Pathway results for Effect on Normal Cells:


Total Targets: 0

Scientific Paper Hit Count for: TumCI, Tumor Cell invasion
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#:324  State#:%  Dir#:1
  wNotes=0  sortOrder:rid,rpid

 

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