Betulinic acid / TumCI Cancer Research Results

BetA, Betulinic acid: Click to Expand ⟱
Features:
Betulinic acid "buh-TOO-li-nik acid" is a natural compound with antiretroviral, anti malarial, anti-inflammatory and anticancer properties. It is found in the bark of several plants, such as white birch, ber tree and rosemary, and has a complex mode of action against tumor cells.
-Betulinic acid is a naturally occurring pentacyclic triterpenoid
-vitro concentrations range from 1–100 µM, in vivo studies in rodents have generally used doses from 10–100 mg/kg
Precursor: Betulin, via oxidation at C-28
Lipophilicity: High (poor aqueous solubility)

Betulinic acid — Betulinic acid is a naturally occurring lupane-type pentacyclic triterpenoid with broad experimental anticancer activity, especially against melanoma, neuroectodermal, glioma, breast, colorectal, and other solid-tumor models. It is a natural-product small molecule, usually abbreviated BA or BetA, and is found in several plants, classically birch bark, with semi-synthesis commonly starting from betulin. A distinguishing feature is preferential induction of tumor-cell death through direct mitochondrial injury with relative sparing of many non-neoplastic cells in preclinical systems. Its main translational limitation is very poor aqueous solubility with correspondingly weak oral/systemic developability unless formulation or derivatization is used.

Primary mechanisms (ranked):

  1. Direct mitochondrial membrane permeabilization with intrinsic apoptosis activation
  2. Mitochondrial ROS increase with collapse of mitochondrial membrane potential and cytochrome c release
  3. ER-stress and unfolded-protein-response activation, including GRP78-linked stress signaling
  4. Suppression of NF-κB and other pro-survival transcriptional programs, including Sp-family signaling in some models
  5. Cell-cycle arrest with reduced cyclin/CDK signaling
  6. Anti-migratory and anti-invasive effects via EMT, FAK, ROCK1, MMP, and cytoskeletal remodeling pathways
  7. Secondary metabolic suppression of aerobic glycolysis and hypoxia-response signaling in susceptible models
  8. Adjunct sensitization to chemo- or radiotherapy in selected preclinical settings

Bioavailability / PK relevance: Betulinic acid is highly lipophilic and poorly water-soluble, which strongly limits oral absorption and systemic exposure. PK behavior is formulation-dependent, and much of the translational literature focuses on nanoparticles, liposomes, micelles, conjugates, or topical delivery rather than conventional oral dosing.

In-vitro vs systemic exposure relevance: Many in-vitro anticancer studies use low-to-mid micromolar concentrations, which are often difficult to reproduce reliably in vivo with unformulated parent betulinic acid. Accordingly, mechanistic findings are useful biologically, but direct concentration matching to standard oral/systemic use is often poor unless enhanced-delivery systems are used.

Clinical evidence status: Strong preclinical and formulation-development literature; very limited human oncology evidence. Cancer-facing clinical development appears to remain early-phase/topical, with orphan designation for topical metastatic melanoma but no FDA approval for that indication. Betulinic acid itself is not an established approved anticancer drug.

-half-life reports vary 3-5 hrs?. Reported half-life varies by formulation and species; several studies report multi-hour systemic persistence.
BioAv -hydrophobic molecule with relatively poor water solubility. 
Main Cancer action
-Direct mitochondrial targeting in cancer cells
-Minimal effect on normal cells

Key pathways
-Mitochondrial membrane permeabilization
-ROS-mediated apoptosis
-Caspase-independent death

Chemo relevance: Generally compatible, Not a redox buffer

Pathways:
- often induce ROS production
- ROS↑ related: MMP↓(ΔΨm), ER Stress↑, UPR↑, GRP78↑, Ca+2↑, Cyt‑c↑, Caspases↑, DNA damage↑, cl-PARP↑, HSP↓
- Lowers AntiOxidant defense in Cancer Cells(Often associated with reduced redox buffering capacity in tumor cells (e.g., GSH depletion); NRF2 direction model-dependent.): NRF2↓, SOD↓, GSH↓
- May Raise AntiOxidant defense in Normal Cells: NRF2↑, SOD↑, GSH↑, Catalase↑ Reports suggest relative sparing of normal cells and preservation of antioxidant capacity in some models
- lowers Inflammation : NF-kB↓(typ), COX2↓, p38↓ (context-dependent; often stress-activated), Pro-Inflammatory Cytokines : IL-1β↓, TNF-α↓, IL-6↓, IL-8↓
- inhibit Growth/Metastases : , MMPs↓, MMP2↓, MMP9↓, TIMP2, IGF-1↓, VEGF↓, ROCK1↓, FAK↓, NF-κB↓, TGF-β↓, α-SMA↓, ERK↓
- reactivate genes thereby inhibiting cancer cell growth : P53↑, HSP↓(model-dependent), Sp proteins↓,
- cause Cell cycle arrest : TumCCA↑, cyclin D1↓, CDK2↓, CDK4↓,
- inhibits Migration/Invasion : TumCMig↓, TumCI↓, FAK↓, ERK↓, EMT↓, TOP1↓,
- inhibits glycolysis (secondary to mitochondrial stress) ATP depletion : HIF-1α↓, PKM2↓, cMyc↓, GLUT1↓, LDH↓, LDHA↓, HK2↓, PFKs↓, PDKs↓, HK2↓, ECAR↓, GRP78↑(ER stress), GlucoseCon↓
- inhibits angiogenesis↓ : VEGF↓, HIF-1α↓, EGFR↓,
- inhibits Cancer Stem Cells in some studies : CSC↓, GLi1↓, β-catenin↓, OCT4↓,
- Others: PI3K↓(typ), AKT↓(typ), JAK↓, STAT↓, β-catenin↓, AMPK↓(AMPK is often activated during metabolic stress), ERK↓, JNK,
- Synergies: chemo-sensitization, chemoProtective, RadioSensitizer, Others(review target notes), Neuroprotective, Cognitive, Renoprotection, Hepatoprotective, CardioProtective,
- Selectivity: Cancer Cells vs Normal Cells

Mechanistic profile

Rank Pathway / Axis Cancer Cells Normal Cells TSF Primary Effect Notes / Interpretation
1 Mitochondrial permeabilization ↑ MOMP, ↓ ΔΨm, ↑ cytochrome c release, ↑ apoptosis ↔ / milder effect P-R Core tumor-selective death trigger Best-supported central mechanism; helps explain activity in apoptosis-competent but therapy-resistant tumors.
2 Mitochondrial ROS increase ↑ ROS ↔ / possible antioxidant sparing (context-dependent) P-R Amplifies mitochondrial stress and death signaling ROS appears mechanistically relevant in many tumor models, but not every study makes it the dominant initiating event.
3 Caspase axis and caspase-independent death ↑ caspase-9, ↑ caspase-3, ↑ PARP cleavage; caspase-independent death also reported ↔ R-G Executes apoptosis after mitochondrial injury BA can still kill some tumor cells when classical caspase execution is partly blocked, indicating non-canonical death contribution.
4 ER stress / UPR / GRP78 ↑ ER stress, ↑ UPR, ↑ GRP78 stress signaling ↔ R-G Links proteostatic stress to apoptosis and metastasis suppression Especially relevant in breast and gastric cancer models; may also connect to metabolic suppression and chemosensitization.
5 NF-κB survival signaling ↓ NF-κB ↔ / ↓ inflammatory tone R-G Reduces survival, inflammatory, and resistance programs Common downstream convergence node across several tumor types.
6 Cell-cycle machinery ↓ cyclin D1, ↓ CDK2, ↓ CDK4, ↑ cell-cycle arrest ↔ G Slows proliferation Usually supportive rather than primary; often follows stress and survival-pathway disruption.
7 EMT / invasion / matrix remodeling ↓ EMT, ↓ FAK, ↓ ROCK1, ↓ MMP2, ↓ MMP9, ↓ migration, ↓ invasion ↔ G Antimetastatic effect Consistent with reduced motility and invasive phenotype in multiple solid-tumor models.
8 Glycolysis ↓ glucose uptake, ↓ lactate, ↓ ECAR, ↓ HK2, ↓ PKM2, ↓ LDHA ↔ G Secondary metabolic suppression Not the universal initiating mechanism; appears important in selected breast-cancer and GRP78-linked systems.
9 HIF-1α hypoxia axis ↓ HIF-1α, ↓ VEGF, ↓ GLUT1, ↓ PDK1 ↔ G Reduces hypoxic adaptation and angiogenic drive Relevant in hypoxic tumor biology and helps explain antiangiogenic/metabolic effects in some models.
10 NRF2 / antioxidant buffering ↓ NRF2 or ↓ redox buffering (model-dependent) ↔ / possible preservation of antioxidant tone (context-dependent) R-G May widen tumor redox vulnerability Direction is not uniform across all models; safer to treat this as contextual rather than universally core.
11 Ca²⁺ stress ↑ Ca²⁺ (context-dependent) ↔ P-R Supports organelle stress and apoptotic signaling Usually part of the broader mitochondrial/ER stress network rather than a stand-alone primary target.
12 Radiosensitization or Chemosensitization ↑ sensitivity to radiation or selected drugs Unclear G Adjunct leverage Preclinical evidence supports additive or sensitizing effects with irradiation and with some chemotherapy settings, but this is not yet clinically established.
13 Clinical Translation Constraint Poor solubility and limited systemic exposure constrain reproducibility Same formulation constraint G Delivery bottleneck Main barrier is not lack of mechanistic richness but drug-like exposure; translation currently depends heavily on formulation, derivatization, or topical/local use.

Time-Scale Flag (TSF): P / R / G

  • P: 0–30 min (primary/physical-chemical effects; rapid kinase/redox signaling)
  • R: 30 min–3 hr (acute redox and stress-response activation)
  • G: >3 hr (gene-regulatory adaptation and phenotypic outcomes)
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⟱
2757- BetA,    Betulinic Acid Inhibits Glioma Progression by Inducing Ferroptosis Through the PI3K/Akt and NRF2/HO-1 Pathways
- in-vitro, GBM, U251
tumCV↓, BA reduced viability; inhibited colony formation, migration, and invasion; and triggered apoptosis.
TumCMig↓,
TumCI↓,
Apoptosis↑,
p‑PI3K↓, BA administration decreased the levels of phosphorylated PI3K and AKT.
p‑Akt↓,
Ferroptosis↑, BA-induced ferroptosis and HO-1 and NRF2 levels were increased
HO-1↑,
NRF2↑,

5591- BetA,    Advances and challenges in betulinic acid therapeutics and delivery systems for breast cancer prevention and treatment
- Review, BC, NA
BioAv↓, However, its poor water solubility limits its optimal therapeutic potential.
BioAv↑, nano-drug delivery systems (NDDSs) have gained significant attention as a method to substantially improve low solubility and poor drug bioavailability, enhance targeted drug delivery, and reduce side effects.
selectivity↑, reviews by Simone Fulda23,24 strengthened BA's potential for cancer treatment and prevention, particularly its ability to selectively trigger apoptosis in cancer cells while causing minimal harm to normal cells.
eff↑, It is important to note that the anticancer effects of BA on different types of tumors are more potent at a pH lower than 6.8.34
angioG↓, figure 3
*antiOx↑,
*Inflam↓,
MMP↓, BA-induced mitochondrial depolarization
Bcl-2↓, BA treatment has been shown to lower Bcl-2 expression and increase Bax, resulting in the activation of caspase-9 and caspase-3 through the mitochondrial pathway.63
BAX↑,
Casp9↑,
Casp3↑,
GRP78/BiP?, BA directly targets GRP78, triggering ER stress by activating the PERK-eIF2α-CHOP apoptotic cascade
ER Stress↑,
PERK↑,
CHOP↑,
ChemoSen↑, BA's ability to chemosensitize BC cells to taxanes highlights its importance in situations of drug resistance
SESN2↑, Under hypoxia, BA strongly increases SESN2 expression.
ROS↑, Reducing SESN2 levels enhances BA-induced ROS production, DNA damage, and radiosensitivity, while decreasing autophagic flux, indicating that SESN2-mediated autophagy serves as a protective adaptive response.68
MOMP↓, decreases the mitochondrial outer membrane potential (MOMP),
MAPK↑, This leads to the activation of p38 Mitogen-activated protein kinase (p38 MAPK), the release of cytochrome C, apoptosis-inducing factor (AIF),
Cyt‑c↑,
AIF↑,
STAT3↓, BA suppresses the signal transducer and activator of transcription (STAT) 3 signaling pathways
FAK↓, BA's inhibition of STAT3, as well as FAK, leads to decreased expression of MMPs and elevated TIMP-2, thereby impairing cancer cell migration and invasion
TIMP2↑,
TumCMig↓,
TumCI↓,
Sp1/3/4↓, Sp inhibition reduces cancer gene expression, inhibiting cancer cell growth.
TumCCA↑, It increases cell numbers in the G2/M phase, leading to cell cycle arrest.
DNAdam↑, causes DNA damage, thereby inhibiting the progression and invasion of cancer cells.

2729- BetA,    Betulinic acid in the treatment of tumour diseases: Application and research progress
- Review, Var, NA
ChemoSen↑, Betulinic acid can increase the sensitivity of cancer cells to other chemotherapy drugs
mt-ROS↑, BA has antitumour activity, and its mechanisms of action mainly include the induction of mitochondrial oxidative stress
STAT3↓, inhibition of signal transducer and activator of transcription 3 and nuclear factor-κB signalling pathways.
NF-kB↓,
selectivity↑, A main advantage of BA and its derivatives is that they are cytotoxic to different human tumour cells, while cytotoxicity is much lower in normal cells.
*toxicity↓, It can kill cancer cells but has no obvious effect on normal cells and is also nontoxic to other organs in xenograft mice at a dose of 500 mg/kg
eff↑, BA combined with chemotherapy drugs, such as platinum and mithramycin A, can induce apoptosis in tumour cells
GRP78/BiP↑, In animal xenograft tumour models, BA enhanced the expression of glucose-regulated protein 78 (GRP78)
MMP2↓, reduced the levels of matrix metalloproteinases (MMPs), such as MMP-2 and MMP-9, in lung metastatic lesions of breast cancer, indicating that BA can reduce the invasiveness of breast cancer in vivo and block epithelial mesenchymal transformation (EMT
P90RSK↓,
TumCI↓,
EMT↓,
MALAT1↓, MALAT1, a lncRNA, was downregulated in hepatocellular carcinoma (HCC) cells treated with BA in vivo,
Glycolysis↓, Suppressing aerobic glycolysis of cancer cells by GRP78/β-Catenin/c-Myc signalling pathways
AMPK↑, activating AMPK signaling pathway
Sp1/3/4↓, inhibiting Sp1. BA at 20 mg/kg/d, the tumour volume and weight were significantly reduced, and the expression levels of Sp1, Sp3, and Sp4 in tumour tissues were lower than those in control mouse tissues
Hif1a↓, Suppressing the hypoxia-induced accumulation of HIF-1α and expression of HIF target genes
angioG↓, PC3: Having anti-angiogenesis effect
NF-kB↑, LNCaP, DU145 — Inducing apoptosis and NF-κB pathway
NF-kB↓, U266 — Inhibiting NF-κB pathway.
MMP↓, BA produces ROS and reduces mitochondrial membrane potential; the mitochondrial permeability transition pore of the mitochondrial membrane plays an important role in apoptosis signal transduction.
Cyt‑c↑, Mitochondria release cytochrome C and increase the levels of Caspase-9 and Caspase-3, inducing cell apoptosis.
Casp9↑,
Casp3↑,
RadioS↑, BA could be a promising drug for increasing radiosensitization in oral squamous cell carcinoma radiotherapy.
PERK↑, BA treatment increased the activation of the protein kinase RNA-like endoplasmic reticulum kinase (PERK)/C/EBP homologous protein (CHOP) apoptosis pathway and decreased the expression of Sp1.
CHOP↑,
*toxicity↓, BA at a concentration of 50 μg/ml did not inhibit the growth of normal peripheral blood lymphocytes, indicating that the toxicity of BA was at least 1000 times less than that of doxorubicin

2719- BetA,    Betulinic Acid Restricts Human Bladder Cancer Cell Proliferation In Vitro by Inducing Caspase-Dependent Cell Death and Cell Cycle Arrest, and Decreasing Metastatic Potential
- in-vitro, CRC, T24/HTB-9 - in-vitro, Bladder, UMUC3 - in-vitro, Bladder, 5637
TumCD↑, BA induced cell death in bladder cancer cells and that are accompanied by apoptosis, necrosis, and cell cycle arrest.
Apoptosis↑,
TumCCA↑,
CycB/CCNB1↓, BA decreased the expression of cell cycle regulators, such as cyclin B1, cyclin A, cyclin-dependent kinase (Cdk) 2, cell division cycle (Cdc) 2, and Cdc25c
cycA1/CCNA1↓,
CDK2↓,
CDC25↓,
mtDam↑, BA-induced apoptosis was associated with mitochondrial dysfunction that is caused by loss of mitochondrial membrane potential, which led to the activation of mitochondrial-mediated intrinsic pathway.
BAX↑, BA up-regulated the expression of Bcl-2-accociated X protein (Bax) and cleaved poly-ADP ribose polymerase (PARP), and subsequently activated caspase-3, -8, and -9.
cl‑PARP↑,
Casp3↑,
Casp8↑,
Casp9↑,
Snail↓, decreased the expression of Snail and Slug in T24 and 5637 cells, and matrix metalloproteinase (MMP)-9 in UMUC-3 cells.
Slug↓,
MMP9↓,
selectivity↑, Among the bladder cancer cell lines, 5637 cells were much more sensitive to BA than T24 or UMUC-3 cells under the same conditions. However, BA does not affect cell growth in normal cell lines including RAW 264.7
MMP↓, BA Induces Loss of Mitochondrial Membrane Potential (MMP, ΔΨm) in Human Bladder Cancer Cells
ROS∅, As a result, we found that BA did not affect intracellular ROS levels in all three bladder cancer cells. In addition, BA-induced cell viability inhibition was not restored by NAC pre-treatment
TumCMig↓, BA Decreases Migration and Invasion of Human Bladder Cancer Cells
TumCI↓,

2742- BetA,    Betulinic acid impairs metastasis and reduces immunosuppressive cells in breast cancer models
- in-vitro, BC, MDA-MB-231 - in-vivo, BC, 4T1 - in-vitro, BC, MCF-7
tumCV↓, BA decreased the viability of three breast cancer cell lines and markedly impaired cell migration and invasion
TumCMig↓,
TumCI↓,
STAT3↑, BA could inhibit the activation of stat3 and FAK which resulted in a reduction of matrix metalloproteinases (MMPs)
FAK↓,
MMPs↓,
MMP2↓, BA treatment decreased the expression of MMP-2 and MMP-9 while increased the expression of TIMP-2 in 4T1 and MDA-MB-231 cells.
MMP9↓,
TIMP2↑,

2741- BetA,    Betulinic acid triggers apoptosis and inhibits migration and invasion of gastric cancer cells by impairing EMT progress
- in-vitro, GC, SNU16 - in-vitro, GC, NCI-N87 - in-vivo, NA, NA
TumCG↓, BA had significant cytotoxic and inhibitory effects on GC cells in a dose- and time-dependent manner.
TumCMig↓, BA inhibited the migratory and invasive abilities of SNU-16 cells
TumCI↓,
N-cadherin↓, relative expression level of N-cadherin in SNU-16 cells was drastically down-regulated, and the expression of E-cadherin in SNU-16 cells was distinctly up-regulated in comparison to that in the control group, implying a break in the EMT process.
E-cadherin↑,
EMT↓,
Ki-67↓, proportions of Ki-67-positive and MMP2-positive cells were significantly lower in the tumour sections of the BA-treated group than those in the sections of the control group
MMP2↓,

2738- BetA,    Betulinic Acid Suppresses Breast Cancer Metastasis by Targeting GRP78-Mediated Glycolysis and ER Stress Apoptotic Pathway
- in-vitro, BC, MDA-MB-231 - in-vitro, BC, BT549 - in-vivo, NA, NA
TumCI↓, BA inhibited invasion and migration of highly aggressive breast cancer cells.
TumCMig↓,
Glycolysis↓, Moreover, BA could suppress aerobic glycolysis of breast cancer cells presenting as a reduction of lactate production, quiescent energy phenotype transition, and downregulation of aerobic glycolysis-related proteins.
lactateProd↓, lactate production in both MDA-MB-231 and BT-549 cells was significantly reduced following BA administration
GRP78/BiP↑, (GRP78) was also identified as the molecular target of BA in inhibiting aerobic glycolysis. BA treatment led to GRP78 overexpression, and GRP78 knockdown abrogated the inhibitory effect of BA on glycolysis.
ER Stress↑, Further studies demonstrated that overexpressed GRP78 activated the endoplasmic reticulum (ER) stress sensor PERK.
PERK↑,
p‑eIF2α↑, Subsequent phosphorylation of eIF2α led to the inhibition of β-catenin expression, which resulted in the inhibition of c-Myc-mediated glycolysis.
β-catenin/ZEB1↓,
cMyc↓, These findings suggested that BA inhibited the β-catenin/c-Myc pathway by interrupting the binding between GRP78 and PERK and ultimately suppressed the glycolysis of breast cancer cells.
ROS↑, (i) the induction of cancer cell apoptosis via the mitochondrial pathway induced by the release of soluble factors or generation of reactive oxygen species (ROS)
angioG↓, (ii) the inhibition of angiogenesis [24];
Sp1/3/4↓, (iii) the degradation of transcription factor specificity protein 1 (Sp1)
DNAdam↑, (iv) the induction of DNA damage by suppressing topoisomerase I
TOP1↓,
TumMeta↓, BA Inhibits Metastasis of Highly Aggressive Breast Cancer Cells
MMP2↓, BA significantly decreased the expression of MMP-2 and MMP-9 secreted by breast cancer cells
MMP9↓,
N-cadherin↓, BA downregulated the levels of N-cadherin and vimentin as the mesenchymal markers, while increased E-cadherin which is an epithelial marker (Figure 2(c)), validating the EMT inhibition effects of BA in breast cancer cells.
Vim↓,
E-cadherin↑,
EMT↓,
LDHA↓, the levels of glycolytic enzymes, including LDHA and p-PDK1/PDK1, were all decreased in a dose-dependent manner by BA
p‑PDK1↓,
PDK1↓,
ECAR↓, extracellular acidification rate (ECAR), which reflects the glycolysis activity, was retarded following BA administration.
OCR↓, oxygen consumption rate (OCR), which is a marker of mitochondrial respiration, was also decreased simultaneously
Hif1a↓, BA could reduce prostate cancer angiogenesis via inhibiting the HIF-1α/stat3 pathway [39]
STAT3↓,


Showing Research Papers: 1 to 7 of 7

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 7

Pathway results for Effect on Cancer / Diseased Cells:


Redox & Oxidative Stress ⓘ

Ferroptosis↑, 1,   HO-1↑, 1,   NRF2↑, 1,   ROS↑, 2,   ROS∅, 1,   mt-ROS↑, 1,  

Mitochondria & Bioenergetics ⓘ

AIF↑, 1,   CDC25↓, 1,   MMP↓, 3,   mtDam↑, 1,   OCR↓, 1,  

Core Metabolism/Glycolysis ⓘ

AMPK↑, 1,   cMyc↓, 1,   ECAR↓, 1,   Glycolysis↓, 2,   lactateProd↓, 1,   LDHA↓, 1,   PDK1↓, 1,   p‑PDK1↓, 1,  

Cell Death ⓘ

p‑Akt↓, 1,   Apoptosis↑, 2,   BAX↑, 2,   Bcl-2↓, 1,   Casp3↑, 3,   Casp8↑, 1,   Casp9↑, 3,   Cyt‑c↑, 2,   Ferroptosis↑, 1,   MAPK↑, 1,   MOMP↓, 1,   TumCD↑, 1,  

Kinase & Signal Transduction ⓘ

Sp1/3/4↓, 3,  

Transcription & Epigenetics ⓘ

tumCV↓, 2,  

Protein Folding & ER Stress ⓘ

CHOP↑, 2,   p‑eIF2α↑, 1,   ER Stress↑, 2,   GRP78/BiP?, 1,   GRP78/BiP↑, 2,   PERK↑, 3,  

Autophagy & Lysosomes ⓘ

SESN2↑, 1,  

DNA Damage & Repair ⓘ

DNAdam↑, 2,   cl‑PARP↑, 1,  

Cell Cycle & Senescence ⓘ

CDK2↓, 1,   cycA1/CCNA1↓, 1,   CycB/CCNB1↓, 1,   TumCCA↑, 2,  

Proliferation, Differentiation & Cell State ⓘ

EMT↓, 3,   P90RSK↓, 1,   p‑PI3K↓, 1,   STAT3↓, 3,   STAT3↑, 1,   TOP1↓, 1,   TumCG↓, 1,  

Migration ⓘ

E-cadherin↑, 2,   FAK↓, 2,   Ki-67↓, 1,   MALAT1↓, 1,   MMP2↓, 4,   MMP9↓, 3,   MMPs↓, 1,   N-cadherin↓, 2,   Slug↓, 1,   Snail↓, 1,   TIMP2↑, 2,   TumCI↓, 7,   TumCMig↓, 6,   TumMeta↓, 1,   Vim↓, 1,   β-catenin/ZEB1↓, 1,  

Angiogenesis & Vasculature ⓘ

angioG↓, 3,   Hif1a↓, 2,  

Immune & Inflammatory Signaling ⓘ

NF-kB↓, 2,   NF-kB↑, 1,  

Drug Metabolism & Resistance ⓘ

BioAv↓, 1,   BioAv↑, 1,   ChemoSen↑, 2,   eff↑, 2,   RadioS↑, 1,   selectivity↑, 3,  

Clinical Biomarkers ⓘ

Ki-67↓, 1,  
Total Targets: 80

Pathway results for Effect on Normal Cells:


Redox & Oxidative Stress ⓘ

antiOx↑, 1,  

Immune & Inflammatory Signaling ⓘ

Inflam↓, 1,  

Functional Outcomes ⓘ

toxicity↓, 2,  
Total Targets: 3

Scientific Paper Hit Count for: TumCI, Tumor Cell invasion
7 Betulinic acid
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#:42  Target#:324  State#:%  Dir#:%
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