Luteolin / HDAC Cancer Research Results

LT, Luteolin: Click to Expand ⟱

Features:

Luteolin a Flavonoid found in celery, parsley, broccoli, onion leaves, carrots, peppers, cabbages, apple skins, and chrysanthemum flowers.
-MDR1 expression, MMP-9, IGF-1 and Epithelial to mesenchymal transition.

Luteolin — a naturally occurring polyhydroxylated flavone (3′,4′,5,7-tetrahydroxyflavone) found in celery, parsley, peppers, broccoli and numerous medicinal plants. It is a dietary phytochemical and experimental small-molecule anticancer/anti-inflammatory agent rather than an approved anticancer drug. Standard abbreviation: LUT or Lut. Luteolin occurs as the free aglycone and as plant glycosides; after oral administration, circulating luteolin is dominated by glucuronide and sulfate conjugates rather than free aglycone. Its cancer pharmacology is pleiotropic and strongly model-dependent, with particularly recurrent effects on PI3K/AKT/mTOR, NF-κB, STAT3, redox regulation, mitochondrial apoptosis, EMT/invasion and cell-cycle control.

Primary mechanisms (ranked):

PI3K/AKT/mTOR survival signaling suppression, reducing proliferation and facilitating apoptosis, autophagy or other programmed cell-death responses.
Redox-selective stress modulation: commonly ↑ ROS in susceptible cancer cells together with ↓ NRF2/HO-1/GSH-associated antioxidant defenses, while frequently reducing oxidative stress and activating protective antioxidant systems in normal tissues.
NF-κB and inflammatory survival signaling inhibition, with context-dependent suppression of TNF-α, IL-6, COX-2 and related inflammatory mediators.
Mitochondrial/intrinsic apoptosis activation through ↓ mitochondrial membrane potential, ↑ BAX:BCL-2 ratio, cytochrome-c release and caspase activation.
STAT3/JAK signaling suppression, reducing survival, stemness, inflammatory signaling and immune-evasion phenotypes in several tumor models.
EMT, migration and invasion suppression through modulation of E-cadherin, N-cadherin, vimentin, MMP2/MMP9, FAK, YAP/TAZ and related pathways.
Cell-cycle arrest through suppression of cyclins/CDKs and context-dependent induction of p21/p27 and p53 signaling.
Metabolic and hypoxic adaptation inhibition, including HIF-1α, PKM2, HK2 and glycolytic signaling in selected models.
Epigenetic modulation, including reported inhibition of DNMTs, HDAC-associated signaling and EZH2 in selected cancer models.
Additional context-dependent cell-death mechanisms including ER stress, autophagy, ferroptosis and pyroptosis.

Bioavailability / PK relevance: Oral luteolin has poor aqueous solubility and unfavorable systemic availability of unconjugated aglycone. It is absorbed from the intestine but undergoes extensive intestinal and hepatic glucuronidation and sulfation. Animal studies report low absolute bioavailability of free luteolin, commonly in the low-single-digit to low-tens percentage range depending on formulation and analytical definition. Nanoemulsions, lipid/phospholipid systems, cyclodextrins, nanoparticles and other delivery systems can substantially improve exposure experimentally. Luteolin and particularly some circulating conjugates can interact with OATP1B1/OATP2B1 transporters; in-vitro CYP inhibition has also been reported, making pharmacokinetic drug interactions plausible at sufficiently high exposure.

In-vitro vs systemic exposure relevance: Many anticancer experiments use approximately 10–100 µM luteolin, often 20–50 µM or higher. These concentrations generally exceed sustained concentrations of free luteolin expected after conventional oral dietary or supplemental dosing because extensive conjugation limits circulating aglycone. Consequently, direct translation of many cell-culture IC50 values to standard oral supplementation is weak. Local gastrointestinal exposure, metabolites, tissue deconjugation and optimized formulations may partly alter this limitation.

Clinical evidence status: Predominantly preclinical, but no longer exclusively preclinical. A 2025 single-arm phase I study administered luteolin 50 mg/day for six months to five men with localized prostate cancer undergoing active surveillance; no treatment-related adverse events were reported, but the study was far too small and uncontrolled to establish anticancer efficacy. A larger phase II single-arm multicenter Japanese study of 50 mg/day for one year is currently recruiting with a planned enrollment of 40 patients. Luteolin is therefore best categorized as early-human/phase I–II investigational evidence, not established cancer therapy. Preclinical evidence for chemotherapy and radiotherapy sensitization is substantial but remains cancer-, drug- and genotype-dependent.

-Note half-life 2–3 hours
BioAv low, but could be improved with Res, or blend of castor oil, kolliphor and polyethylene glycol
Pathways:
- induce ROS production in cancer cell but a few reports of reduction. Always seems to reduce ROS in normal cells.
- ROS↑ related: MMP↓(ΔΨm), ER Stress↑, UPR↑, GRP78↑, Ca+2↑, Cyt‑c↑, Caspases↑, DNA damage↑, cl-PARP↑, HSP↓
- Lowers AntiOxidant defense in Cancer Cells: NRF2↓, SOD↓, GSH↓ Catalase↓ HO1↓ GPx↓
- Raises AntiOxidant defense in Normal Cells: ROS↓, NRF2↑, SOD↑, GSH↑, Catalase↑,
- lowers Inflammation : NF-kB↓, COX2↓, p38↓, Pro-Inflammatory Cytokines : IL-1β↓, TNF-α↓, IL-6↓,
- inhibit Growth/Metastases : TumMeta↓, TumCG↓, EMT↓, MMP2↓, MMP9↓, TIMP2, IGF-1↓, VEGF↓, FAK↓, RhoA↓, NF-κB↓, CXCR4↓, ERK↓
- reactivate genes thereby inhibiting cancer cell growth : HDAC↓, DNMT1↓, DNMT3A↓, EZH2↓, P53↑, HSP↓,
- cause Cell cycle arrest : TumCCA↑, cyclin D1↓, cyclin E↓, CDK2↓, CDK4↓, CDK6↓,
- inhibits Migration/Invasion : TumCMig↓, FAK↓, ERK↓, EMT↓, TOP1↓, TET1↓,
- inhibits glycolysis and ATP depletion : HIF-1α↓, PKM2↓, cMyc↓, LDHA↓, HK2↓, GRP78↑,
- inhibits angiogenesis↓ : VEGF↓, HIF-1α↓, Notch↓, PDGF↓, EGFR↓, Integrins↓,
- Others: PI3K↓, AKT↓, STAT↓, Wnt↓, β-catenin↓, AMPK, ERK↓, JNK, TrxR**, - Shown to modulate the nuclear translocation of SREBP-2 (related to cholesterol).
- Synergies: chemo-sensitization, chemoProtective, RadioSensitizer, Others(review target notes), Neuroprotective, Renoprotection, Hepatoprotective, CardioProtective,

- Selectivity: Cancer Cells vs Normal Cells

-"Additionally, when reacted with concentrated sulfuric acid, a zinc salt is produced, resulting in a dark red and yellow solution. These color changes serve as a strong basis for the identification of luteolin"

Common Dietary and Plant Sources of Luteolin

Source	Luteolin Content	Approximate Equivalent	Relative Source Level	Notes
Bird chili	1035 mg/kg	103.5 mg/100 g	Very high	Highest source in the cited quantitative food table; concentration may vary substantially by cultivar, maturity and analytical method.
Belimbi leaves	464.5 mg/kg	46.45 mg/100 g	Very high	Leaf material; not a common Western dietary source.
Onion leaves	391 mg/kg	39.1 mg/100 g	Very high	Green onion/scallion-type leaf tissue can contain substantially more luteolin than onion bulbs.
Belimbi fruit	202 mg/kg	20.2 mg/100 g	High	Tropical fruit source.
Dried asam gelugur	107.5 mg/kg	10.75 mg/100 g	High	Dried plant material; dry-weight concentration is not directly comparable with fresh vegetables.
Celery	80.5 mg/kg	8.05 mg/100 g	High	One of the most commonly cited dietary sources of luteolin; content differs among celery varieties and plant parts.
Broccoli	74.5 mg/kg	7.45 mg/100 g	High	Common dietary source. Other compositional surveys report a broad range, indicating strong cultivar and methodology effects.
Carrot	37.5 mg/kg	3.75 mg/100 g	Moderate	Common dietary source; luteolin may occur predominantly in glycosylated forms.
Green chili	33 mg/kg	3.3 mg/100 g	Moderate	Content varies substantially among Capsicum species and cultivars.
Limau purut leaves	30.5 mg/kg	3.05 mg/100 g	Moderate	Kaffir lime leaves; primarily used as a culinary herb rather than consumed in large quantities.
French bean	11 mg/kg	1.1 mg/100 g	Low to moderate	Common food source but substantially lower than celery, broccoli or onion leaves in the cited dataset.
White radish	9 mg/kg	0.9 mg/100 g	Low	Lower-luteolin dietary source in the cited dataset.
Parsley	Approximately 19.75 mg/100 g dried	Approximately 197.5 mg/kg dried	High	Frequently cited as a rich luteolin-containing herb. Dry-weight values should not be compared directly with fresh-weight vegetables.
Thyme	Approximately 51 mg/100 g	Approximately 510 mg/kg	Very high	Herb source reported in reviews; intake per serving is usually small despite the high concentration.
Peppermint	Approximately 11.33 mg/100 g fresh	Approximately 113.3 mg/kg	High	Fresh peppermint is a relatively concentrated herbal source.
Spinach	Approximately 1.11 mg/100 g	Approximately 11.1 mg/kg	Low to moderate	Common dietary source but lower than many herbs and celery-family plants.
Cabbage	Approximately 0.4–0.6 mg/100 g	Approximately 4–6 mg/kg	Low	Widely consumed but generally a relatively dilute luteolin source.
Black olives	Approximately 3.2–17.5 mg/100 g	Approximately 32–175 mg/kg	Moderate to high	Luteolin concentration depends strongly on olive cultivar and processing.
Green olives	Approximately 0.2–1.2 mg/100 g	Approximately 2–12 mg/kg	Low to moderate	Generally reported at lower concentrations than black olives.
Apple peel	Variable	Not consistently quantified	Low to moderate	Luteolin is reported principally in the peel rather than the flesh; concentration is cultivar-dependent.
Chrysanthemum flowers	Variable	Not consistently quantified	Potentially high	Traditional medicinal/tea source containing luteolin and luteolin glycosides.

Luteolin — Cancer Mechanisms

Rank	Pathway / Axis	Cancer Cells	Normal Cells	TSF	Primary Effect	Notes / Interpretation
1	PI3K / AKT / mTOR survival signaling	↓ PI3K; ↓ p-AKT; ↓ mTOR	↔ / adaptive modulation	R–G	↓ survival and proliferation; ↑ cell death	One of the most recurrent anticancer signaling effects; confirmed in multiple tumor systems and newer NSCLC studies.
2	ROS and antioxidant defense	↑ ROS; ↓ SOD/GSH/NRF2/HO-1 (context-dependent)	↓ ROS; ↑ antioxidant defenses (context-dependent)	P–R	Selective oxidative stress in susceptible tumors	Biphasic and highly context-dependent. ROS generation can be mechanistically upstream of NF-κB inhibition, JNK activation, apoptosis and radiosensitization.
3	NRF2 / HO-1 antioxidant survival axis	↓ NRF2; ↓ HO-1 (model-dependent)	↑ NRF2; ↑ HO-1 (model-dependent)	R–G	↓ tumor antioxidant capacity and drug resistance	Especially relevant in NRF2-high cancer cells. Luteolin has sensitized tumor cells to chemotherapy through NRF2 suppression, whereas NRF2 activation contributes to normal-tissue protection.
4	NF-κB inflammatory survival signaling	↓ NF-κB; ↓ inflammatory survival signaling	↓ pathological NF-κB activation	R–G	↑ apoptosis; ↓ inflammation and survival	ROS accumulation can participate upstream in some tumor models; not all NF-κB inhibition requires ROS.
5	Mitochondria and intrinsic apoptosis	↓ MMP; ↑ BAX; ↓ BCL-2; ↑ Cyt-c; ↑ caspase-9/3	↔ / ↓ mitochondrial injury under oxidative-stress conditions	R–G	↑ mitochondrial apoptosis	A common downstream execution mechanism following AKT inhibition, ROS elevation or ER stress.
6	JAK / STAT3 signaling	↓ STAT3; ↓ p-STAT3	↔ / ↓ inflammatory STAT3	R–G	↓ proliferation, stemness and immune escape	Recent work also links PRDX2 inhibition to JAK2/STAT3 suppression and ↓ PD-L1 in lung adenocarcinoma.
7	EMT and metastatic signaling	↓ EMT; ↑ E-cadherin; ↓ N-cadherin; ↓ vimentin; ↓ MMP2/9	↔	G	↓ migration, invasion and metastasis	PI3K/AKT, TGF-β/Smad, YAP/TAZ, FAK and related axes contribute depending on tumor type.
8	Cell-cycle control	↑ G1 or G2/M arrest; ↓ cyclins/CDKs; ↑ p21/p27	↔ (model-dependent)	G	↓ proliferation	Cell-cycle phase varies with tumor lineage and concentration.
9	p53 / JNK apoptotic signaling	↑ JNK; ↑ p53 stability/activity (context-dependent)	↔	R–G	↑ apoptosis and chemotherapy response	Cisplatin sensitization can depend strongly on functional p53.
10	Glycolysis and metabolic adaptation	↓ glycolysis; ↓ PKM2; ↓ HK2; ↓ ATP (model-dependent)	↔	G	↓ metabolic support for proliferation	Not universal across cancers; strongest evidence comes from selected hepatocellular and other metabolically dependent models.
11	HIF-1α and hypoxic adaptation	↓ HIF-1α; ↓ hypoxic adaptation	↔	G	↓ angiogenesis and hypoxia tolerance	Reported in breast, colon and other cancer models; linked to reduced VEGF signaling.
12	VEGF and angiogenesis	↓ VEGF; ↓ VEGFR signaling	↔ / anti-inflammatory vascular effects	G	↓ tumor angiogenesis	Predominantly preclinical evidence.
13	ER stress and unfolded protein response	↑ PERK/eIF2α/ATF4/CHOP; ↑ ER stress (model-dependent)	↓ pathological ER stress in several injury models	R–G	↑ tumor cell death	Illustrates luteolin's frequently opposite stress response in malignant versus nonmalignant models.
14	Autophagy	↑ Beclin-1; ↑ LC3-II; ↓ p62 (context-dependent)	↔ / protective modulation	G	Autophagic stress or contribution to cell death	Can be cytotoxic or cytoprotective depending on cancer model and treatment context.
15	GPX4-dependent ferroptosis	↓ GPX4; ↓ GSH; ↑ lipid oxidation; ↑ ferroptosis	↔ / ↓ ferroptotic injury in some normal-tissue models	R–G	↑ ferroptotic cancer-cell death	Recent colon-cancer work supports GPX4-linked ferroptosis plus enhanced antitumor immune activation.
16	Epigenetic regulation	↓ DNMT activity; ↓ HDAC-associated signaling; ↓ EZH2 (model-dependent)	↔ / context-dependent	G	Re-expression of growth-suppressive programs	Mechanistically interesting but less broadly established than AKT, redox and inflammatory pathways.
17	YAP / Wnt and tumor immunity	↓ YAP; ↓ Wnt-associated signaling; ↓ immune escape	↑ CTL functional activity indirectly	G	↑ antitumor T-cell effectiveness	2025 animal work suggests luteolin can enhance tumor-specific CTL therapy; clinical relevance remains unproven.
18	Chemosensitization	↑ response to cisplatin and several other agents (drug-dependent)	Variable; possible tissue protection in other contexts	G	↓ treatment resistance	Mechanisms include ↓ NRF2, ↓ AKT, ↑ p53/JNK, mitochondrial apoptosis and suppression of resistance pathways. Evidence remains predominantly preclinical.
19	Radiosensitization	↑ radiation-induced ROS and apoptosis	Potential radioprotection reported in nonmalignant models	R–G	↑ radiation response	In NSCLC models, p38/ROS/caspase signaling increased radiosensitivity; tumor versus normal-tissue effects require careful context separation.
20	Clinical Translation Constraint	High in-vitro concentrations often required	Systemic exposure dominated by conjugated metabolites	G	Limits translation of cell-culture potency	Poor aqueous solubility, extensive phase-II metabolism, formulation dependence, possible transporter/drug interactions and extremely limited controlled human oncology evidence remain major constraints.

P: 0–30 min R: 30 min–3 hr G: >3 hr

Luteolin — Alzheimer’s disease relevance: Luteolin has substantial preclinical neuroprotective evidence and is sufficiently relevant to Alzheimer’s disease to warrant a separate database section. Reported effects include ↓ amyloid-β production/accumulation, ↓ BACE1-associated amyloidogenic processing, ↓ tau hyperphosphorylation, ↓ neuroinflammation, ↓ oxidative stress, ↓ NLRP3/NF-κB signaling and ↑ BDNF/TrkB-associated neuroplasticity. Acetylcholinesterase inhibition has also been reported. However, evidence remains predominantly cellular and animal; convincing disease-modifying clinical evidence in Alzheimer’s disease is absent. Oral bioavailability and blood-brain exposure of free luteolin remain important translational constraints.

Clinical evidence status: Preclinical. Contemporary reviews identify Alzheimer’s disease as the neurodegenerative disorder in which luteolin has been studied most extensively, but explicitly note that clinical therapeutic evidence remains deficient.

Luteolin — Alzheimer’s Disease Mechanisms

Rank	Pathway / Axis	Modulation	Primary Effect	Notes / Interpretation
1	Neuroinflammation / NF-κB	↓ NF-κB; ↓ IL-1β; ↓ IL-6; ↓ TNF-α	↓ chronic neuroinflammation	Among the most consistently proposed neuroprotective actions.
2	Amyloid-β pathology	↓ Aβ; ↓ Aβ42	↓ amyloid burden	Supported predominantly by cellular and animal studies.
3	BACE1 / amyloidogenic processing	↓ BACE1	↓ amyloidogenic APP processing	Potential upstream mechanism contributing to reduced Aβ generation.
4	Tau phosphorylation	↓ p-tau	↓ tau pathology	Multiple preclinical models report reduced abnormal tau phosphorylation.
5	Oxidative stress / NRF2	↓ ROS; ↑ NRF2; ↑ antioxidant defenses	↓ neuronal oxidative injury	Direction differs from the pro-oxidant effect frequently exploited in cancer cells.
6	NLRP3 inflammasome	↓ NLRP3	↓ inflammasome-driven neuronal inflammation	Potential bridge between redox stress and neuroinflammation.
7	BDNF / TrkB neuroplasticity	↑ BDNF; ↑ TrkB	↑ synaptic and neuronal support	Observed in several neurobehavioral models.
8	Acetylcholinesterase	↓ AChE	↑ cholinergic signaling	Primarily biochemical/preclinical evidence; clinical magnitude is unknown.
9	Neuronal apoptosis and mitochondrial stress	↓ apoptosis; ↓ mitochondrial injury	↑ neuronal survival	Opposite phenotypic direction from luteolin-induced apoptosis in many cancer models.
10	Clinical Translation Constraint	Low free-luteolin exposure; limited human CNS data	Uncertain clinical efficacy	Human Alzheimer’s disease efficacy trials are insufficient; brain exposure and formulation remain unresolved.

HDAC, Histone deacetylases: Click to Expand ⟱

Source:

Type:

Enzymes involved in regulating gene expression by removing acetyl groups from histones, the proteins around which DNA is wrapped.
-Many cancers exhibit altered expression levels of HDACs, which can contribute to the dysregulation of genes involved in cell growth, survival, and differentiation.
-HDACs can repress the expression of tumor suppressor genes, leading to uncontrolled cell proliferation and survival. This repression can be a key factor in the development and progression of cancer.
-HDAC inhibitors (HDACi) have been developed and are being investigated for their ability to reactivate silenced genes, induce cell cycle arrest, and promote apoptosis in cancer cells.
-HDAC1, HDAC2): Often overexpressed in various cancers, including breast, prostate, and colorectal cancers. Their overexpression is associated with poor prognosis.
-HDAC4, HDAC5): These may have both oncogenic and tumor-suppressive roles depending on the context and cancer type.
-While HDACs are not classified as traditional oncogenes, their overexpression and activity can contribute to oncogenic processes.
-HDAC inhibitor works by preventing the removal of acetyl groups from histones, thereby modulating gene expression, influencing cell behavior, and potentially reversing aberrant gene silencing seen in various diseases.
-HDAC inhibitors can help reactivate these genes, thereby inhibiting growth and inducing apoptosis in cancer cells.

Scientific Papers found: Click to Expand⟱

1064-

LT,

Cisplatin,

Inhibition of cell survival, invasion, tumor growth and histone deacetylase activity by the dietary flavonoid luteolin in human epithelioid cancer cells

vitro+vivo,

Lung,

LNM35

25-200μM

intraperitoneal injection (20mg/kg/day for 18days)

in-vitro,

CRC,

HT-29

in-vitro,

Liver,

HepG2

in-vitro,

BC,

MCF7

in-vitro,

BC,

MDA-MB-231

Casp3↑,
Casp7↑,
HDAC↓, luteolin is a potent HDAC inhibitor

2927-

LT,

Luteolin Causes 5′CpG Demethylation of the Promoters of TSGs and Modulates the Aberrant Histone Modifications, Restoring the Expression of TSGs in Human Cancer Cells

in-vitro,

Cerv,

HeLa

 5, 10, and 20 µM of luteolin for 48 h

TumCMig↓, luteolin inhibited migration and colony formation in HeLa cells.
DNMTs↓, Luteolin decreased DNMT activity in HeLa cells in a concentration-dependent manner.
HDAC↓, Luteolin Decreases HDAC Activity in HeLa Cells
HATs↓, Luteolin Reduces the HAT Activity in a Dose-Dependent Manner
ac‑H3↓, H3 acetylation marks were diminished after treatment with the 20 µM of luteolin
ac‑H4↓, the acetylation marks at H4 were also modulated,
MMP2↓, Luteolin resulted in downregulation of expression of various proteins related to migration and inflammation in HeLa cells, and fold changes (FC) after treatment with 10 and 20 µM for 48 h are given, respectively, for MMP2 (FC 0.33, 0.26), MMP3 (FC 0.
MMP9↓,
HO-1↓, Genes related to cell proliferation, growth, and apoptosis such as BCL-X (FC 0.55, 0.45), HO-1/HMOX1 (FC 0.40, 0.25), Kallikrein6 (FC 0.55, 0.48), Kallikrein 3/PSA (FC 0.58, 0.48) were reduced.
E-cadherin↑, E-cadherin (FC 1.8, 2.9) were upregulated
EZH2↓, Luteolin has depicted increased expression of MiR-26a, which is a regulator of EZH2, and at the same time, it has inhibited EZH2
HER2/EBBR2↓, luteolin treatment decreased the inflammatory and migratory proteins such as MMp-2, MMP-3, HO-1/HMOX1, Her1, HER2, Her4, mesothelin, cathepsin B, MUC1, nectin 4, FOXC2, IL-18 BPa, CCL3/MIP-1α, CXCL8/IL-8, IL-2
IL18↓,
IL8↓,
IL2↓,

2919-

LT,

Luteolin as a potential therapeutic candidate for lung cancer: Emerging preclinical evidence

Review,

Var,

RadioS↑, it can be used as an adjuvant to radio-chemotherapy and helps to ameliorate cancer complications
ChemoSen↑,
chemoP↑,
*lipid-P↓, ↓LPO, ↑CAT, ↑SOD, ↑GPx, ↑GST, ↑GSH, ↓TNF-α, ↓IL-1β, ↓Caspase-3, ↑IL-10
*Catalase↑,
*SOD↑,
*GPx↑,
*GSTs↑,
*GSH↑,
*TNF-α↓,
*IL1β↓,
*Casp3↓,
*IL10↑,
NRF2↓, Lung cancer model ↓Nrf2, ↓HO-1, ↓NQO1, ↓GSH
HO-1↓,
NQO1↓,
GSH↓,
MET↓, Lung cancer model ↓MET, ↓p-MET, ↓p-Akt, ↓HGF
p‑MET↓,
p‑Akt↓,
HGF/c-Met↓,
NF-kB↓, Lung cancer model ↓NF-κB, ↓Bcl-XL, ↓MnSOD, ↑Caspase-8, ↑Caspase-3, ↑PARP
Bcl-2↓,
SOD2↓,
Casp8↑,
Casp3↑,
PARP↑,
MAPK↓, LLC-induced BCP mouse model ↓p38 MAPK, ↓GFAP, ↓IBA1, ↓NLRP3, ↓ASC, ↓Caspase1, ↓IL-1β
NLRP3↓,
ASC↓,
Casp1↓,
IL6↓, Lung cancer model ↓TNF‑α, ↓IL‑6, ↓MuRF1, ↓Atrogin-1, ↓IKKβ, ↓p‑p65, ↓p-p38
IKKα↓,
p‑p65↓,
p‑p38↑,
MMP2↓, Lung cancer model ↓MMP-2, ↓ICAM-1, ↓EGFR, ↓p-PI3K, ↓p-Akt
ICAM-1↓,
EGFR↑,
p‑PI3K↓,
E-cadherin↓, Lung cancer model ↑E-cadherin, ↑ZO-1, ↓N-cadherin, ↓Claudin-1, ↓β-Catenin, ↓Snail, ↓Vimentin, ↓Integrin β1, ↓FAK
ZO-1↑,
N-cadherin↓,
CLDN1↓,
β-catenin/ZEB1↓,
Snail↓,
Vim↑,
ITGB1↓,
FAK↓,
p‑Src↓, Lung cancer model ↓p-FAK, ↓p-Src, ↓Rac1, ↓Cdc42, ↓RhoA
Rac1↓,
Cdc42↓,
Rho↓,
PCNA↓, Lung cancer model ↓Cyclin B1, ↑p21, ↑p-Cdc2, ↓Vimentin, ↓MMP9, ↑E-cadherin, ↓AIM2, ↓Pro-caspase-1, ↓Caspase-1 p10, ↓Pro-IL-1β, ↓IL-1β, ↓PCNA
Tyro3↓, Lung cancer model ↓TAM RTKs, ↓Tyro3, ↓Axl, ↓MerTK, ↑p21
AXL↓,
CEA↓, B(a)P induced lung carcinogenesis ↓CEA, ↓NSE, ↑SOD, ↑CAT, ↑GPx, ↑GR, ↑GST, ↑GSH, ↑Vitamin E, ↑Vitamin C, ↓PCNA, ↓CYP1A1, ↓NF-kB
NSE↓,
SOD↓,
Catalase↓,
GPx↓,
GSR↓,
GSTs↓,
GSH↓,
VitE↓,
VitC↓,
CYP1A1↓,
cFos↑, Lung cancer model ↓Claudin-2, ↑p-ERK1/2, ↑c-Fos
AR↓, ↓Androgen receptor
AIF↑, Lung cancer model ↑Apoptosis-inducing factor protein
p‑STAT6↓, ↓p-STAT6, ↓Arginase-1, ↓MRC1, ↓CCL2
p‑MDM2↓, Lung cancer model ↓p-PI3K, ↓p-Akt, ↓p-MDM2, ↑p-P53, ↓Bcl-2, ↑Bax
NOTCH1↓, Lung cancer model ↑Bax, ↑Cleaved-caspase 3, ↓Bcl2, ↑circ_0000190, ↓miR-130a-3p, ↓Notch-1, ↓Hes-1, ↓VEGF
VEGF↓,
H3↓, Lung cancer model ↑Caspase 3, ↑Caspase 7, ↓H3 and H4 HDAC activities
H4↓,
HDAC↓,
SIRT1↓, Lung cancer model ↑Bax/Bcl-2, ↓Sirt1
ROS↑, Lung cancer model ↓NF-kB, ↑JNK, ↑Caspase 3, ↑PARP, ↑ROS, ↓SOD
DR5↑, Lung cancer model ↑Caspase-8, ↑Caspase-3, ↑Caspase-9, ↑DR5, ↑p-Drp1, ↑Cytochrome c, ↑p-JNK
Cyt‑c↑,
p‑JNK↑,
PTEN↓, Lung cancer model 1/5/10/30/50/80/100 μmol/L ↑Cleaved caspase-3, ↑PARP, ↑Bax, ↓Bcl-2, ↓EGFR, ↓PI3K/Akt/PTEN/mTOR, ↓CD34, ↓PCNA
mTOR↓,
CD34↓,
FasL↑, Lung cancer model ↑DR 4, ↑FasL, ↑Fas receptor, ↑Bax, ↑Bad, ↓Bcl-2, ↑Cytochrome c, ↓XIAP, ↑p-eIF2α, ↑CHOP, ↑p-JNK, ↑LC3II
Fas↑,
XIAP↓,
p‑eIF2α↑,
CHOP/DDIT3↑,
LC3II↑,
PD-1↓, Lung cancer model ↓PD-L1, ↓STAT3, ↑IL-2
STAT3↓,
IL2↑,
EMT↓, Luteolin exerts anticancer activity by inhibiting EMT, and the possible mechanisms include the inhibition of the EGFR-PI3K-AKT and integrin β1-FAK/Src signaling pathways
cachexia↓, luteolin could be a potential safe and efficient alternative therapy for the treatment of cancer cachexi
BioAv↑, A low-energy blend of castor oil, kolliphor and polyethylene glycol 200 increases the solubility of luteolin by a factor of approximately 83
*Half-Life↝, ats administered an intraperitoneal injection of luteolin (60 mg/kg) absorbed it rapidly as well, with peak levels reached at 0.083 h (71.99 ± 11.04 μg/mL) and a prolonged half-life (3.2 ± 0.7 h)
*eff↑, Luteolin chitosan-encapsulated nano-emulsions increase trans-nasal mucosal permeation nearly 6-fold, drug half-life 10-fold, and biodistribution of luteolin in brain tissue 4.4-fold after nasal administration

2915-

LT,

Luteolin promotes apoptotic cell death via upregulation of Nrf2 expression by DNA demethylase and the interaction of Nrf2 with p53 in human colon cancer cells

in-vitro,

Colon,

HT29

30 μM

in-vitro,

CRC,

SNU-407

30 μM

in-vitro,

Nor,

FHC

65 μM

DNMTs↓, luteolin inhibited the expression of DNA methyltransferases, a transcription repressor, and increased the expression and activity of ten-eleven translocation (TET) DNA demethylases,
TET1↑,
NRF2↑, luteolin decreased the methylation of the Nrf2 promoter region, which corresponded to the increased mRNA expression of Nrf2
HDAC↓, Recently, Zao et al. demonstrated that luteolin epigenetically activates the Nrf2 pathway by downregulating DNA methyltransferase (DNMT) and histone deacetylase (HDAC) expression
tumCV↓, Luteolin decreased the viability of all three cell lines in a dose-dependent manner
BAX↑, luteolin upregulated the expression of the apoptotic protein Bax, active caspase-9, and active caspase-3, while it downregulated the expression of the anti-apoptotic protein Bcl-2,
Casp9↑,
Casp3↑,
Bcl-2↓,
ROS↓, Luteolin promotes ROS scavenging by inducing the expression of antioxidant enzymes
GSS↑, luteolin increased the protein expression of the antioxidant enzymes GCLc, GSS, catalase, and HO-1 in a dose- and time-dependent manner
Catalase↑,
HO-1↑,
DNMT1↓, Luteolin markedly decreased the protein expression of DNMT1, DNMT3A, and DNMT3B in a dose- and time-dependent manner
DNMT3A↓,
TET1↑, In contrast, it markedly increased the protein expression of TET1, TET2, and TET3 in a dose- and time-dependent manner
TET3↑,
TET2↓,
P53↑, Luteolin upregulated the expression of p53 and its target p21 in a dose- and time-dependent manner
P21↑,

Showing Research Papers: 1 to 4 of 4

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 4

Pathway results for Effect on Cancer / Diseased Cells:

Functional Outcomes(tgid=23) ⓘ

cachexia↓, 1, chemoP↑, 1,
Total Targets: 118

Pathway results for Effect on Normal Cells:

Redox & Oxidative Stress(tgid=1) ⓘ

Catalase↑, 1, GPx↑, 1, GSH↑, 1, GSTs↑, 1, lipid-P↓, 1, SOD↑, 1,

Cell Death(tgid=5) ⓘ

Casp3↓, 1,

Immune & Inflammatory Signaling(tgid=16) ⓘ

IL10↑, 1, IL1β↓, 1, TNF-α↓, 1,

Drug Metabolism & Resistance(tgid=21) ⓘ

eff↑, 1, Half-Life↝, 1,
Total Targets: 12

Scientific Paper Hit Count for: HDAC, Histone deacetylases

4 Luteolin
1 Cisplatin

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#:118  Target#:140  State#:%  Dir#:%
  wNotes=on  sortOrder:rid,rpid

Luteolin / HDAC Cancer Research Results

Common Dietary and Plant Sources of Luteolin

Luteolin — Cancer Mechanisms

Luteolin — Alzheimer’s Disease Mechanisms

Pathway results for Effect on Cancer / Diseased Cells:

Redox & Oxidative Stress(tgid=1) ⓘ

Core Metabolism/Glycolysis(tgid=4) ⓘ

Cell Death(tgid=5) ⓘ

Kinase & Signal Transduction(tgid=6) ⓘ

Transcription & Epigenetics(tgid=7) ⓘ

Protein Folding & ER Stress(tgid=8) ⓘ

Autophagy & Lysosomes(tgid=9) ⓘ

DNA Damage & Repair(tgid=10) ⓘ

Cell Cycle & Senescence(tgid=11) ⓘ

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

Migration(tgid=13) ⓘ

Angiogenesis & Vasculature(tgid=14) ⓘ

Barriers & Transport(tgid=15) ⓘ

Immune & Inflammatory Signaling(tgid=16) ⓘ

Hormonal & Nuclear Receptors(tgid=20) ⓘ

Drug Metabolism & Resistance(tgid=21) ⓘ

Clinical Biomarkers(tgid=22) ⓘ

Functional Outcomes(tgid=23) ⓘ

Pathway results for Effect on Normal Cells:

Redox & Oxidative Stress(tgid=1) ⓘ

Cell Death(tgid=5) ⓘ

Immune & Inflammatory Signaling(tgid=16) ⓘ

Drug Metabolism & Resistance(tgid=21) ⓘ

Home Page