Beclin-1 Cancer Research Results
Beclin-1, Beclin-1 (BECN1 gene): Click to Expand ⟱
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| Type: Protein Coding gene |
Beclin 1, an autophagy and haploinsufficient tumor-suppressor protein, is frequently monoallelically deleted in breast and ovarian cancers. However, the precise mechanisms by which Beclin 1 inhibits tumor growth remain largely unknown.
A key biomarker of autophagy is Beclin-1. Beclin-1 stimulates LC3-I’s lipidation to produce LC3-II, which localizes to the autophagosome membrane to activate the development of autophagosomes.
-BECN1 = the official gene symbol (human gene name)
-Beclin-1 = the protein name encoded by the BECN1 gene
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Scientific Papers found: Click to Expand⟱
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in-vitro, |
Pca, |
LNCaP |
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in-vitro, |
Pca, |
DU145 |
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ROS↓, ALA decreased ROS production, SOD1 and GSTP1 protein expression
SOD↓, SOD1, DU145
GSTP1/GSTπ↓,
NRF2↓, significantly reduced the cytosolic and nuclear content of the transcription factor Nrf2
p62↓, du145
p62↑, LNCaP
SOD↑, LNCaP
p‑mTOR↑, revealed that in both cancer cells, ALA, by upregulating pmTOR expression, reduced the protein content of two autophagy initiation markers, Beclin-1 and MAPLC3.
Beclin-1↓,
ROS↑, Interestingly, in LNCaP cells, we observed an almost significant increase in ROS content (p = 0.06) after ALA compared to the control, concomitantly with a significant upregulation of the antioxidant enzyme SOD1 after 48 h.
SOD1↑,
Keap1↝, The findings revealed that BA activated Keap1/Nrf2 pathway and triggered mitochondria-dependent apoptosis due to ROS production.
ROS↑,
Ca+2↑, Furthermore, BA increased the intracellular Ca2+ levels
Beclin-1↓, inhibited the expression of Beclin1 and promoted the expression of GRP78, LC3-II, and p62 associated with ERS and autophagy.
GRP78/BiP↑,
LC3II↑,
p62↑,
ERStress↑,
TumAuto↑,
Ferroptosis↑, including the induction of ferroptosis by regulating the SLC7A11/GPX4 axis
GutMicro↑, and modulating gut microbiota metabolism. I
Akt↓, it inhibits pro-tumorigenic signals such as Akt/mTOR, NF-κB, Wnt/β-catenin, and STAT3, thereby blocking tumor proliferation, invasion, and metastasis
mTOR↓,
NF-kB↓,
Wnt↓,
β-catenin/ZEB1↓,
STAT3↓,
TumCP↓,
TumCI↓,
TumMeta↓,
AMPK↑, activates tumor-suppressive and cytoprotective pathways, including AMPK, p53, and nuclear factor erythroid 2-related factor 2 (Nrf2), which induce cell cycle arrest and apoptosis
P53↑,
NRF2↑,
TumCCA↑,
Apoptosis↑,
Casp↑, activation of the Caspase cascade
GPx4↓, as well as ferroptosis by inhibiting the solute carrier family 7 member 11 (SLC7A11)/glutathione peroxidase 4 (GPX4) axis [5]
DNMTs↓, inhibiting epigenetic regulatory mechanisms such as DNMTs and HDACs.
HDAC↓,
VEGF↓, inhibiting VEGF signaling and enhances the immune microenvironment by improving T cell and NK cell function
Imm↑,
NK cell↑,
Warburg↓, Curcumin effectively reverses the Warburg effect and interferes with glucose metabolism by targeting HIF-1α and inhibiting key enzymes, including hexokinase 2 (HK2), pyruvate kinase M2 (PKM2), and lactate dehydrogenase A (LDHA)
Hif1a↓,
HK2↓,
PKM2↓,
LDHA↓,
GLUT1↓, as well as the functions of glucose transporter 1 (GLUT1) and monocarboxylate transporters (MCTs) [12].
MCT1↓,
AMPK↑, curcumin activates signaling pathways such as AMPK, downregulates fatty acid synthase (FASN) and stearoyl-CoA desaturase (SCD1),
FASN↓,
SCD1↓,
GLS↓, Curcumin extensively intervenes in amino acid metabolism by inhibiting the activity of glutaminase (GLS), ornithine decarboxylase (ODC), and other enzymes,
Apoptosis↑, inducing apoptosis through mechanisms such as disrupting the electron transport chain, reducing membrane potential, and promoting the generation of reactive oxygen species (ROS)
ETC↓,
MMP↓,
ROS↑,
lipid-P↑, curcumin induces lipid peroxidation and collapses redox homeostasis, thereby activating the ferroptosis program [
ChemoSen↑, blocking invasion and metastasis, and enhancing chemosensitivity.
PDK1↓, In hypoxic pancreatic cancer cells, curcumin downregulates the expression of GLUT1, HK2, LDHA, and PDK1 by inhibiting the Beclin1/HIF-1α axis, which results in reduced ATP production and inhibited cell proliferation [
Beclin-1↓,
ATP↓,
Glycolysis↓, inhibiting glycolysis
GlucoseCon↓, decreased glucose uptake and increased lactate production
lactateProd↑,
MMPs↓, reduces MMP, GSH, and G6PD activities
GSH↓, inhibition of SLC7A11 to limit GSH synthesis, thereby triggering the collapse of the antioxidant defense system
G6PD↓,
OXPHOS↓, downregulate OXPHOS and glycolysis activities
SREBP2↓, curcumin treatment leads to a marked downregulation of the mRNA expression of SREBP and its target genes. inhibiting the expression of NPC1L1, SREBP-2, and HNF1α
COX2↓, curcumin exerts anti-tumor effects by downregulating the expression of NF-κB, COX-2, and AP-1
AP-1↓,
NADH↓, decreased GPx4 and FSP1 expression, induced ferroptosis by inhibiting GSH-GPx4 and FSP1-CoQ 10-NADH pathways
NRF2↑, it inhibits GPX4 and activates Nrf2 and heme oxygenase-1 (HO-1). This results in an abnormal accumulation of intracellular Fe2+, ROS, lipid peroxides, and malondialdehyde (MDA), along with a depletion of GSH
HO-1↑,
Iron↑,
MDA↑,
*ROS↓, studies have demonstrated that the topical application of curcumin on the skin exerts antitumor effects by synergistically downregulating COX-2 and ODC activities, alleviating oxidative damage, and concurrently inhibiting inflammatory proliferation i
*Inflam↓,
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in-vitro, |
AML, |
U937 |
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in-vivo, |
AML, |
NA |
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TumCP↓, DAP significantly inhibited cell proliferation, increased apoptosis induction and suppressed autophagy in AML cells in vitro
Apoptosis↑,
TumCG↓, inhibited tumor growth in an AML mouse model in vivo
PDK1↓, inhibition of PDK1 with DAP
cl‑PARP↑, increased the cleavage of pro-apoptotic proteins (PARP and Caspase 3)
Bcl-xL↓, decreased the expression of the anti-apoptotic proteins (BCL-xL and BCL-2) and autophagy regulators (ULK1, Beclin-1 and Atg).
Bcl-2↓,
Beclin-1↓,
ATG3↓,
PI3K↓, DAP inhibited the PI3K/Akt signaling pathway
Akt↓,
eff↑, Importantly, 2,2-dichloroacetophenone (DAP) is a much more potent inhibitor of PDK1(than DCA). It is effective at concentrations in the micromolar (μM) range.
AntiCan↑, It has therapeutic effects in cancer, diabetes, neurodegenerative diseases or chronic inflammatory diseases.
*AntiDiabetic↑, anticancer, neuroprotective, antidiabetic, antioxidant and anti-inflammatory.
*neuroP↑,
*Inflam↓,
*antiOx↑,
*BioAv↓, Because its bioavailability is low, there are limitations in clinical therapeutic use.
*BioAv↑, combined administration of emodin and piperine has been observed to clinically improve emodin pharmacokinetics, increasing 221 % of the area under the curve (AUC), 258 % the maximum concentration (Cmax), and decreasing 230 % the clearance related to
*SOD↑, fig 2 antioxidant
*GPx↑,
*GSH↑,
*NRF2↑,
*ROS↓,
*lipid-P↓,
*Cyt‑c↓,
*BAX↓, fig 2 antiinflammatory
*Bcl-2↓,
*iNOS↓,
*NO↓,
*IL6↓,
*IL10↓,
*IL17↓,
*IFN-γ↓,
*NF-kB↓,
*LC3II↓,
*Akt↓,
*Beclin-1↓,
*AMPK↓, fig 2 neuroprotective
*TNF-α↓,
*PGE2↓,
*Apoptosis↓,
*Casp3↓,
*Casp9↓,
*P53↓,
*P21↓,
*NAD↓, neuronal oxidative stress
*ATP↓,
*CHOP↓,
*GADD34↓,
*ATF4↓,
tumCV↓, fig 2 anticancer
Apoptosis↑,
TumCG↓,
TumCI↓,
TumMeta↓,
CSCs↓, glioma stem cells ↓b-catenin, ↓Notch-1, ↓STAT3
NOTCH1↓,
STAT3↓,
eff↑, emodin combined with curcumin ↓proliferation, ↑miR-34a
miR-34a↓,
*neuroP↑, Neuroprotective LPS-stimulated mouse ↓Nrf-2, NQO1, ↓TNF-α,↓↓ IL-6, ↓NO, ↓PGE2
*BDNF↓, model of chronic stress mice in vivo ↓progression of behavioral impairments in mice ↓consumption of sucrose, ↓plasmatic corticosterone, ↓mRNA, ↓BDNF,
*hepatoP↑, Hepatoprotective rats in vivo ↓ethanol-mediated liver steatosis ↓ ALT, ↓AST, ↓ TGL
*ALAT↓,
*AST↓,
TG/TAG↓,
ROS↑, However, at higher concentrations, emodin significantly increased ROS generation and reduced cell viability.
Slug↓, expression levels of Slug (a transcription factor) were also suppressed with emodin treatment.
EMT↓, results suggested that emodin suppressed the epithelial-mesenchymal transition of cancer cells through the ILK/GSK-3β/Slug signaling pathway
Glycolysis↓, In addition, emodin inhibited glycolysis via ROS-induced inactivation of the PI3K/AKT signaling pathway.
ChemoSen↑, The study by Peng et al. [130] also showed chemosensitizing effects of emodin to cisplatin in A549 (2–20 µM, for 48 h) and H460 (0.5–10 µM) non-small cell lung cancer cells.
P-gp↓, The sensitization mechanism was mediated by the inhibition of P-glycoprotein (Pgp), a drug-resistant protein related to the efflux pump mechanism.
Ki-67↓, The significant reduction of Ki-67 and proliferating cell nuclear antigen (PCNA) protein levels supported the antiproliferative effect of emodin in animal models.
PCNA↓,
ER Stress↑, findings suggested that emodin exerts its apoptotic effects in a process mediated by ER stress and the activation of the TRIB3/NF-κB pathway in lung cancer cells.
TRIB3↑,
NF-kB↑,
TumMeta↑, Emodin (40 mg/kg for 7 days) significantly decreased the metastatic recurrence of breast cancer after surgery in the lungs by reducing the formation of epithelial-mesenchymal transition (EMT) and cancer stem cell (CSC).
*Imm↓, emodin may be developed as an immunosuppressive agent in case of immune activation, autoimmune disorders even in organ transplantation
*toxicity↝, An excess of emodin due to its laxative effects causes intestinal pain and severe diarrhea with subsequent electrolyte imbalance and dehydration [157]. Therefore, treatment should begin when symptoms appear, with special attention to electrolyte leve
tyrosinase↓,
CK2↓,
TumCP↓,
TumCMig↓,
FGF↓,
FGFR1↓,
PI3K↓,
Akt↓,
VEGF↓,
FGFR1↓,
FGFR2↓,
PDGF↓,
ALAT↓,
AST↓,
TumCCA↑, G0/G1 phase arrest
CDK2↓,
CDK4↓,
CDK6↓,
BAX↓,
Bcl-2↓,
MMP2↓,
MMP9↓,
P53↑,
PARP↑,
PUMA↑,
NOXA↑,
Casp3↑,
Casp9↑,
TIMP1↑,
lipid-P↑,
mtDam↑,
EMT↓,
Vim↓,
E-cadherin↓,
p‑STAT3↓,
COX2↓,
CDC25↓,
RadioS↑,
ROS↑,
DNAdam↑,
γH2AX↑,
PTEN↑,
LC3II↓,
Beclin-1↓,
SOD↓,
Catalase↓,
GPx↓,
Fas↑,
*BioAv↓, ferulic acid stability and limited solubility in aqueous media continue to be key obstacles to its bioavailability, preclinical efficacy, and clinical use.
cMyc↓,
Beclin-1↑, ferulic acid by elevating the levels of the apoptosis and autophagy biomarkers, including beclin-1, Light chain (LC3-I/LC3-II), PTEN-induced putative kinase 1 (PINK-1), and Parkin
LC3‑Ⅱ/LC3‑Ⅰ↓,
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Review, |
Var, |
NA |
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Review, |
AD, |
NA |
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*Inflam↓, wide spectrum of pharmacological activities including anti-inflammatory, anticancer, antimicrobial, antioxidant, and neuroprotective activities.
*AntiCan↑,
*AntiBio↑,
*antiOx↑,
*neuroP↑,
ROS↓, GNL scavenges free radicals and preserves the activity of antioxidant enzymes.
Apoptosis↑, GNL induces apoptosis and cell cycle arrest, modulates multiple molecular targets, including p53 and STAT3, activates caspases, and modulates inflammation via transcriptional regulation.
TumCCA↑,
P53↝,
STAT3↓, GNL reduces survivin protein levels by downregulating phosphorylated STAT3.
Casp↝,
*Catalase↑, This compound protects various antioxidant enzymes, such as catalase, glutathione-S-transferase, and glutathione peroxidase.
*GSTs↑,
*GPx↑,
*AChE↓, In addition, GNL suppressed acetylcholinesterase (AChE) activity and alleviated oxidative stress by boosting neuronal reduced glutathione (GSH), catalase (CAT), glutathione-S-transferase (GST), and superoxide dismutase (SOD) activities.
*GSH↑,
*SOD↑,
*TBARS↓, It lowered malondialdehyde concentration (TBARS), nitric oxide (NO), and xanthine oxidase (XO), and restored the structural damage to the brain tissue caused by HFD.
*NO↓,
*XO↓,
*memory↑, GNL boosted learning and memory function and ameliorated the inflammation status in the brain by lowering the protein levels of IL-1β, iNOS, NF-κBp65, and COX-2
*IL1β↓,
*iNOS↓,
*NF-kB↓,
*COX2↓,
*NRF2↑, GNL administration ameliorated renal function, alleviated histological changes, and enhanced Nrf-2/HO-1/NQO-1 with a subsequent intensification of antioxidant enzyme activities.
*HO-1↑,
*survivin↓, GNL reduces survivin protein levels by downregulating phosphorylated STAT3.
TumCP↓, They have shown that GNL treatment significantly suppressed oral squamous cell carcinoma (OSCC) cell proliferation and migration in vitro and tumor growth in vivo in a time- and dose-dependent manner.
TumCMig↓,
TumCG↑,
selectivity↑, GNL may be helpful in treating different types of malignancy, while having limited effects on normal cells.
TumMeta↓, GNL has been reported to inhibit cancer metastasis and angiogenesis.
angioG↓,
Hif1a↓, A549 lung cancer cells treated with GNL, downregulation of HIF-1alpha, a VEGF regulator, occurred
Beclin-1↓, GNL also decreases autophagy through downregulation of BNIP3 and beclin-1 expression, which increases apoptotic cell death through HIF-1α signaling.
ROS↑, induction of oxidative stress, cell cycle arrest, upregulation of apoptotic genes, and inhibition of cell proliferation and angiogenesis in cancer cells.
TumCCA↑,
TumCP↓,
angioG↓,
ER Stress↑, Luteolin induces mitochondrial dysfunction and activates the endoplasmic reticulum stress response in glioblastoma cells, which triggers the generation of intracellular reactive oxygen species (ROS)
mtDam↑,
PERK↑, activate the expression of stress-related proteins by mediating the phosphorylation of PERK, ATF4, eIF2α, and cleaved-caspase 12.
ATF4↑,
eIF2α↑,
cl‑Casp12↑,
EMT↓, Luteolin is known to reverse epithelial-to-mesenchymal transition (EMT), which is associated with the cancer cell progression and metastasis.
E-cadherin↑, upregulating the biomarker E-cadherin expression, followed by a significant downregulation of the N-cadherin and vimentin expression
N-cadherin↓,
Vim↓,
*neuroP↑, Furthermore, luteolin holds potential to improve the spinal damage and brain trauma caused by 1-methyl-4-phenylpyridinium due to its excellent neuroprotective properties.
NF-kB↓, downregulation and suppression of cellular pathways such as nuclear factor kappa B (NF-kB), phosphatidylinositol 3’-kinase (PI3K)/Akt, and X-linked inhibitor of apoptosis protein (XIAP)
PI3K↓,
Akt↑,
XIAP↓,
MMP↓, Furthermore, the membrane action potential of mitochondria depletes in the presence of luteolin, Ca2+ levels and Bax expression upregulate, the levels of caspase-3 and caspase-9 increase, while the downregulation of Bcl-2
Ca+2↑,
BAX↑,
Casp3↑,
Casp9↑,
Bcl-2↓,
Cyt‑c↑, cause the cytosolic release of cytochrome c from mitochondria
IronCh↑, Luteolin serves as a good metal-chelating agent owing to the presence of dihydroxyl substituents on the aromatic ring framework
SOD↓, luteolin further triggered an early phase accumulation of ROS due to the suppression of the activity of cellular superoxide dismutase.
*ROS↓, Luteolin reportedly demonstrated an optimal 43.7% inhibition of the accumulation of ROS, 24.5% decrease in malondialdehyde levels, and 38.7% lowering of lactate dehydrogenase levels at a concentration of 30 µM
*LDHA↑,
*SOD↑, expression of superoxide dismutase ameliorated by 73.7%, while the activity of glutathione improved by 72.3% at the same concentration of luteolin
*GSH↑,
*BioAv↓, Poor bioavailability of luteolin limits its optimal therapeutic efficacy and bioactivity
Telomerase↓, MDA-MB-231 cells with luteolin led to dose dependent arrest of cell cycle in S phase by reducing the levels of telomerase and by inhibiting the phosphorylation of NF-kB inhibitor α along with its target gene c-Myc
cMyc↓,
hTERT/TERT↓, These events led to the suppression of the expression of human telomerase reverse transcriptase (hTERT) encoding for the catalytic subunit of telomerase
DR5↑, luteolin upregulated the expression of caspase cascades and death receptors, including DR5
Fas↑, expression of proapoptotic genes such as FAS, FADD, BAX, BAD, BOK, BID, TRADD upregulates, while the anti-apoptotic genes NAIP, BCL-2, and MCL-1 experience downregulation.
FADD↑,
BAD↑,
BOK↑,
BID↑,
NAIP↓,
Mcl-1↓,
CDK2↓, expression of cell cycle regulatory genes CDK2, CDKN2B, CCNE2, CDKN1A, and CDK4 decreased on incubation with luteolin
CDK4↓,
MAPK↓, expression of MAPK1, MAPK3, MAP3K5, MAPK14, PIK3C2A, PIK3C2B, AKT1, AKT2, and ELK1 downregulated
AKT1↓,
Akt2↓,
*Beclin-1↓, luteolin led to downregulation of the expression of hypoxia-inducible factor-1α and autophagy-associated proteins, Beclin 1, and LC3
Hif1a↓,
LC3II↑, LC3-II is upregulated following the luteolin treatment in p53 wild type HepG2 cells i
Beclin-1↑, Luteolin treatment reportedly increased the number of intracellular autophagosomes, as indicated by an increased expression of Beclin 1, and conversion of LC3B-I to LC3B-II in hepatocellular carcinoma SMMC-7721 cells.
PI3K↓, Nimbolide negatively regulates PI3K/Akt signalling with consequent increase in p-GSK-3βTyr216, the active form of GSK-3β that inhibits autophagy.
Akt↓,
GSK‐3β↑, Nimbolide stimulates GSK-3β expression by modulating miR-126 and HOTAIR
MMP↓, Treatment of cells with nimbolide induced a change in fluorescence from red to green indicating collapse of the MMP
Apoptosis↑, Apoptosis induction in SCC131 and SCC4 cells upon nimbolide treatment was further confirmed by an increase in the Bax/Bcl-2 ratio and higher cytosolic cytochrome c relative to the mitochondrial fraction associated with increased expression of cleaved
Bax:Bcl2↑,
Cyt‑c↑,
cl‑Casp3↑, increased expression of cleaved caspase -9 and -3
cl‑Casp9↑,
TumAuto↑, Nimbolide induces autophagy in oral cancer cells
Beclin-1↓, 24 h of treatment with nimbolide Beclin-1 expression was decreased with increased expression of p62 associated with presence of truncated ATG5
p62↑,
PI3K↓, Nimbolide induces autophagy via inhibition of PI3K pathway in oral cancer cells
chemoPv↑, The chemopreventive efficacy of nimbolide is well established in the HBP model
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Review, |
BC, |
MDA-MB-231 |
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Review, |
BC, |
MCF7 |
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TumCP↓, The anticancer mechanisms of RES in regard to breast cancer include the inhibition of cell proliferation, and reduction of cell viability, invasion, and metastasis.
tumCV↓,
TumCI↓,
TumMeta↓,
*antiOx↑, antioxidative, cardioprotective, estrogenic, antiestrogenic, anti-inflammatory, and antitumor properties it has been used against several diseases, including diabetes, neurodegenerative diseases, coronary diseases, pulmonary diseases, arthritis, and
*cardioP↑,
*Inflam↓,
*neuroP↑,
*Keap1↓, RES administration resulted in a downregulation of Keap1 expression, therefore, inducing Nrf2 signaling, and leading to a decrease in oxidative damage
*NRF2↑,
*ROS↓,
p62↓, decrease the severity of rheumatoid arthritis by inducing autophagy via p62 downregulation, decreasing the levels of interleukin-1β (IL-1β) and C-reactive protein as well as mitigating angiopoietin-1 and vascular endothelial growth factor (VEGF) path
IL1β↓,
CRP↓,
VEGF↓,
Bcl-2↓, RES downregulates the levels of Bcl-2, MMP-2, and MMP-9, and induces the phosphorylation of extracellular-signal-regulated kinase (ERK)/p-38 and FOXO4
MMP2↓,
MMP9↓,
FOXO4↓,
POLD1↓, The in vivo experiment involving a xenograft model confirmed the ability of RES to reduce tumor growth via POLD1 downregulation
CK2↓, RES reduces the expression of casein kinase 2 (CK2) and diminishes the viability of MCF-7 cells.
MMP↓, Furthermore, RES impairs mitochondrial membrane potential, enhances ROS generation, and induces apoptosis, impairing BC progression
ROS↑,
Apoptosis↑,
TumCCA↑, RES has the capability of triggering cell cycle arrest at S phase and reducing the number of 4T1 BC cells in G0/G1 phase
Beclin-1↓, RES administration promotes cytotoxicity of DOX against BC cells by downregulating Beclin-1 and subsequently inhibiting autophagy
Ki-67↓, Reducing the Ki-67
ATP↓, RES’s administration is responsible for decreasing ATP production and glucose metabolism in MCF-7 cells.
GlutMet↓,
PFK↓, RES decreased PFK activity, preventing glycolysis and glucose metabolism in BC cells and decreasing cellular growth rate
TGF-β↓, RES (12.5–100 µM) inhibited TGF-β signaling and reduced the expression levels of its downstream targets that include Smad2 and Smad3 and as a result impaired the progression of BC cells.
SMAD2↓,
SMAD3↓,
Vim?, a significant decrease in the levels of vimentin, Snail1 and Slug occurred, while E-cadherin levels increased to suppress EMT and metastasis of BC cells.
Snail↓,
Slug↓,
E-cadherin↑,
EMT↓,
Zeb1↓, a significant decrease in the levels of vimentin, Snail1 and Slug occurred, while E-cadherin levels increased to suppress EMT and metastasis of BC cells.
Fibronectin↓,
IGF-1↓, RES administration (10 and 20 µM) impaired the migration and invasion of BC cells via inhibiting PI3K/Akt and therefore decreasing IGF-1 expression and preventing the upregulation of MMP-2
PI3K↓,
Akt↓,
HO-1↑, The activation of heme oxygenase-1 (HO-1) signaling by RES reduced MMP-9 expression and prevented metastasis of BC cells
eff↑, RES-loaded gold nanoparticles were found to enhance RES’s ability to reduce MMP-9 expression as compared to RES alone
PD-1↓, RES inhibited PD-1 expression to promote CD8+ T cell activity and enhance Th1 immune responses.
CD8+↑,
Th1 response↑,
CSCs↓, RES has the ability to target CSCs in various tumors
RadioS↑, RES in reversing drug resistance and radio resistance.
SIRT1↑, RES administration (12.5–200 µmol/L) promotes sensitivity of BC cells to DOX by increasing Sirtuin 1 (SIRT1) expression
Hif1a↓, downregulating HIF-1α expression, an important factor in enhancing radiosensitivity
mTOR↓, mTOR suppression
*ROS↓, Studies have reported that selenium (Se), which is one of the essential trace elements of the poultry and participates in the oxidative metabolism, can alleviate Cr(Ⅵ)-induced organ damage by inhibiting oxidative stress,
*NRF2↑, levels of Nrf2, glutathione peroxidase 1 (GPx-1), NAD(P)H: quinone oxidoreductase 1 (NQO1), and mechanistic target of rapamycin (mTOR) in the Se&Cr group was upregulated
*GPx1↑,
*NQO1↑,
*mTOR↑,
*Beclin-1↓, along with decreased expression of Beclin 1, ATG5 and LC3 compared to the Cr group.
*ATG5↓,
*LC3s↓,
*hepatoP↑,
p‑P53↑, Selenite induced phosphorylation of p53 at the vital site Ser15 via p38MAPK and ERK.
Beclin-1↓, The active p53 participated in the decrease of autophagic protein Beclin-1 and LC-3, as well as activation of apoptosis-related caspases.
LC3I↓,
Apoptosis↑,
Casp↑,
Showing Research Papers: 1 to 12 of 12
* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 12
Pathway results for Effect on Cancer / Diseased Cells:
Redox & Oxidative Stress(tgid=1) ⓘ
Catalase↓, 1, Ferroptosis↑, 1, GPx↓, 1, GPx4↓, 1, GSH↓, 1, GSTP1/GSTπ↓, 1, HO-1↑, 2, Iron↑, 1, Keap1↝, 1, lipid-P↑, 2, MDA↑, 1, NADH↓, 1, NRF2↓, 1, NRF2↑, 2, OXPHOS↓, 1, ROS↓, 2, ROS↑, 7, SOD↓, 3, SOD↑, 1, SOD1↑, 1,
Metal & Cofactor Biology(tgid=2) ⓘ
IronCh↑, 1,
Mitochondria & Bioenergetics(tgid=3) ⓘ
ATP↓, 2, BOK↑, 1, CDC25↓, 1, ETC↓, 1, FGFR1↓, 2, MMP↓, 4, mtDam↑, 2, XIAP↓, 1,
Core Metabolism/Glycolysis(tgid=4) ⓘ
AKT1↓, 1, ALAT↓, 1, AMPK↑, 2, cMyc↓, 2, FASN↓, 1, G6PD↓, 1, GLS↓, 1, GlucoseCon↓, 1, GlutMet↓, 1, Glycolysis↓, 2, HK2↓, 1, lactateProd↑, 1, LDHA↓, 1, PDK1↓, 2, PFK↓, 1, PKM2↓, 1, POLD1↓, 1, SCD1↓, 1, SIRT1↑, 1, SREBP2↓, 1, Warburg↓, 1,
Cell Death(tgid=5) ⓘ
Akt↓, 5, Akt↑, 1, Apoptosis↑, 8, BAD↑, 1, BAX↓, 1, BAX↑, 1, Bax:Bcl2↑, 1, Bcl-2↓, 4, Bcl-xL↓, 1, BID↑, 1, Casp↑, 2, Casp↝, 1, cl‑Casp12↑, 1, Casp3↑, 2, cl‑Casp3↑, 1, Casp9↑, 2, cl‑Casp9↑, 1, CK2↓, 2, Cyt‑c↑, 2, DR5↑, 1, FADD↑, 1, Fas↑, 2, Ferroptosis↑, 1, hTERT/TERT↓, 1, MAPK↓, 1, Mcl-1↓, 1, MCT1↓, 1, NAIP↓, 1, NOXA↑, 1, PUMA↑, 1, Telomerase↓, 1,
Transcription & Epigenetics(tgid=7) ⓘ
tumCV↓, 2,
Protein Folding & ER Stress(tgid=8) ⓘ
eIF2α↑, 1, ER Stress↑, 2, ERStress↑, 1, GRP78/BiP↑, 1, PERK↑, 1,
Autophagy & Lysosomes(tgid=9) ⓘ
ATG3↓, 1, Beclin-1↓, 9, Beclin-1↑, 2, LC3‑Ⅱ/LC3‑Ⅰ↓, 1, LC3I↓, 1, LC3II↓, 1, LC3II↑, 2, p62↓, 2, p62↑, 3, TumAuto↑, 2,
DNA Damage & Repair(tgid=10) ⓘ
DNAdam↑, 1, DNMTs↓, 1, P53↑, 2, P53↝, 1, p‑P53↑, 1, PARP↑, 1, cl‑PARP↑, 1, PCNA↓, 1, γH2AX↑, 1,
Cell Cycle & Senescence(tgid=11) ⓘ
CDK2↓, 2, CDK4↓, 2, TumCCA↑, 5,
Proliferation, Differentiation & Cell State(tgid=12) ⓘ
CSCs↓, 2, EMT↓, 4, FGF↓, 1, FGFR2↓, 1, FOXO4↓, 1, GSK‐3β↑, 1, HDAC↓, 1, IGF-1↓, 1, miR-34a↓, 1, mTOR↓, 2, p‑mTOR↑, 1, NOTCH1↓, 1, PI3K↓, 6, PTEN↑, 1, STAT3↓, 3, p‑STAT3↓, 1, TumCG↓, 2, TumCG↑, 1, tyrosinase↓, 1, Wnt↓, 1,
Migration(tgid=13) ⓘ
Akt2↓, 1, AP-1↓, 1, Ca+2↑, 2, E-cadherin↓, 1, E-cadherin↑, 2, Fibronectin↓, 1, Ki-67↓, 2, MMP2↓, 2, MMP9↓, 2, MMPs↓, 1, N-cadherin↓, 1, PDGF↓, 1, Slug↓, 2, SMAD2↓, 1, SMAD3↓, 1, Snail↓, 1, TGF-β↓, 1, TIMP1↑, 1, TRIB3↑, 1, TumCI↓, 3, TumCMig↓, 2, TumCP↓, 6, TumMeta↓, 4, TumMeta↑, 1, Vim?, 1, Vim↓, 2, Zeb1↓, 1, β-catenin/ZEB1↓, 1,
Angiogenesis & Vasculature(tgid=14) ⓘ
angioG↓, 2, ATF4↑, 1, Hif1a↓, 4, VEGF↓, 3,
Barriers & Transport(tgid=15) ⓘ
GLUT1↓, 1, P-gp↓, 1,
Immune & Inflammatory Signaling(tgid=16) ⓘ
COX2↓, 2, CRP↓, 1, IL1β↓, 1, Imm↑, 1, NF-kB↓, 2, NF-kB↑, 1, NK cell↑, 1, PD-1↓, 1, Th1 response↑, 1,
Hormonal & Nuclear Receptors(tgid=20) ⓘ
CDK6↓, 1,
Drug Metabolism & Resistance(tgid=21) ⓘ
ChemoSen↑, 2, eff↑, 3, RadioS↑, 2, selectivity↑, 1,
Clinical Biomarkers(tgid=22) ⓘ
ALAT↓, 1, AST↓, 1, CRP↓, 1, GutMicro↑, 1, hTERT/TERT↓, 1, Ki-67↓, 2, TG/TAG↓, 1, TRIB3↑, 1,
Functional Outcomes(tgid=23) ⓘ
AntiCan↑, 1, chemoPv↑, 1,
Infection & Microbiome(tgid=24) ⓘ
CD8+↑, 1,
Total Targets: 188
Pathway results for Effect on Normal Cells:
NA, unassigned(tgid=0) ⓘ
AntiBio↑, 1,
Redox & Oxidative Stress(tgid=1) ⓘ
antiOx↑, 3, Catalase↑, 1, GPx↑, 2, GPx1↑, 1, GSH↑, 3, GSTs↑, 1, HO-1↑, 1, Keap1↓, 1, lipid-P↓, 1, NQO1↑, 1, NRF2↑, 4, ROS↓, 5, SOD↑, 3, TBARS↓, 1,
Mitochondria & Bioenergetics(tgid=3) ⓘ
ATP↓, 1,
Core Metabolism/Glycolysis(tgid=4) ⓘ
ALAT↓, 1, AMPK↓, 1, LDHA↑, 1, NAD↓, 1,
Cell Death(tgid=5) ⓘ
Akt↓, 1, Apoptosis↓, 1, BAX↓, 1, Bcl-2↓, 1, Casp3↓, 1, Casp9↓, 1, Cyt‑c↓, 1, GADD34↓, 1, iNOS↓, 2, survivin↓, 1,
Protein Folding & ER Stress(tgid=8) ⓘ
CHOP↓, 1,
Autophagy & Lysosomes(tgid=9) ⓘ
ATG5↓, 1, Beclin-1↓, 3, LC3II↓, 1, LC3s↓, 1,
DNA Damage & Repair(tgid=10) ⓘ
P53↓, 1,
Cell Cycle & Senescence(tgid=11) ⓘ
P21↓, 1,
Proliferation, Differentiation & Cell State(tgid=12) ⓘ
mTOR↑, 1,
Angiogenesis & Vasculature(tgid=14) ⓘ
ATF4↓, 1, NO↓, 2,
Immune & Inflammatory Signaling(tgid=16) ⓘ
COX2↓, 1, IFN-γ↓, 1, IL10↓, 1, IL17↓, 1, IL1β↓, 1, IL6↓, 1, Imm↓, 1, Inflam↓, 4, NF-kB↓, 2, PGE2↓, 1, TNF-α↓, 1,
Synaptic & Neurotransmission(tgid=18) ⓘ
AChE↓, 1, BDNF↓, 1,
Protein Aggregation(tgid=19) ⓘ
XO↓, 1,
Drug Metabolism & Resistance(tgid=21) ⓘ
BioAv↓, 3, BioAv↑, 1,
Clinical Biomarkers(tgid=22) ⓘ
ALAT↓, 1, AST↓, 1, IL6↓, 1,
Functional Outcomes(tgid=23) ⓘ
AntiCan↑, 1, AntiDiabetic↑, 1, cardioP↑, 1, hepatoP↑, 2, memory↑, 1, neuroP↑, 5, toxicity↝, 1,
Total Targets: 66
Scientific Paper Hit Count for: Beclin-1, Beclin-1 (BECN1 gene)
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#:% Target#:30 State#:% Dir#:1
wNotes=on sortOrder:rid,rpid
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