Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Schisandrin B exhibits anti-proliferative effects by inducing ferroptosis in pancreatic cancer

ABSTRACT: Sch B exerts anti-proliferative effects at least partially by inducing ACSL4-dependent ferroptosis in PC

ORGANISM(S): Homo Sapiens

SUBMITTER: Fengjin Li

PROVIDER: PXD078099 | iProX | Wed May 06 00:00:00 BST 2026

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Publications

Schisandrin B exhibits anti‑proliferative effects by inducing ferroptosis in pancreatic cancer.

Li Fengjin F Fu Jiacai J Lin Xiaowei X Liu Yanting Y Yang Lu L Li Yuxin Y Peng Tieli T Qi Ling L

Oncology reports 20260619 2

Pancreatic cancer (PC) is a lethal malignant tumor of the digestive system with a low survival rate. Current therapies provide only modest benefits for patients and new therapeutic options are urgently needed. Schisandrin B (Sch B) has demonstrated novel antitumor activity in several preclinical models; however, its effects on PC remain unclear. In the present study, the anti‑proliferative effects of Sch B <i>in vitro </i>were evaluated in PC cell lines. The underlying molecular mechanisms were ...[more]

PMID: 42318966

Similar Datasets

Schisandrin B exhibits anti-proliferative effects by inducing ferroptosis in pancreatic cancer

Project description:Schisandrin B exhibits anti-proliferative effects by inducing ferroptosis in pancreatic cancer

| PRJNA1399323 | ENA

Schisandrin B exhibits anti-proliferative effects by inducing ferroptosis in pancreatic cancer

Project description:Pancreatic cancer (PC) is a lethal malignancy of the digestive system with an extremely low survival rate. Schisandrin B (Sch B) has demonstrated novel pre-clinical antitumor activity in several animal tumor models. However, it remains unclear whether Sch B exerts antitumor effects in PC. The molecular mechanisms underlying the antitumor properties of Sch B were explored using RNA sequencing.

2026-05-21 | GSE315793 | GEO

Interactome of ferroptosis pathways genes

Project description:We conducted a proteomic interactome analysis of well-known regulators of ferroptosis, ACSL4, LPCAT3, ALOX12, ALOX15, PEBP1, NCOA4, GCH1, FSP1, DHODH, SLC7A11, GCLC, GCLM, GSS, and GPX4. Take LPCAT3 as an example, we uncovered an opposing role of its binding protein CEPT1 in suppressing ferroptosis.

2024-10-17 | PXD035146 | Pride

VSTM2L protects prostate cancer cells against ferroptosis via inhibiting VDAC1 oligomerization and maintaining mitochondria homeostasis

Project description:Mitochondria play a critical role in initiating and amplifying ferroptosis. VDAC1 embedded in the mitochondrial outer membrane, exerts a crucial role in regulation of ferroptosis. However, the mechanisms of VDAC1 oligomerization in regulating ferroptosis are not well elucidated. Here, we identified that VSTM2L, a novel VDAC1 binding protein, is positively associated with prostate cancer (PCa) progression, and a key regulator of ferroptosis. Moreover, VSTM2L knockdown in PCa cells enhanced the sensibility of RSL3-induced ferroptosis. Mechanistically, VSTM2L forms complex with VDAC1 and HK2, enhancing their binding affinity and preventing VDAC1 oligomerization, thereby inhibiting ferroptosis and maintaining mitochondria homeostasis in vitro and in vivo. Collectively, our findings reveal a pivotal role for VSTM2L in driving ferroptosis resistance and highlight its potential as a ferroptosis-inducing therapeutic target for the treatment of PCa.

2025-05-07 | PXD052173 | Pride

Elimination of aggressive cancers by a ferroptosis-inducing PROTAC

Project description:Elimination of aggressive cancers by a ferroptosis-inducing PROTAC

| PRJNA1197519 | ENA

Polyamine Depletion Inhibits Ewing Sarcoma Metastasis by Inducing Ferroptosis

Project description:Polyamine Depletion Inhibits Ewing Sarcoma Metastasis by Inducing Ferroptosis

| PRJNA1144979 | ENA

Acsl4 Determines Ferroptosis Sensitivity by Shaping Cellular Lipid Composition

Project description:Ferroptosis is a form of regulated necrotic cell death controlled by glutathione peroxidase 4 (GPX4). At present, mechanisms that could predict sensitivity and/or resistance and that may be exploited to modulate this form of cell death are needed. We applied two independent approaches, a genome-wide CRISPR-based genetic screen and microarray analysis of ferroptosis-resistant cell lines to uncover acyl-CoA synthetase long-chain family member 4 (Acsl4) as an essential component for ferroptosis execution.

2017-06-01 | GSE86384 | GEO

Nrf1 deficiency promotes tubular ferroptosis by regulating ACSL4 in cisplatin-induced acute kidney injury

Project description:Nrf1 is a transcription factor that is highly conserved and reacts to oxidative, proteotoxic and endoplasmic reticulum stress in cells; nonetheless, its function in the context of acute kidney injury (AKI) remains unclear. Using a model of cisplatin-induced nephrotoxicity in vitro and in vivo, we found that the expression of Nrf1, which is expressed at high levels in renal tubular cells, was significantly downregulated after cisplatin treatment. Proximal tubule-specific Nrf1 knockout worsened and Nrf1 overexpression attenuated cisplatin-induced (CI)-AKI. RNA sequencing analysis revealed that Nrf1 overexpression decreased the number of transcripts involved in cell death, specifically those associated with ferroptosis, after cisplatin treatment. Furthermore, ferroptosis responses, characterized by increased lipid peroxidation and iron content and decreased FPN, XCT and glutathione peroxidase 4 levels, were attenuated in Nrf1-overexpressing HK-2 cells but worsened in Nrf1-knockout mice and Nrf1-knockdown HK-2 cells. Moreover, lipidomic and RNA sequencing results indicated that Nrf1 regulated the levels of polyunsaturated fatty acids (PUFAs) and inhibited the expression of ACSL4. Additionally, ChIP experiments revealed that Nrf1 bound to the promoter region of ACSL4, thereby inhibiting its transcription. Furthermore, inhibitors of ACSL4 significantly reduced the sensitivity of HK-2 cells to ferroptosis induced by Nrf1 knockdown. Collectively, these findings suggest that Nrf1 is a novel target for inhibiting ferroptosis in renal tubule cells by suppressing the transcription and expression of ACSL4, thereby reducing PUFA levels. Consequently, activators developed for Nrf1 may hold therapeutic potential in the treatment of patients with CI-AKI.

2025-01-01 | GSE282573 | GEO

Myeloid FtH deficiency accelerates kidney disease by inducing Snca and ferroptosis

Project description:This study aimed to investigate impact of myeloid ferritin heavy chain (FtH) deletion on iron trafficking in kidney health and disease. Myeloid FtH deletion (FtHΔ/Δ) led to upregulation of synuclein-α (Snca) as the only iron-binding protein. When exposed to kidney injury, FtHΔ/Δ mice exhibited significantly worse kidney function. Transcriptome analysis identified ferroptosis as a key pathway triggered by FtH deletion. This was confirmed by elevated expression of ferroptosis-related genes, oxidative stress markers, and increased iron deposition in the kidneys. The latter was mediated via reprogramming of macrophages to an iron-recycling phenotype by inducing Spic. Mechanistically, we demonstrate ferrireductase activity of monomeric Snca acts as a catalyst triggering oxidative stress and ferroptosis. Moreover, kidney accumulation of Snca is promoted in kidney diseases marked by heavy leukocyte infiltration in both mice and humans. These findings emphasize role of FtH in regulating iron metabolism and promoting kidney repair by suppressing Snca and Spic.

2025-03-17 | GSE291562 | GEO

Phospholipids with two polyunsaturated fatty acyl tails drive ferroptosi.

Project description:Phospholipids containing polyunsaturated fatty acyl tails (PL-PUFAs) are susceptible to lipid peroxidation by reactive oxygen species, lipoxygenases, and radical species. The accumulation of peroxidized lipids in cell membranes overwhelms endogenous lipid repair processes and triggers ferroptosis. We discovered that phospholipids with both PUFA tails (PL-PUFA2s) acted as key drivers of ferroptosis in numerous cancer cell lines, compared with phospholipids with a single PUFA tail (PL-PUFA1s), which were substantially less capable of inducing ferroptosis. We found that exogenously supplied phosphatidylcholine with two PUFA tails (PC-PUFA2) was rapidly incorporated into and remodeled membranes in cell lipids. Moreover, PC-PUFA2s were enriched upon free PUFA treatment, suggesting a key role in driving free-PUFA-initiated ferroptosis. We examined the protein-binding profile of PC-PUFA2 and found a specific interaction with the mitochondrial electron transport chain complex I. We confirmed that PC-PUFA2s accumulate in mitochondria and induce production of mitochondrial ROS, which then spread to the endoplasmic reticulum. Depletion of mitochondria through mitophagy eliminated the enhanced potency of PC-PUFA2s over PC-PUFA1s in driving ferroptosis, consistent with mitochondria being the key target of PC-PUFA2s. PC-PUFA2s are thus important lipid markers and drivers of ferroptosis and may serve as future biomarkers and therapeutic targets for modulating ferroptosis in pathological contexts.

2025-05-06 | PXD041993 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data