Evidence map›Paper›PMID 37995078›Full record

ArticleMolecular neurobiology2024

A Disintegrin and Metalloproteinase-8 Protects Against Erastin-Induced Neuronal Ferroptosis via Activating Nrf2/HO-1/FTH1 Signaling Pathway.

Zhanyang Qian, Qinyang Zhang, Pengfei Li, Yang Li, Yanan Zhang, Rulin Li, Tianyu Zhao, Mingjie Xia, Yongyi Chen, Xin Hong

Abstract read
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In one paragraph

Article in Molecular neurobiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Current issues in molecular biology · 2026
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  2. Molecules (Basel, Switzerland) · 2026
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  5. Review
  6. Glycine Alleviates HMolecular neurobiology · 2026
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  7. Review
  8. Article
  9. Article
  10. Article
  11. Ursonic Acid Ameliorates HMolecular neurobiology · 2025
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Zhanyang QianDepartment of Orthopedics, Taizhou People Hospital, Nanjing Medical University, Taizhou, China.
Qinyang ZhangDepartment of Orthopedics, Taizhou People Hospital, Nanjing Medical University, Taizhou, China.
Pengfei LiDepartment of Orthopedics, Taizhou People Hospital, Nanjing Medical University, Taizhou, China.
Yang LiDepartment of Orthopedics, Taizhou People Hospital, Nanjing Medical University, Taizhou, China.
Yanan ZhangDepartment of Orthopedics, Taizhou People Hospital, Nanjing Medical University, Taizhou, China.
Rulin LiDepartment of Orthopedics, Taizhou People Hospital, Nanjing Medical University, Taizhou, China.
Tianyu ZhaoDepartment of Orthopedics, Taizhou People Hospital, Nanjing Medical University, Taizhou, China.
Mingjie XiaDepartment of Spine Surgery, The Second Affiliated Hospital of Nantong University, Nantong First People's Hospital, Nantong, China. xmjjj1997@126.com.
Yongyi ChenDepartment of Anesthesiology, Jiangsu Cancer Hospital & Jiangsu Institute of Cancer Research & The Affiliated Cancer Hospital of Nanjing Medical University, Nanjing, China. plcyy2016@126.com.
Xin HongDepartment of Orthopedics, Zhongda Hospital of Southeast University, Nanjing, China. xinhong102400@163.com.ORCID http://orcid.org/0000-0003-3115-972X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ferroptosis is a type of iron-dependent programmed cell death caused by the imbalance between oxidants and antioxidants. A disintegrin and metalloproteinase-8 (ADAM8) is a metalloproteinase that mediates cell adhesion, cell migration, and proteolytic activity. However, the molecular mechanism of ADAM8 regulating ferroptosis after neural disorder is unclear, especially in the neuron. In the present study, we identified the protective role of ADAM8 in Erastin-induced ferroptosis in vitro of the HT22 cells. It was found that overexpression of ADAM8 resulted in upregulated expression of GPX4 and FTH1 along with the decreased reactive oxygen species (ROS) production and reduced neuronal death; however, knockdown of ADAM8 resulted in an opposite. Mechanically, using the Nrf2 activator NK-252 and inhibitor nrf2-IN-1, we dmonstrated that ADAM8 regulates Erastin-mediated neuronal ferroptosis via activating the Nrf2/HO-1/FTH1 signaling pathway. In conclusion, the current study suggested that ADAM8 inhibited Erastin-induced neuronal ferroptosis through activating the Nrf2/HO-1/FTH1 signaling pathway, playing a protective role in vitro of the HT22 cell line. ADAM8 may be a promising and feasible target for neuronal survival in diseases of neural disorder.

Indexed as

ADAM ProteinsFerroptosisHeme Oxygenase-1Membrane ProteinsNeuronsNF-E2-Related Factor 2PiperazinesSignal TransductionAnimalsAntigens, CDCell LineMiceReactive Oxygen SpeciesAdam8 protein, mouseADAM ProteinsAntigens, CDerastinHeme Oxygenase-1Membrane ProteinsNfe2l2 protein, mouseNF-E2-Related Factor 2PiperazinesReactive Oxygen SpeciesA disintegrin and metalloproteinase-8ErastinFerroptosisNrf2/HO-1 pathwayReactive oxygen species

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.