[Corrigendum] Neurotoxin βNmethylaminoLalanine induces endoplasmic reticulum stressmediated neuronal apoptosis

Haiying Shen1, Kiyoon Kim1, Yoojung Oh1

  • 1Department of Biochemistry and Molecular Biology (BK21 Project), Medical Research Center for Bioreaction to Reactive Oxygen Species and Biomedical Science Institute, School of Medicine, Kyung Hee University, Seoul 130‑701, Republic of Korea.

Insights

This corrigendum corrects an error in Fig. 4A regarding heat shock protein 70 (HSP70) and its effect on neuronal death induced by beta-N-methylamino-L-alanine (BMAA). The corrected figure does not alter the study's conclusions.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cellular Stress Response

Background:

  • Beta-N-methylamino-L-alanine (BMAA) is a neurotoxin implicated in neurodegenerative diseases.
  • Endoplasmic reticulum (ER) stress is a key mechanism in BMAA-induced neuronal death.
  • Heat shock protein 70 (HSP70) is a known cellular protectant against various stressors.

Purpose of the Study:

  • To investigate the role of HSP70 in mitigating ER stress-mediated neuronal death induced by BMAA.
  • To present a corrected figure (Fig. 4A) clarifying the experimental results.

Main Methods:

  • Overexpression of HSP70 in neuronal cells.
  • Induction of ER stress using BMAA.
  • Assessment of neuronal viability and cell death markers.
  • Western blot analysis to evaluate protein expression.

Main Results:

  • The corrected Fig. 4A demonstrates that HSP70 overexpression suppresses BMAA-induced neuronal death.
  • Specific band images in the HA panel of Fig. 1A were identified as incorrectly compiled.
  • The corrected figure accurately represents the protective effect of HSP70 against BMAA toxicity.

Conclusions:

  • HSP70 overexpression effectively protects against ER stress-induced neuronal death caused by BMAA.
  • The correction of Fig. 4A ensures accurate data presentation without impacting the study's overall findings or conclusions.

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