Calcineurin Activation by Prion Protein Induces Neurotoxicity via Mitochondrial Reactive Oxygen Species

Prion diseases are caused by PrPsc accumulation in the brain, which triggers dysfunctional mitochondrial injury and reactive oxygen species (ROS) generation in neurons. Recent studies on prion diseases suggest that endoplasmic reticulum (ER) stress induced by misfolding proteins such as misfolded pr...

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Published inOxidative medicine and cellular longevity Vol. 2021; no. 1; p. 5572129
Main Authors Moon, Ji-Hong, Hong, Jeong-Min, Park, Sang-Youel
Format Journal Article
LanguageEnglish
Published United States Hindawi 2021
Hindawi Limited
Subjects
Acetylcysteine - pharmacology
Alzheimer's disease
Antibodies
Apoptosis
Apoptosis - drug effects
Calcineurin - metabolism
Cell Line, Tumor
Cytosol - drug effects
Cytosol - metabolism
Endoplasmic reticulum
Flow cytometry
Humans
Medical research
Microscopy
Mitochondria - drug effects
Mitochondria - metabolism
Neurotoxicity
Oxidative stress
Peptides
Peptides - chemical synthesis
Peptides - pharmacology
Phosphatase
Prion Proteins - chemistry
Proteins
Reactive Oxygen Species - metabolism
Tacrolimus - pharmacology
Up-Regulation - drug effects
Variance analysis
Grand Island New York
St Louis Missouri
France
United States > US
Online AccessGet full text

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Abstract Prion diseases are caused by PrPsc accumulation in the brain, which triggers dysfunctional mitochondrial injury and reactive oxygen species (ROS) generation in neurons. Recent studies on prion diseases suggest that endoplasmic reticulum (ER) stress induced by misfolding proteins such as misfolded prion protein results in activation of calcineurin. Calcineurin is a calcium-related protein phosphatase of type 2B that exists in copious quantities in the brain and acts as a critical nodal component in the control of cellular functions. To investigate the relationship between calcineurin and intracellular ROS, we assessed the alteration of CaN and ROS induced by prion peptide (PrP) 106-126. Human prion peptide increased mitochondrial ROS by activating calcineurin, and the inhibition of calcineurin activity protected mitochondrial function and neuronal apoptosis in neuronal cells. These results suggest that calcineurin plays a pivotal role in neuronal apoptosis by mediating mitochondrial injury and ROS in prion diseases.
AbstractList Prion diseases are caused by PrPsc accumulation in the brain, which triggers dysfunctional mitochondrial injury and reactive oxygen species (ROS) generation in neurons. Recent studies on prion diseases suggest that endoplasmic reticulum (ER) stress induced by misfolding proteins such as misfolded prion protein results in activation of calcineurin. Calcineurin is a calcium-related protein phosphatase of type 2B that exists in copious quantities in the brain and acts as a critical nodal component in the control of cellular functions. To investigate the relationship between calcineurin and intracellular ROS, we assessed the alteration of CaN and ROS induced by prion peptide (PrP) 106-126. Human prion peptide increased mitochondrial ROS by activating calcineurin, and the inhibition of calcineurin activity protected mitochondrial function and neuronal apoptosis in neuronal cells. These results suggest that calcineurin plays a pivotal role in neuronal apoptosis by mediating mitochondrial injury and ROS in prion diseases.
Author Hong, Jeong-Min
Park, Sang-Youel
Moon, Ji-Hong
AuthorAffiliation Biosafety Research Institute, College of Veterinary Medicine, Jeonbuk National University, Iksan, Jeonbuk 54596, Republic of Korea
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  organization: Biosafety Research InstituteCollege of Veterinary MedicineJeonbuk National UniversityIksanJeonbuk 54596Republic of Koreacbnu.edu
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ContentType Journal Article
Copyright Copyright © 2021 Ji-Hong Moon et al.
Copyright © 2021 Ji-Hong Moon et al. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. https://creativecommons.org/licenses/by/4.0
Copyright © 2021 Ji-Hong Moon et al. 2021
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– notice: Copyright © 2021 Ji-Hong Moon et al. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. https://creativecommons.org/licenses/by/4.0
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Snippet Prion diseases are caused by PrPsc accumulation in the brain, which triggers dysfunctional mitochondrial injury and reactive oxygen species (ROS) generation in...
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SubjectTerms Acetylcysteine - pharmacology
Alzheimer's disease
Antibodies
Apoptosis
Apoptosis - drug effects
Calcineurin - metabolism
Cell Line, Tumor
Cytosol - drug effects
Cytosol - metabolism
Endoplasmic reticulum
Flow cytometry
Humans
Medical research
Microscopy
Mitochondria - drug effects
Mitochondria - metabolism
Neurotoxicity
Oxidative stress
Peptides
Peptides - chemical synthesis
Peptides - pharmacology
Phosphatase
Prion Proteins - chemistry
Proteins
Reactive Oxygen Species - metabolism
Tacrolimus - pharmacology
Up-Regulation - drug effects
Variance analysis
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Title Calcineurin Activation by Prion Protein Induces Neurotoxicity via Mitochondrial Reactive Oxygen Species
URI https://dx.doi.org/10.1155/2021/5572129
https://www.ncbi.nlm.nih.gov/pubmed/34394828
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Volume 2021
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