Dysregulation of schizophrenia‐related aquaporin 3 through disruption of paranode influences neuronal viability

Myelinated axons segregate the axonal membrane into four defined regions: the node of Ranvier, paranode, juxtaparanode, and internode. The paranodal junction consists of specific component proteins, such as neurofascin155 (NF155) on the glial side, and Caspr and Contactin on the axonal side. Althoug...

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Published inJournal of neurochemistry Vol. 147; no. 3; pp. 395 - 408
Main Authors Kunisawa, Kazuo, Shimizu, Takeshi, Kushima, Itaru, Aleksic, Branko, Mori, Daisuke, Osanai, Yasuyuki, Kobayashi, Kenta, Taylor, Anna M., Bhat, Manzoor A., Hayashi, Akiko, Baba, Hiroko, Ozaki, Norio, Ikenaka, Kazuhiro
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LanguageEnglish
Published England Blackwell Publishing Ltd 01.11.2018
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Abstract Myelinated axons segregate the axonal membrane into four defined regions: the node of Ranvier, paranode, juxtaparanode, and internode. The paranodal junction consists of specific component proteins, such as neurofascin155 (NF155) on the glial side, and Caspr and Contactin on the axonal side. Although paranodal junctions are thought to play crucial roles in rapid saltatory conduction and nodal assembly, the role of their interaction with neurons is not fully understood. In a previous study, conditional NF155 knockout in oligodendrocytes led to disorganization of the paranodal junctions. To examine if disruption of paranodal junctions affects neuronal gene expression, we prepared total RNA from the retina of NF155 conditional knockout, and performed expression analysis. We found that the expression level of 433 genes changed in response to paranodal junction ablation. Interestingly, expression of aquaporin 3 (AQP3) was significantly reduced in NF155 conditional knockout mice, but not in cerebroside sulfotransferase knockout (CST‐KO) mice, whose paranodes are not originally formed during development. Copy number variations have an important role in the etiology of schizophrenia (SCZ). We observed rare duplications of AQP3 in SCZ patients, suggesting a correlation between abnormal AQP3 expression and SCZ. To determine if AQP3 over‐expression in NF155 conditional knockout mice influences neuronal function, we performed adeno‐associated virus (AAV)‐mediated over‐expression of AQP3 in the motor cortex of mice and found a significant increase in caspase 3‐dependent neuronal apoptosis in AQP3‐transduced cells. This study may provide new insights into therapeutic approaches for SCZ by regulating AQP3 expression, which is associated with paranodal disruption. The aquaporin 3 was related to the list of genes identified with copy number variations of schizophrenia, suggesting a correlation between abnormal aquaporin 3 expression and schizophrenia. We found that aquaporin 3 was sensitive to paranodal abnormalities. We further showed that dysregulation of aquaporin 3 expression through disruption of paranode affected neuronal viability. Further understanding of aquaporin 3 function may provide new insights into the etiology of schizophrenia caused by oligodendrocyte abnormalities and potential therapeutic approaches.
AbstractList Myelinated axons segregate the axonal membrane into four defined regions: the node of Ranvier, paranode, juxtaparanode, and internode. The paranodal junction consists of specific component proteins, such as neurofascin155 (NF155) on the glial side, and Caspr and Contactin on the axonal side. Although paranodal junctions are thought to play crucial roles in rapid saltatory conduction and nodal assembly, the role of their interaction with neurons is not fully understood. In a previous study, conditional NF155 knockout in oligodendrocytes led to disorganization of the paranodal junctions. To examine if disruption of paranodal junctions affects neuronal gene expression, we prepared total RNA from the retina of NF155 conditional knockout, and performed expression analysis. We found that the expression level of 433 genes changed in response to paranodal junction ablation. Interestingly, expression of aquaporin 3 (AQP3) was significantly reduced in NF155 conditional knockout mice, but not in cerebroside sulfotransferase knockout (CST‐KO) mice, whose paranodes are not originally formed during development. Copy number variations have an important role in the etiology of schizophrenia (SCZ). We observed rare duplications of AQP3 in SCZ patients, suggesting a correlation between abnormal AQP3 expression and SCZ. To determine if AQP3 over‐expression in NF155 conditional knockout mice influences neuronal function, we performed adeno‐associated virus (AAV)‐mediated over‐expression of AQP3 in the motor cortex of mice and found a significant increase in caspase 3‐dependent neuronal apoptosis in AQP3‐transduced cells. This study may provide new insights into therapeutic approaches for SCZ by regulating AQP3 expression, which is associated with paranodal disruption.
Myelinated axons segregate the axonal membrane into four defined regions: the node of Ranvier, paranode, juxtaparanode and internode. The paranodal junction consists of specific component proteins, such as neurofascin155 (NF155) on the glial side, and Caspr and Contactin on the axonal side. Although paranodal junctions are thought to play crucial roles in rapid saltatory conduction and nodal assembly, the role of their interaction with neurons is not fully understood. In a previous study, conditional NF155 knockout in oligodendrocytes led to disorganization of the paranodal junctions. To examine if disruption of paranodal junctions affects neuronal gene expression, we prepared total RNA from the retina of NF155 conditional knockout, and performed expression analysis. We found that the expression level of 433 genes changed in response to paranodal junction ablation. Interestingly, expression of aquaporin 3 ( AQP3 ) was significantly reduced in NF155 conditional knockout mice, but not in cerebroside sulfotransferase knockout ( CST-KO ) mice, whose paranodes are not originally formed during development. Copy number variations (CNVs) have an important role in the etiology of schizophrenia (SCZ). We observed rare duplications of AQP3 in SCZ patients, suggesting a correlation between abnormal AQP3 expression and SCZ. To determine if AQP3 overexpression in NF155 conditional knockout mice influences neuronal function, we performed adeno-associated virus (AAV)-mediated overexpression of AQP3 in the motor cortex of mice and found a significant increase in caspase-3-dependent neuronal apoptosis in AQP3 -transduced cells. This study may provide new insights into therapeutic approaches for SCZ by regulating AQP3 expression, which is associated with paranodal disruption. The aquaporin 3 was related to the list of genes identified with copy number variations of schizophrenia, suggesting a correlation between abnormal aquaporin 3 expression and schizophrenia. We found that aquaporin 3 was sensitive to paranodal abnormalities. We further showed that dysregulation of aquaporin 3 expression through disruption of paranode affected neuronal viability. Further understanding of aquaporin 3 function may provide new insights into the etiology of schizophrenia caused by oligodendrocyte abnormalities and potential therapeutic approaches.
Myelinated axons segregate the axonal membrane into four defined regions: the node of Ranvier, paranode, juxtaparanode, and internode. The paranodal junction consists of specific component proteins, such as neurofascin155 (NF155) on the glial side, and Caspr and Contactin on the axonal side. Although paranodal junctions are thought to play crucial roles in rapid saltatory conduction and nodal assembly, the role of their interaction with neurons is not fully understood. In a previous study, conditional NF155 knockout in oligodendrocytes led to disorganization of the paranodal junctions. To examine if disruption of paranodal junctions affects neuronal gene expression, we prepared total RNA from the retina of NF155 conditional knockout, and performed expression analysis. We found that the expression level of 433 genes changed in response to paranodal junction ablation. Interestingly, expression of aquaporin 3 (AQP3) was significantly reduced in NF155 conditional knockout mice, but not in cerebroside sulfotransferase knockout (CST‐KO) mice, whose paranodes are not originally formed during development. Copy number variations have an important role in the etiology of schizophrenia (SCZ). We observed rare duplications of AQP3 in SCZ patients, suggesting a correlation between abnormal AQP3 expression and SCZ. To determine if AQP3 over‐expression in NF155 conditional knockout mice influences neuronal function, we performed adeno‐associated virus (AAV)‐mediated over‐expression of AQP3 in the motor cortex of mice and found a significant increase in caspase 3‐dependent neuronal apoptosis in AQP3‐transduced cells. This study may provide new insights into therapeutic approaches for SCZ by regulating AQP3 expression, which is associated with paranodal disruption. The aquaporin 3 was related to the list of genes identified with copy number variations of schizophrenia, suggesting a correlation between abnormal aquaporin 3 expression and schizophrenia. We found that aquaporin 3 was sensitive to paranodal abnormalities. We further showed that dysregulation of aquaporin 3 expression through disruption of paranode affected neuronal viability. Further understanding of aquaporin 3 function may provide new insights into the etiology of schizophrenia caused by oligodendrocyte abnormalities and potential therapeutic approaches.
Myelinated axons segregate the axonal membrane into four defined regions: the node of Ranvier, paranode, juxtaparanode, and internode. The paranodal junction consists of specific component proteins, such as neurofascin155 (NF155) on the glial side, and Caspr and Contactin on the axonal side. Although paranodal junctions are thought to play crucial roles in rapid saltatory conduction and nodal assembly, the role of their interaction with neurons is not fully understood. In a previous study, conditional NF155 knockout in oligodendrocytes led to disorganization of the paranodal junctions. To examine if disruption of paranodal junctions affects neuronal gene expression, we prepared total RNA from the retina of NF155 conditional knockout, and performed expression analysis. We found that the expression level of 433 genes changed in response to paranodal junction ablation. Interestingly, expression of aquaporin 3 (AQP3) was significantly reduced in NF155 conditional knockout mice, but not in cerebroside sulfotransferase knockout (CST-KO) mice, whose paranodes are not originally formed during development. Copy number variations have an important role in the etiology of schizophrenia (SCZ). We observed rare duplications of AQP3 in SCZ patients, suggesting a correlation between abnormal AQP3 expression and SCZ. To determine if AQP3 over-expression in NF155 conditional knockout mice influences neuronal function, we performed adeno-associated virus (AAV)-mediated over-expression of AQP3 in the motor cortex of mice and found a significant increase in caspase 3-dependent neuronal apoptosis in AQP3-transduced cells. This study may provide new insights into therapeutic approaches for SCZ by regulating AQP3 expression, which is associated with paranodal disruption.
Author Baba, Hiroko
Mori, Daisuke
Hayashi, Akiko
Shimizu, Takeshi
Kushima, Itaru
Kobayashi, Kenta
Ozaki, Norio
Ikenaka, Kazuhiro
Aleksic, Branko
Kunisawa, Kazuo
Osanai, Yasuyuki
Bhat, Manzoor A.
Taylor, Anna M.
AuthorAffiliation 3 Brain and Mind Research Center, Nagoya University, Nagoya 466-8550, Japan
5 Department of Cellular and Integrative Physiology, School of Medicine, University of Texas Health Science Center, San Antonio 78229-3900, USA
1 Division of Neurobiology and Bioinformatics, National Institute for Physiological Sciences, Okazaki 444-8787, Japan
6 Department of Molecular Neurobiology, Tokyo University of Pharmacy and Life Sciences, Hachioji 192-0392, Japan
7 SOKENDAI (The Graduate University for Advanced Studies), Okazaki 444-8787, Japan
2 Department of Psychiatry, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan
4 Section of Viral Vector Development, National Institute for Physiological Sciences, Okazaki 444-8585, Japan
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Issue 3
Keywords copy number variant
aquaporin 3
paranodal junction
schizophrenia
neurofascin155
multiple sclerosis
Language English
License 2018 International Society for Neurochemistry.
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Notes Present address: Department of Neurophysiology and Brain Science, Graduate School of Medical Sciences, Nagoya City University, Nagoya, Aichi 467-8601, Japan
DR. TAKESHI SHIMIZU (Orcid ID : 0000-0003-1041-1199)
DR. KAZUO KUNISAWA (Orcid ID : 0000-0002-4786-9681)
ORCID 0000-0003-1041-1199
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2009; 4
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Snippet Myelinated axons segregate the axonal membrane into four defined regions: the node of Ranvier, paranode, juxtaparanode, and internode. The paranodal junction...
Myelinated axons segregate the axonal membrane into four defined regions: the node of Ranvier, paranode, juxtaparanode and internode. The paranodal junction...
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pubmed
wiley
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StartPage 395
SubjectTerms Ablation
Animals
Apoptosis
Aquaporin 3
Aquaporin 3 - metabolism
Aquaporins
Axons
Axons - metabolism
Axons - pathology
Caspase
Caspase 3 - genetics
Caspase 3 - metabolism
Caspase-3
Cell Adhesion Molecules - biosynthesis
Cell Adhesion Molecules - genetics
Cell Survival
Conduction
Contactin
Copy number
copy number variant
Cortex (motor)
Dependovirus - genetics
Disruption
DNA Copy Number Variations
Etiology
Female
Gene Duplication
Gene Expression
Male
Mental disorders
Mice
Mice, Knockout
Mice, Transgenic
Motor Cortex - metabolism
multiple sclerosis
Nerve Growth Factors - biosynthesis
Nerve Growth Factors - genetics
neurofascin155
Neuronal-glial interactions
Neurons - metabolism
Neurons - pathology
Oligodendrocytes
paranodal junction
Proteins
Retina
Ribonucleic acid
RNA
Rodents
Schizophrenia
Schizophrenia - metabolism
Schizophrenia - pathology
Sulfotransferase
Viability
Viruses
Title Dysregulation of schizophrenia‐related aquaporin 3 through disruption of paranode influences neuronal viability
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fjnc.14553
https://www.ncbi.nlm.nih.gov/pubmed/30025158
https://www.proquest.com/docview/2126549665
https://pubmed.ncbi.nlm.nih.gov/PMC6205917
Volume 147
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