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Affiliation |
Faculty of Medicine School of Medicine Department of Medical Sciences, Integrative Physiology |
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Associate Professor |
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External Link |
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WAKAZONO Yoshihiko
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Degree 【 display / non-display 】
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博士（学術） ( 1997.9 総合研究大学院大学 )
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修士（薬学） ( 1994.3 静岡県立大学 )
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学士（薬学） ( 1992.3 静岡県立大学 )
Research Areas 【 display / non-display 】
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Life Science / Neuroscience-general
Papers 【 display / non-display 】
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Wakazono Y, Midorikawa R, Takamiya K
Neuroscience Research 198 21 - 29 2024.1
Language：English Publishing type：Research paper (scientific journal) Publisher：Neuroscience Research
In the present study, we attempted to temporally and quantitatively analyze the functional contributions of Ca2+-permeable (CP) α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) during long-term potentiation (LTP) expression using electrophysiological and pharmacological approaches. In hippocampal CA1 neurons, using 1-naphthyl acetyl spermine (NASPM), a CP-AMPAR antagonist, we began by demonstrating that NASPM-sensitive components, probably including the GluA1 homomer, functionally contributed to about 15% of AMPAR-mediated EPSC amplitude in basal conditions. Then, when NASPM was treated at different time points (3–30 min) after LTP induction, it was found that LTP was almost completely impaired at 3 or 10 min but maintained at 20 or 30 min, although its potentiation was reduced. Further temporal and quantitative analysis revealed that the functional expression of CP-AMPARs began increasing approximately 20 min after LTP induction and reached more than twice the basal level at 30 min. These results suggest that CP-AMPARs in the first 3–10 min of LTP might play an important role in LTP maintenance. Moreover, their decay time was also significantly increased at 30 min, suggesting that CP-AMPARs changed not only quantitatively in LTP but also qualitatively.
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Monitoring the glycosylation of AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate )-type glutamate receptors using specific antibodies reveals a novel regulatory mechanism of N-glycosylation occupancy by molecular chaperones in Mice. Reviewed
Midorikawa R, Takakura D, Morise J, Wakazono Y, Kawasaki N, Oka S, Takamiya K
Journal of neurochemistry e14964 2020.1
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AMPA receptors in the synapse turnover by monomer diffusion. Reviewed
Morise J, Suzuki KGN, Kitagawa A, Wakazono Y, Takamiya K, Tsunoyama TA, Nemoto YL, Takematsu H, Kusumi A, Oka S
Nat Commun. 10 ( 1 ) 2019.11
Language：English Publishing type：Research paper (scientific journal)
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Kandel M., Yamamoto S., Midorikawa R., Morise J., Wakazono Y., Oka S., Takamiya K.
Journal of Neurochemistry 147 ( 6 ) 730 - 747 2018.12
Language：English Publishing type：Research paper (scientific journal) Publisher：Journal of Neurochemistry
© 2018 International Society for Neurochemistry The AMPA-type glutamate receptor (AMPA-R) plays a primary role in principal excitatory synaptic transmission and many neuronal functions including synaptic plasticity that underlie learning and memory. N-glycosylation is one of the major post-translational modifications of membrane proteins, but its specific roles in neurons remain largely unknown. AMPA-R subunits are N-glycosylated at their extracellular domains during their biosynthesis in the lumen of the endoplasmic reticulum and Golgi system. Six N-glycosylation sites are presumed to exist in the extracellular domain of GluA1, which is a member of the AMPA-R subunits. We observed that the intracellular trafficking and cell surface expression were strongly suppressed in the GluA1 mutants lacking N-glycans at N63/N363 in HEK293T cells. Multimer analysis using Blue Native-PAGE displayed the impaired tetramer formation in the glycosylation mutants (N63S and N363S), indicating that the mis-transport was caused by impaired tetramer formation. N63S and N363S mutants were primarily degraded via the lysosomal pathway. Flag-tagged N363S GluA1, but not N63S GluA1, expressed in primary cortical neuron cultures prepared from GluA1 knockout mice was observed to localize at the cell surface. Co-expression of GluA2 partially rescued tetramer formation and the cell surface expression of N363S GluA1 but not N63S GluA1, in HEK293T cells. Electrophysiological analysis also demonstrated functional heteromers of N363S GluA1 with GluA2. These data suggest that site-specific N-glycans on GluA1 subunit regulates tetramer formation, intracellular trafficking, and cell surface expression of AMPA-R. Open science badges: This article has received a badge for *Open Materials* because it provided all relevant information to reproduce the study in the manuscript. The complete Open Science Disclosure form for this article can be found at the end of the article. More information about the Open Practices badges can be found at https://cos.io/our-services/open-science-badges/. (Figure presented.).
DOI： 10.1111/jnc.14565
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Selective injection system into hippocampus CA1 via monitored theta oscillation. Reviewed
Jyoji Tsutajima, Takato Kunitake, Yoshihiko Wakazono, Kogo Takamiya
PLoS One 8 ( 12 ) 2013.12
Language：English Publishing type：Research paper (scientific journal)
DOI： 10.1371
Books 【 display / non-display 】
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無敵のバイオテクニカルシリーズ（特別編）脳・神経研究の進めかた「基礎技術・細胞培養法」 （共著）
南木浩二、若園佳彦、池中一裕（ Role： Joint author）
羊土社 1998.5
Language：Japanese
MISC 【 display / non-display 】
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エバネッセンス顕微鏡 （共著）
寺川 進、桜井孝司、坪井貴司、菊田敏輝、若園佳彦、山本清二
生体の科学 2003.5
Language：Japanese Publishing type：Article, review, commentary, editorial, etc. (trade magazine, newspaper, online media) Publisher：医学書院
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小脳顆粒細胞分化・成熟と電位依存性カリウムチャネルの発現 （共著）
中平健祐、柴田理一、若園佳彦、池中一裕
蛋白質・核酸・酵素 2000.5
Language：Japanese Publishing type：Article, review, commentary, editorial, etc. (trade magazine, newspaper, online media) Publisher：共立出版
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小脳顆粒細胞の成熟 （共著）
若園佳彦、池中一裕
生理学研究所年報 1996.5
Language：Japanese Publishing type：Article, review, commentary, editorial, etc. (other) Publisher：岡崎国立共同研究機構 生理学研究所
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神経発生とカリウムチャネル （共著）
池中一裕、若園佳彦、秋田裕美、中平健祐
神経研究の進歩 1995.5
Language：Japanese Publishing type：Article, review, commentary, editorial, etc. (trade magazine, newspaper, online media) Publisher：医学書院
Presentations 【 display / non-display 】
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A crucial role of N-glycosylation of homomeric GluA1 AMPA receptor in LTP induction
Yoshihiko Wakazono, Ryosuke Midorikawa, Shogo Oka, Kogo Takamiya
第97回日本生理学会大会 (大分県別府市) 日本生理学会
Event date： 2020.3.17 - 2020.3.19
Language：English Presentation type：Poster presentation
Venue：大分県別府市
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AMPA受容体におけるN型糖鎖修飾の神経可塑性メカニズムの電気生理学的解析
若園 佳彦, 緑川 良介, 岡 昌吾 , 高宮 考悟
第70回西日本生理学会大会 (宮崎県宮崎市) 西日本生理学会
Event date： 2019.11.1 - 2019.11.2
Language：Japanese Presentation type：Oral presentation (general)
Venue：宮崎県宮崎市
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N-glycosylation of homomeric GluA1 AMPA receptor play a key role in synaptic plasticity
Yoshihiko Wakazono, Ryosuke Midorikawa, Munal B. Kandel, Shogo Oka, Kogo Takamiya
NEURO2019 (新潟県新潟市) 日本神経科学学会、日本神経化学学会
Event date： 2019.7.25 - 2019.7.28
Language：English Presentation type：Poster presentation
Venue：新潟県新潟市
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Arsenic and its metabolites promote internalization of surface AMPA receptors
Yoshihiko Wakazono, Harishkumar Madhyastha, Ryosuke Midorikawa, Masugi Maruyama, Kogo Takamiya
第41回日本神経科学大会 (兵庫県神戸市) 日本神経科学学会
Event date： 2018.7.26 - 2018.7.29
Language：English Presentation type：Poster presentation
Venue：兵庫県神戸市
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Arsenic and its metabolites affect synaptic plasticity mediated by AMPA type glutamate receptor trafficking in neurons
Yoshihiko Wakazono, Harishkumar Madhyastha, Ryosuke Midorikawa, Masugi Maruyama and Kogo Takamiya
第95回日本生理学会大会 (香川県高松市) 日本生理学会
Event date： 2018.3.28 - 2018.3.30
Language：English Presentation type：Poster presentation
Venue：香川県高松市
Grant-in-Aid for Scientific Research 【 display / non-display 】
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グルタミン酸受容体の糖鎖修飾による脳高次機能と精神疾患への関与
Grant number：21K07483 2021.04 - 2024.03
独立行政法人日本学術振興会 科学研究費補助金 基盤研究(C)
高宮 考悟、
Authorship：Coinvestigator(s)
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自由行動下、細胞レベルでのｉｎ ｖｉｖｏイメージング装置の開発と場所細胞への適用
2012.04 - 2014.03
科学研究費補助金 挑戦的萌芽研究
Authorship：Principal investigator
自由行動下、細胞レベルでのｉｎ ｖｉｖｏイメージング装置の開発と場所細胞への適用