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  1. Article: [Development of demetia therapeutics regurating synaptic plasticity].

    Fukunaga, Kohji

    Nihon yakurigaku zasshi. Folia pharmacologica Japonica

    2023  Volume 158, Issue 3, Page(s) 218–222

    Abstract: Alzheimer's disease (AD) is the most common dementia in the world characterized by the neuropathological hallmarks consisting of an accumulation of extracellular amyloid-β (Aβ) plaques and intracellular neurofibrillary tangles (NFT). There is no ... ...

    Abstract Alzheimer's disease (AD) is the most common dementia in the world characterized by the neuropathological hallmarks consisting of an accumulation of extracellular amyloid-β (Aβ) plaques and intracellular neurofibrillary tangles (NFT). There is no fundamental therapeutic treatment. We have developed a novel AD therapeutic candidate SAK3 which improves neuronal plasticity in the brain. SAK3 enhanced the acetylcholine release via T-type calcium channels. T-type calcium channels is highly expressed in neuro-progenitor cells in the hippocampal dentate gyrus. SAK3 enhanced the proliferation and differentiation of the neuro-progenitor cells, thereby improving depressive behaviors. The Cav3.1 null mice impaired the proliferation and differentiation of the neuro-progenitor cells. In addition, SAK3 activated CaMKII involving neuronal plasticity, thereby improving spine regeneration and proteasome activities impaired in AD related App
    MeSH term(s) Mice ; Animals ; Calcium Channels, T-Type/physiology ; Proteasome Endopeptidase Complex/therapeutic use ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Alzheimer Disease/drug therapy ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/therapeutic use ; Mice, Knockout ; Neuronal Plasticity
    Chemical Substances Calcium Channels, T-Type ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 (EC 2.7.11.17) ; Amyloid beta-Peptides
    Language Japanese
    Publishing date 2023-03-29
    Publishing country Japan
    Document type English Abstract ; Journal Article
    ZDB-ID 1097532-9
    ISSN 1347-8397 ; 0015-5691
    ISSN (online) 1347-8397
    ISSN 0015-5691
    DOI 10.1254/fpj.22138
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Protein Kinases and Neurodegenerative Diseases.

    Kawahata, Ichiro / Fukunaga, Kohji

    International journal of molecular sciences

    2023  Volume 24, Issue 6

    Abstract: Global aging has led to an increase in age-related neurological disorders, which have become a societal problem [ ... ]. ...

    Abstract Global aging has led to an increase in age-related neurological disorders, which have become a societal problem [...].
    MeSH term(s) Humans ; Neurodegenerative Diseases ; Protein Kinases ; Aging
    Chemical Substances Protein Kinases (EC 2.7.-)
    Language English
    Publishing date 2023-03-14
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms24065574
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  3. Article: Editorial: Environmental risk factors in autism spectrum disorder.

    Matsuzaki, Hideo / Fukunaga, Kohji

    Frontiers in psychiatry

    2022  Volume 13, Page(s) 978489

    Language English
    Publishing date 2022-08-23
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2564218-2
    ISSN 1664-0640
    ISSN 1664-0640
    DOI 10.3389/fpsyt.2022.978489
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  4. Article ; Online: Protein Kinases and Neurodegenerative Diseases

    Ichiro Kawahata / Kohji Fukunaga

    International Journal of Molecular Sciences, Vol 24, Iss 5574, p

    2023  Volume 5574

    Abstract: Global aging has led to an increase in age-related neurological disorders, which have become a societal problem [.] ...

    Abstract Global aging has led to an increase in age-related neurological disorders, which have become a societal problem [.]
    Keywords n/a ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Language English
    Publishing date 2023-03-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Pathogenic Impact of Fatty Acid-Binding Proteins in Parkinson's Disease-Potential Biomarkers and Therapeutic Targets.

    Kawahata, Ichiro / Fukunaga, Kohji

    International journal of molecular sciences

    2023  Volume 24, Issue 23

    Abstract: Parkinson's disease is a neurodegenerative condition characterized by motor dysfunction resulting from the degeneration of dopamine-producing neurons in the midbrain. This dopamine deficiency gives rise to a spectrum of movement-related symptoms, ... ...

    Abstract Parkinson's disease is a neurodegenerative condition characterized by motor dysfunction resulting from the degeneration of dopamine-producing neurons in the midbrain. This dopamine deficiency gives rise to a spectrum of movement-related symptoms, including tremors, rigidity, and bradykinesia. While the precise etiology of Parkinson's disease remains elusive, genetic mutations, protein aggregation, inflammatory processes, and oxidative stress are believed to contribute to its development. In this context, fatty acid-binding proteins (FABPs) in the central nervous system, FABP3, FABP5, and FABP7, impact α-synuclein aggregation, neurotoxicity, and neuroinflammation. These FABPs accumulate in mitochondria during neurodegeneration, disrupting their membrane potential and homeostasis. In particular, FABP3, abundant in nigrostriatal dopaminergic neurons, is responsible for α-synuclein propagation into neurons and intracellular accumulation, affecting the loss of mesencephalic tyrosine hydroxylase protein, a rate-limiting enzyme of dopamine biosynthesis. This review summarizes the characteristics of FABP family proteins and delves into the pathogenic significance of FABPs in the pathogenesis of Parkinson's disease. Furthermore, it examines potential novel therapeutic targets and early diagnostic biomarkers for Parkinson's disease and related neurodegenerative disorders.
    MeSH term(s) Humans ; Parkinson Disease/genetics ; Parkinson Disease/drug therapy ; alpha-Synuclein/metabolism ; Dopamine/metabolism ; Fatty Acid-Binding Proteins/genetics ; Fatty Acid-Binding Proteins/metabolism ; Neurodegenerative Diseases/metabolism ; Dopaminergic Neurons/metabolism
    Chemical Substances alpha-Synuclein ; Dopamine (VTD58H1Z2X) ; Fatty Acid-Binding Proteins ; FABP5 protein, human
    Language English
    Publishing date 2023-12-01
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms242317037
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  6. Article ; Online: Pathogenic Impact of Fatty Acid-Binding Proteins in Parkinson’s Disease—Potential Biomarkers and Therapeutic Targets

    Ichiro Kawahata / Kohji Fukunaga

    International Journal of Molecular Sciences, Vol 24, Iss 23, p

    2023  Volume 17037

    Abstract: Parkinson’s disease is a neurodegenerative condition characterized by motor dysfunction resulting from the degeneration of dopamine-producing neurons in the midbrain. This dopamine deficiency gives rise to a spectrum of movement-related symptoms, ... ...

    Abstract Parkinson’s disease is a neurodegenerative condition characterized by motor dysfunction resulting from the degeneration of dopamine-producing neurons in the midbrain. This dopamine deficiency gives rise to a spectrum of movement-related symptoms, including tremors, rigidity, and bradykinesia. While the precise etiology of Parkinson’s disease remains elusive, genetic mutations, protein aggregation, inflammatory processes, and oxidative stress are believed to contribute to its development. In this context, fatty acid-binding proteins (FABPs) in the central nervous system, FABP3, FABP5, and FABP7, impact α-synuclein aggregation, neurotoxicity, and neuroinflammation. These FABPs accumulate in mitochondria during neurodegeneration, disrupting their membrane potential and homeostasis. In particular, FABP3, abundant in nigrostriatal dopaminergic neurons, is responsible for α-synuclein propagation into neurons and intracellular accumulation, affecting the loss of mesencephalic tyrosine hydroxylase protein, a rate-limiting enzyme of dopamine biosynthesis. This review summarizes the characteristics of FABP family proteins and delves into the pathogenic significance of FABPs in the pathogenesis of Parkinson’s disease. Furthermore, it examines potential novel therapeutic targets and early diagnostic biomarkers for Parkinson’s disease and related neurodegenerative disorders.
    Keywords Parkinson’s disease ; tyrosine hydroxylase ; dopaminergic neurons ; fatty acid-binding protein ; α-synuclein ; mitochondria ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 571
    Language English
    Publishing date 2023-12-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Endocytosis of dopamine receptor: Signaling in brain.

    Kawahata, Ichiro / Fukunaga, Kohji

    Progress in molecular biology and translational science

    2022  Volume 196, Page(s) 99–111

    Abstract: This chapter describes the physiological significance of dopamine receptor endocytosis and the consequence of the receptor signaling. Endocytosis of dopamine receptors is regulated by many components such as clathrin, β-arrestin, caveolin, and Rab family ...

    Abstract This chapter describes the physiological significance of dopamine receptor endocytosis and the consequence of the receptor signaling. Endocytosis of dopamine receptors is regulated by many components such as clathrin, β-arrestin, caveolin, and Rab family proteins. The dopamine receptors escape from lysosomal digestion, and their recycling occurs rapidly, reinforcing the dopaminergic signal transduction. In addition, the pathological impact of the receptors interacting with specific proteins has been the focus of much attention. Based on this background, this chapter provides an in-depth understanding of the mechanisms of molecules interacting with dopamine receptors and discusses the potential pharmacotherapeutic targets for α-synucleinopathies and neuropsychiatric disorders.
    MeSH term(s) Humans ; Receptors, Dopamine ; Signal Transduction ; Endocytosis ; Brain/metabolism ; beta-Arrestins/metabolism
    Chemical Substances Receptors, Dopamine ; beta-Arrestins
    Language English
    Publishing date 2022-10-22
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2471995-X
    ISSN 1878-0814 ; 0079-6603 ; 1877-1173
    ISSN (online) 1878-0814
    ISSN 0079-6603 ; 1877-1173
    DOI 10.1016/bs.pmbts.2022.09.005
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    Uc I Zs 357: Show issues Location:
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  8. Article: [Development of therapeutic peptides for Lewy body diseases preventing α-synuclein propagation].

    Kawahata, Ichiro / Fukunaga, Kohji

    Nihon yakurigaku zasshi. Folia pharmacologica Japonica

    2022  Volume 157, Issue 6, Page(s) 401–404

    Abstract: With the advent of a super-aging society, overcoming age-related neurological diseases and developing fundamental therapeutic agents are urgent issues. In Lewy body diseases such as Parkinson's disease and dementia with Lewy bodies, the accumulation and ... ...

    Abstract With the advent of a super-aging society, overcoming age-related neurological diseases and developing fundamental therapeutic agents are urgent issues. In Lewy body diseases such as Parkinson's disease and dementia with Lewy bodies, the accumulation and aggregation of α-synuclein in the neuronal cells, called Lewy bodies, are known as pathological features. Intracellular accumulation of the causative protein α-synuclein in the central nervous system requires an uptake process into neurons. Type 3 fatty acid-binding protein (FABP3) is highly expressed in dopaminergic neurons and has the ability to bind dopamine receptors, particularly dopamine D2 long type (D2L) receptors, which are abundantly localized on caveolae structures in the plasma membrane. We found that dopaminergic neurons do not take up α-synuclein in FABP3 knockout or D2L receptor-selective knockout mice. Next, we found that the C-terminal deletion of α-synuclein reduces the uptake ability. α-Synuclein has a FABP3 binding site in its C-terminal region. On this point, exposure to the C-terminal peptide reduced α-synuclein uptake into dopaminergic neurons. Based on these findings, this article describes the unique mechanism of the propagation and uptake process of α-synuclein, focusing on the physiological significance of FABP3 and dopamine D2 receptors. Additionally, we will review the development status of therapeutic peptide candidates for Lewy body diseases, and then discuss the novel pathogenic mechanism of Lewy body disease as well as the potential of fundamental therapeutics targeting the uptake process of α-synuclein.
    MeSH term(s) Animals ; Mice ; Lewy Body Disease/drug therapy ; Lewy Body Disease/metabolism ; Lewy Body Disease/pathology ; alpha-Synuclein ; Lewy Bodies/metabolism ; Lewy Bodies/pathology ; Dopaminergic Neurons/metabolism ; Mice, Knockout ; Peptides/metabolism
    Chemical Substances alpha-Synuclein ; Peptides
    Language Japanese
    Publishing date 2022-08-18
    Publishing country Japan
    Document type English Abstract ; Journal Article
    ZDB-ID 1097532-9
    ISSN 1347-8397 ; 0015-5691
    ISSN (online) 1347-8397
    ISSN 0015-5691
    DOI 10.1254/fpj.22055
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 439: Show issues Location:
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  9. Article: [Role of fatty acid-binding protein 7 and novel therapeutic approach in synucleinopathies].

    Cheng, An / Fukunaga, Kohji

    Nihon yakurigaku zasshi. Folia pharmacologica Japonica

    2022  Volume 157, Issue 6, Page(s) 396–400

    Abstract: The synucleinopathies are neurodegenerative disease caused by abnormal accumulation of the 140-amino acid-containing protein α-synuclein (αSyn), including Parkinson's disease (PD), diffuse Lewy body dementia (DLBD), and multiple system atrophy (MSA). In ... ...

    Abstract The synucleinopathies are neurodegenerative disease caused by abnormal accumulation of the 140-amino acid-containing protein α-synuclein (αSyn), including Parkinson's disease (PD), diffuse Lewy body dementia (DLBD), and multiple system atrophy (MSA). In patients with PD and DLBD, αSyn is misfolded in neurons, and its aggregation forms Lewy bodies (LB) and Lewy neurites (LN). On the other hand, in patients with MSA, αSyn accumulates primarily in oligodendrocytes (OLGs) and forms glial inclusion bodies (GCIs), a typical pathological feature of MSA. We recently demonstrated a making complex between αSyn and fatty acid-binding proteins (FABPs) in synucleinopathies and received wide attention. Fatty acid-binding protein 3 (FABP3) in dopamine nerves, and fatty acid-binding protein 7 (FABP7) in glial cells promoted αSyn accumulation and aggregation, respectively and caused cell death. Here, we introduced the current studies about the role of αSyn and FABP7 in MSA and novel therapeutic approach targeting for FABP7.
    MeSH term(s) Humans ; Synucleinopathies ; Fatty Acid-Binding Protein 7 ; Neurodegenerative Diseases/etiology ; alpha-Synuclein ; Lewy Body Disease/drug therapy ; Lewy Body Disease/metabolism ; Lewy Body Disease/pathology ; Parkinson Disease/therapy
    Chemical Substances Fatty Acid-Binding Protein 7 ; alpha-Synuclein
    Language Japanese
    Publishing date 2022-08-18
    Publishing country Japan
    Document type English Abstract ; Journal Article
    ZDB-ID 1097532-9
    ISSN 1347-8397 ; 0015-5691
    ISSN (online) 1347-8397
    ISSN 0015-5691
    DOI 10.1254/fpj.22056
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Feasibility and considerations of epsin2 as a candidate target for multiple system atrophy treatment.

    Cheng, An / Cai, Bo / Fukunaga, Kohji / Sasaki, Takuya / Lakkaraju, Aparna

    Expert opinion on therapeutic targets

    2023  Volume 27, Issue 11, Page(s) 1031–1034

    MeSH term(s) Humans ; Multiple System Atrophy/drug therapy ; Feasibility Studies ; alpha-Synuclein/metabolism ; Brain/metabolism
    Chemical Substances alpha-Synuclein
    Language English
    Publishing date 2023-12-07
    Publishing country England
    Document type Editorial ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2055208-7
    ISSN 1744-7631 ; 1472-8222
    ISSN (online) 1744-7631
    ISSN 1472-8222
    DOI 10.1080/14728222.2023.2277227
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    Zs.A 5244: Show issues Location:
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