New Treatment for Alzheimer’s Disease, Kamikihito, Reverses Amyloid- β -Induced Progression of Tau Phosphorylation and Axonal Atrophy
Aims. We previously reported that kamikihito (KKT), a traditional Japanese medicine, improved memory impairment and reversed the degeneration of axons in the 5XFAD mouse model of Alzheimer’s disease (AD). However, the mechanism underlying the effects of KKT remained unknown. The aim of the present s...
Gespeichert in:
| Veröffentlicht in: | Evidence-based complementary and alternative medicine 2014-01, Vol.2014 (2014), p.1-10 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 10 |
|---|---|
| container_issue | 2014 |
| container_start_page | 1 |
| container_title | Evidence-based complementary and alternative medicine |
| container_volume | 2014 |
| creator | Watari, Hidetoshi Tohda, Chihiro Shimada, Yutaka |
| description | Aims. We previously reported that kamikihito (KKT), a traditional Japanese medicine, improved memory impairment and reversed the degeneration of axons in the 5XFAD mouse model of Alzheimer’s disease (AD). However, the mechanism underlying the effects of KKT remained unknown. The aim of the present study was to investigate the mechanism by which KKT reverses the progression of axonal degeneration. Methods. Primary cultured cortical neurons were treated with amyloid beta (Aβ) fragment comprising amino acid residues (25–35) (10 μM) in an in vitro AD model. KKT (10 μg/mL) was administered to the cells before or after Aβ treatment. The effects of KKT on Aβ-induced tau phosphorylation, axonal atrophy, and protein phosphatase 2A (PP2A) activity were investigated. We also performed an in vivo assay in which KKT (500 mg/kg/day) was administered to 5XFAD mice once a day for 15 days. Cerebral cortex homogenates were used to measure PP2A activity. Results. KKT improved Aβ-induced tau phosphorylation and axonal atrophy after they had already progressed. In addition, KKT increased PP2A activity in vitro and in vivo. Conclusions. KKT reversed the progression of Aβ-induced axonal degeneration. KKT reversed axonal degeneration at least in part through its role as an exogenous PP2A stimulator. |
| doi_str_mv | 10.1155/2014/706487 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3953424</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1768581068</sourcerecordid><originalsourceid>FETCH-LOGICAL-c463t-3e424b694c142adb6c19e95dc1422a05a5c0d97c547e67f340d3293b29a3d2fc3</originalsourceid><addsrcrecordid>eNqNkstu1DAUhi0Eou3Aij2yxAZBQ32N4w1S1HKpqKBCg8TO8sQnjUsSD3bSMqxY8gq8Bg_CQ_AkZDRlVNjAypfz6T_-j3-E7lHyhFIpDxih4kCRXBTqBtqlStBMsKK4ud2r9ztoL6VzQphWSt1GO0woojilu-jra7jE8wh26KAfcB0iLtvPDfgO4s8v3xI-8glsgn38ynb-g2_8EPbxW7iAmCDhslu1wbsM__iOs-PejRU4fBrDWYSUfOhxqPHcjvi0CWnZhLhq7bC-tr3D5afQ2xaXQwzLZnUH3aptm-Du1TpD754_mx--zE7evDg-LE-ySuR8yDgIJha5FhUVzLpFXlENWrr1kVkirayI06qSQkGuai6I40zzBdOWO1ZXfIaebnSX46IDV02uo23NMvrOxpUJ1ps_K71vzFm4MFxLPvWeBB5eCcTwcYQ0mM6nCtrW9hDGZKjKC1lQkhf_RiUVgueFWKMP_kLPwxin-STDSM4KQuXkf4Yeb6gqhpQi1Nt3U2LWYTDrMJhNGCb6_nWrW_b370_Aow3Q-N7ZS_9_ajAhUNtrMC001fwXVMnIRA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2062801546</pqid></control><display><type>article</type><title>New Treatment for Alzheimer’s Disease, Kamikihito, Reverses Amyloid- β -Induced Progression of Tau Phosphorylation and Axonal Atrophy</title><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central Open Access</source><source>Wiley-Blackwell Open Access Titles</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Watari, Hidetoshi ; Tohda, Chihiro ; Shimada, Yutaka</creator><contributor>Kogure, Toshiaki ; Toshiaki Kogure</contributor><creatorcontrib>Watari, Hidetoshi ; Tohda, Chihiro ; Shimada, Yutaka ; Kogure, Toshiaki ; Toshiaki Kogure</creatorcontrib><description>Aims. We previously reported that kamikihito (KKT), a traditional Japanese medicine, improved memory impairment and reversed the degeneration of axons in the 5XFAD mouse model of Alzheimer’s disease (AD). However, the mechanism underlying the effects of KKT remained unknown. The aim of the present study was to investigate the mechanism by which KKT reverses the progression of axonal degeneration. Methods. Primary cultured cortical neurons were treated with amyloid beta (Aβ) fragment comprising amino acid residues (25–35) (10 μM) in an in vitro AD model. KKT (10 μg/mL) was administered to the cells before or after Aβ treatment. The effects of KKT on Aβ-induced tau phosphorylation, axonal atrophy, and protein phosphatase 2A (PP2A) activity were investigated. We also performed an in vivo assay in which KKT (500 mg/kg/day) was administered to 5XFAD mice once a day for 15 days. Cerebral cortex homogenates were used to measure PP2A activity. Results. KKT improved Aβ-induced tau phosphorylation and axonal atrophy after they had already progressed. In addition, KKT increased PP2A activity in vitro and in vivo. Conclusions. KKT reversed the progression of Aβ-induced axonal degeneration. KKT reversed axonal degeneration at least in part through its role as an exogenous PP2A stimulator.</description><identifier>ISSN: 1741-427X</identifier><identifier>EISSN: 1741-4288</identifier><identifier>DOI: 10.1155/2014/706487</identifier><identifier>PMID: 24707311</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Alzheimer's disease ; Amino acids ; Atrophy ; Axons ; Cerebral cortex ; Dementia ; Drugs ; Experiments ; Herbal medicine ; Kinases ; Laboratory animals ; Medical treatment ; Memory ; Neurodegeneration ; Phosphoprotein phosphatase ; Phosphorylation ; Protein phosphatase ; Stimulators ; Tau protein ; Ziziphus jujuba</subject><ispartof>Evidence-based complementary and alternative medicine, 2014-01, Vol.2014 (2014), p.1-10</ispartof><rights>Copyright © 2014 Hidetoshi Watari et al.</rights><rights>Copyright © 2014 Hidetoshi Watari 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</rights><rights>Copyright © 2014 Hidetoshi Watari et al. 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-3e424b694c142adb6c19e95dc1422a05a5c0d97c547e67f340d3293b29a3d2fc3</citedby><cites>FETCH-LOGICAL-c463t-3e424b694c142adb6c19e95dc1422a05a5c0d97c547e67f340d3293b29a3d2fc3</cites><orcidid>0000-0002-2836-0492 ; 0000-0002-4254-9523</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3953424/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3953424/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24707311$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Kogure, Toshiaki</contributor><contributor>Toshiaki Kogure</contributor><creatorcontrib>Watari, Hidetoshi</creatorcontrib><creatorcontrib>Tohda, Chihiro</creatorcontrib><creatorcontrib>Shimada, Yutaka</creatorcontrib><title>New Treatment for Alzheimer’s Disease, Kamikihito, Reverses Amyloid- β -Induced Progression of Tau Phosphorylation and Axonal Atrophy</title><title>Evidence-based complementary and alternative medicine</title><addtitle>Evid Based Complement Alternat Med</addtitle><description>Aims. We previously reported that kamikihito (KKT), a traditional Japanese medicine, improved memory impairment and reversed the degeneration of axons in the 5XFAD mouse model of Alzheimer’s disease (AD). However, the mechanism underlying the effects of KKT remained unknown. The aim of the present study was to investigate the mechanism by which KKT reverses the progression of axonal degeneration. Methods. Primary cultured cortical neurons were treated with amyloid beta (Aβ) fragment comprising amino acid residues (25–35) (10 μM) in an in vitro AD model. KKT (10 μg/mL) was administered to the cells before or after Aβ treatment. The effects of KKT on Aβ-induced tau phosphorylation, axonal atrophy, and protein phosphatase 2A (PP2A) activity were investigated. We also performed an in vivo assay in which KKT (500 mg/kg/day) was administered to 5XFAD mice once a day for 15 days. Cerebral cortex homogenates were used to measure PP2A activity. Results. KKT improved Aβ-induced tau phosphorylation and axonal atrophy after they had already progressed. In addition, KKT increased PP2A activity in vitro and in vivo. Conclusions. KKT reversed the progression of Aβ-induced axonal degeneration. KKT reversed axonal degeneration at least in part through its role as an exogenous PP2A stimulator.</description><subject>Alzheimer's disease</subject><subject>Amino acids</subject><subject>Atrophy</subject><subject>Axons</subject><subject>Cerebral cortex</subject><subject>Dementia</subject><subject>Drugs</subject><subject>Experiments</subject><subject>Herbal medicine</subject><subject>Kinases</subject><subject>Laboratory animals</subject><subject>Medical treatment</subject><subject>Memory</subject><subject>Neurodegeneration</subject><subject>Phosphoprotein phosphatase</subject><subject>Phosphorylation</subject><subject>Protein phosphatase</subject><subject>Stimulators</subject><subject>Tau protein</subject><subject>Ziziphus jujuba</subject><issn>1741-427X</issn><issn>1741-4288</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkstu1DAUhi0Eou3Aij2yxAZBQ32N4w1S1HKpqKBCg8TO8sQnjUsSD3bSMqxY8gq8Bg_CQ_AkZDRlVNjAypfz6T_-j3-E7lHyhFIpDxih4kCRXBTqBtqlStBMsKK4ud2r9ztoL6VzQphWSt1GO0woojilu-jra7jE8wh26KAfcB0iLtvPDfgO4s8v3xI-8glsgn38ynb-g2_8EPbxW7iAmCDhslu1wbsM__iOs-PejRU4fBrDWYSUfOhxqPHcjvi0CWnZhLhq7bC-tr3D5afQ2xaXQwzLZnUH3aptm-Du1TpD754_mx--zE7evDg-LE-ySuR8yDgIJha5FhUVzLpFXlENWrr1kVkirayI06qSQkGuai6I40zzBdOWO1ZXfIaebnSX46IDV02uo23NMvrOxpUJ1ps_K71vzFm4MFxLPvWeBB5eCcTwcYQ0mM6nCtrW9hDGZKjKC1lQkhf_RiUVgueFWKMP_kLPwxin-STDSM4KQuXkf4Yeb6gqhpQi1Nt3U2LWYTDrMJhNGCb6_nWrW_b370_Aow3Q-N7ZS_9_ajAhUNtrMC001fwXVMnIRA</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Watari, Hidetoshi</creator><creator>Tohda, Chihiro</creator><creator>Shimada, Yutaka</creator><general>Hindawi Publishing Corporation</general><general>Hindawi Limited</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7RV</scope><scope>7T5</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88G</scope><scope>8AO</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>K9.</scope><scope>KB0</scope><scope>M0S</scope><scope>M2M</scope><scope>M2O</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PSYQQ</scope><scope>Q9U</scope><scope>7X8</scope><scope>7TK</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2836-0492</orcidid><orcidid>https://orcid.org/0000-0002-4254-9523</orcidid></search><sort><creationdate>20140101</creationdate><title>New Treatment for Alzheimer’s Disease, Kamikihito, Reverses Amyloid- β -Induced Progression of Tau Phosphorylation and Axonal Atrophy</title><author>Watari, Hidetoshi ; Tohda, Chihiro ; Shimada, Yutaka</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-3e424b694c142adb6c19e95dc1422a05a5c0d97c547e67f340d3293b29a3d2fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Alzheimer's disease</topic><topic>Amino acids</topic><topic>Atrophy</topic><topic>Axons</topic><topic>Cerebral cortex</topic><topic>Dementia</topic><topic>Drugs</topic><topic>Experiments</topic><topic>Herbal medicine</topic><topic>Kinases</topic><topic>Laboratory animals</topic><topic>Medical treatment</topic><topic>Memory</topic><topic>Neurodegeneration</topic><topic>Phosphoprotein phosphatase</topic><topic>Phosphorylation</topic><topic>Protein phosphatase</topic><topic>Stimulators</topic><topic>Tau protein</topic><topic>Ziziphus jujuba</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Watari, Hidetoshi</creatorcontrib><creatorcontrib>Tohda, Chihiro</creatorcontrib><creatorcontrib>Shimada, Yutaka</creatorcontrib><collection>الدوريات العلمية والإحصائية - e-Marefa Academic and Statistical Periodicals</collection><collection>معرفة - المحتوى العربي الأكاديمي المتكامل - e-Marefa Academic Complete</collection><collection>Hindawi Publishing Complete</collection><collection>Hindawi Publishing Subscription Journals</collection><collection>Hindawi Publishing Open Access Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nursing & Allied Health Database</collection><collection>Immunology Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Psychology Database (Alumni)</collection><collection>ProQuest Pharma Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Psychology Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest One Psychology</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Neurosciences Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Evidence-based complementary and alternative medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watari, Hidetoshi</au><au>Tohda, Chihiro</au><au>Shimada, Yutaka</au><au>Kogure, Toshiaki</au><au>Toshiaki Kogure</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New Treatment for Alzheimer’s Disease, Kamikihito, Reverses Amyloid- β -Induced Progression of Tau Phosphorylation and Axonal Atrophy</atitle><jtitle>Evidence-based complementary and alternative medicine</jtitle><addtitle>Evid Based Complement Alternat Med</addtitle><date>2014-01-01</date><risdate>2014</risdate><volume>2014</volume><issue>2014</issue><spage>1</spage><epage>10</epage><pages>1-10</pages><issn>1741-427X</issn><eissn>1741-4288</eissn><abstract>Aims. We previously reported that kamikihito (KKT), a traditional Japanese medicine, improved memory impairment and reversed the degeneration of axons in the 5XFAD mouse model of Alzheimer’s disease (AD). However, the mechanism underlying the effects of KKT remained unknown. The aim of the present study was to investigate the mechanism by which KKT reverses the progression of axonal degeneration. Methods. Primary cultured cortical neurons were treated with amyloid beta (Aβ) fragment comprising amino acid residues (25–35) (10 μM) in an in vitro AD model. KKT (10 μg/mL) was administered to the cells before or after Aβ treatment. The effects of KKT on Aβ-induced tau phosphorylation, axonal atrophy, and protein phosphatase 2A (PP2A) activity were investigated. We also performed an in vivo assay in which KKT (500 mg/kg/day) was administered to 5XFAD mice once a day for 15 days. Cerebral cortex homogenates were used to measure PP2A activity. Results. KKT improved Aβ-induced tau phosphorylation and axonal atrophy after they had already progressed. In addition, KKT increased PP2A activity in vitro and in vivo. Conclusions. KKT reversed the progression of Aβ-induced axonal degeneration. KKT reversed axonal degeneration at least in part through its role as an exogenous PP2A stimulator.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><pmid>24707311</pmid><doi>10.1155/2014/706487</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-2836-0492</orcidid><orcidid>https://orcid.org/0000-0002-4254-9523</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1741-427X |
| ispartof | Evidence-based complementary and alternative medicine, 2014-01, Vol.2014 (2014), p.1-10 |
| issn | 1741-427X 1741-4288 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3953424 |
| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central Open Access; Wiley-Blackwell Open Access Titles; PubMed Central; Alma/SFX Local Collection |
| subjects | Alzheimer's disease Amino acids Atrophy Axons Cerebral cortex Dementia Drugs Experiments Herbal medicine Kinases Laboratory animals Medical treatment Memory Neurodegeneration Phosphoprotein phosphatase Phosphorylation Protein phosphatase Stimulators Tau protein Ziziphus jujuba |
| title | New Treatment for Alzheimer’s Disease, Kamikihito, Reverses Amyloid- β -Induced Progression of Tau Phosphorylation and Axonal Atrophy |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T04%3A21%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=New%20Treatment%20for%20Alzheimer%E2%80%99s%20Disease,%20Kamikihito,%20Reverses%20Amyloid-%20%CE%B2%20-Induced%20Progression%20of%20Tau%20Phosphorylation%20and%20Axonal%20Atrophy&rft.jtitle=Evidence-based%20complementary%20and%20alternative%20medicine&rft.au=Watari,%20Hidetoshi&rft.date=2014-01-01&rft.volume=2014&rft.issue=2014&rft.spage=1&rft.epage=10&rft.pages=1-10&rft.issn=1741-427X&rft.eissn=1741-4288&rft_id=info:doi/10.1155/2014/706487&rft_dat=%3Cproquest_pubme%3E1768581068%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2062801546&rft_id=info:pmid/24707311&rfr_iscdi=true |