Angiostrongylus cantonensis infection induces MMP-9 and causes tight junction protein disruption associated with Purkinje cell degeneration
Angiostrongylus cantonensis causes a human central nervous system (CNS) infection characterized by eosinophilic meningitis or meningoencephalitis. Individuals infected with A. cantonensis exhibit unbalanced walking. The mechanism of extensive neurological impairments of hosts caused by A. cantonensi...
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| Veröffentlicht in: | Parasitology research (1987) 2020-10, Vol.119 (10), p.3433-3441 |
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| creator | Lai, Shih-Chan Lu, Cheng-You Shyu, Ling-Yuh Chen, Ke-Min |
| description | Angiostrongylus cantonensis
causes a human central nervous system (CNS) infection characterized by eosinophilic meningitis or meningoencephalitis. Individuals infected with
A. cantonensis
exhibit unbalanced walking. The mechanism of extensive neurological impairments of hosts caused by
A. cantonensis
larvae remains unclear. Tight junction proteins (e.g., claudin-5 and zonula occludens-1) are the most important regulators of paracellular permeability and cellular adhesion. In a previous study, we found that increased matrix metalloproteinase-9 (MMP-9) activity may be associated with blood–CNS barrier disruption and/or the degeneration of Purkinje cells in eosinophilic meningitis caused by
A. cantonensis
. In the present study, the co-localization of MMP-9 and tight junction proteins on the degeneration of Purkinje cells was measured via confocal laser scanning immunofluorescence microscopy. The statistical evidence indicated that MMP-9 correlated between tight junction protein disruption and Purkinje cell degeneration at 20 days post-infection with
A. cantonensis
. In conclusion, Purkinje cell degeneration is highly correlated with tight junction protein disruption via the MMP-9 activation pathway. |
| doi_str_mv | 10.1007/s00436-020-06840-y |
| format | Article |
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causes a human central nervous system (CNS) infection characterized by eosinophilic meningitis or meningoencephalitis. Individuals infected with
A. cantonensis
exhibit unbalanced walking. The mechanism of extensive neurological impairments of hosts caused by
A. cantonensis
larvae remains unclear. Tight junction proteins (e.g., claudin-5 and zonula occludens-1) are the most important regulators of paracellular permeability and cellular adhesion. In a previous study, we found that increased matrix metalloproteinase-9 (MMP-9) activity may be associated with blood–CNS barrier disruption and/or the degeneration of Purkinje cells in eosinophilic meningitis caused by
A. cantonensis
. In the present study, the co-localization of MMP-9 and tight junction proteins on the degeneration of Purkinje cells was measured via confocal laser scanning immunofluorescence microscopy. The statistical evidence indicated that MMP-9 correlated between tight junction protein disruption and Purkinje cell degeneration at 20 days post-infection with
A. cantonensis
. In conclusion, Purkinje cell degeneration is highly correlated with tight junction protein disruption via the MMP-9 activation pathway.</description><identifier>ISSN: 0932-0113</identifier><identifier>EISSN: 1432-1955</identifier><identifier>DOI: 10.1007/s00436-020-06840-y</identifier><identifier>PMID: 32789733</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Angiostrongylus cantonensis ; Angiostrongylus cantonensis - physiology ; Animals ; Biomedical and Life Sciences ; Biomedicine ; Central nervous system ; Degeneration ; Disease Models, Animal ; Gelatinase B ; Health aspects ; Helminthology - Original Paper ; Immunofluorescence ; Immunology ; Infections ; Larva - physiology ; Leukocytes (eosinophilic) ; Localization ; Matrix metalloproteinase ; Matrix Metalloproteinase 9 - metabolism ; Medical Microbiology ; Meningitis ; Meningoencephalitis ; Metalloproteinase ; Mice ; Microbiology ; Permeability ; Physiological aspects ; Proteins ; Purkinje cells ; Purkinje Cells - metabolism ; Purkinje Cells - parasitology ; Purkinje Cells - pathology ; Strongylida Infections - metabolism ; Strongylida Infections - parasitology ; Strongylida Infections - pathology ; Tight Junction Proteins - metabolism ; Zonula occludens-1 protein</subject><ispartof>Parasitology research (1987), 2020-10, Vol.119 (10), p.3433-3441</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020</rights><rights>COPYRIGHT 2020 Springer</rights><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357y-d31fccaae29b54c9773dd1a97216ec4a230c26721e0b6ec640fc06529e0b66c23</citedby><cites>FETCH-LOGICAL-c357y-d31fccaae29b54c9773dd1a97216ec4a230c26721e0b6ec640fc06529e0b66c23</cites><orcidid>0000-0002-2778-3098</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00436-020-06840-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00436-020-06840-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32789733$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lai, Shih-Chan</creatorcontrib><creatorcontrib>Lu, Cheng-You</creatorcontrib><creatorcontrib>Shyu, Ling-Yuh</creatorcontrib><creatorcontrib>Chen, Ke-Min</creatorcontrib><title>Angiostrongylus cantonensis infection induces MMP-9 and causes tight junction protein disruption associated with Purkinje cell degeneration</title><title>Parasitology research (1987)</title><addtitle>Parasitol Res</addtitle><addtitle>Parasitol Res</addtitle><description>Angiostrongylus cantonensis
causes a human central nervous system (CNS) infection characterized by eosinophilic meningitis or meningoencephalitis. Individuals infected with
A. cantonensis
exhibit unbalanced walking. The mechanism of extensive neurological impairments of hosts caused by
A. cantonensis
larvae remains unclear. Tight junction proteins (e.g., claudin-5 and zonula occludens-1) are the most important regulators of paracellular permeability and cellular adhesion. In a previous study, we found that increased matrix metalloproteinase-9 (MMP-9) activity may be associated with blood–CNS barrier disruption and/or the degeneration of Purkinje cells in eosinophilic meningitis caused by
A. cantonensis
. In the present study, the co-localization of MMP-9 and tight junction proteins on the degeneration of Purkinje cells was measured via confocal laser scanning immunofluorescence microscopy. The statistical evidence indicated that MMP-9 correlated between tight junction protein disruption and Purkinje cell degeneration at 20 days post-infection with
A. cantonensis
. In conclusion, Purkinje cell degeneration is highly correlated with tight junction protein disruption via the MMP-9 activation pathway.</description><subject>Angiostrongylus cantonensis</subject><subject>Angiostrongylus cantonensis - physiology</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Central nervous system</subject><subject>Degeneration</subject><subject>Disease Models, Animal</subject><subject>Gelatinase B</subject><subject>Health aspects</subject><subject>Helminthology - Original Paper</subject><subject>Immunofluorescence</subject><subject>Immunology</subject><subject>Infections</subject><subject>Larva - physiology</subject><subject>Leukocytes (eosinophilic)</subject><subject>Localization</subject><subject>Matrix metalloproteinase</subject><subject>Matrix Metalloproteinase 9 - metabolism</subject><subject>Medical Microbiology</subject><subject>Meningitis</subject><subject>Meningoencephalitis</subject><subject>Metalloproteinase</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Permeability</subject><subject>Physiological aspects</subject><subject>Proteins</subject><subject>Purkinje cells</subject><subject>Purkinje Cells - metabolism</subject><subject>Purkinje Cells - parasitology</subject><subject>Purkinje Cells - pathology</subject><subject>Strongylida Infections - metabolism</subject><subject>Strongylida Infections - parasitology</subject><subject>Strongylida Infections - pathology</subject><subject>Tight Junction Proteins - metabolism</subject><subject>Zonula occludens-1 protein</subject><issn>0932-0113</issn><issn>1432-1955</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kk1v1DAQhiMEokvhD3BAkbhwSRl_xN4cVxUUpFb0AGfL60xSL1l78Yeq_Ab-dJ1uoQIh5IM942dGr8dvVb0mcEYA5PsIwJlogEIDYs2hmZ9UK8IZbUjXtk-rFXTlDISwk-pFjDsAIgXnz6sTRuW6k4ytqp8bN1ofU_BunKcca6Nd8g5dtLG2bkCTrHfl1GeDsb66um66Wru-cDmWRLLjTap32R25Q_AJrat7G0M-3Kd0jN5YnbCvb226qa9z-G7dDmuD01T3OKLDoBf0ZfVs0FPEVw_7afXt44ev55-ayy8Xn883l41hrZybnpHBGK2RdtuWm05K1vdEd5ISgYZrysBQUSKEbUkIDoMB0dJuiYWh7LR6d-xb1P7IGJPa27io0Q59jopyxqFtJSzo27_Qnc_BFXWFaoETtu7gkRr1hKpMzaegzdJUbQQTZeqSskKd_YMqq8e9NWXmgy35PwroscAEH2PAQR2C3eswKwJqcYA6OkAVB6h7B6i5FL15UJy3e-x_l_z68gKwIxDLlRsxPD7pP23vABYwvZg</recordid><startdate>20201001</startdate><enddate>20201001</enddate><creator>Lai, Shih-Chan</creator><creator>Lu, Cheng-You</creator><creator>Shyu, Ling-Yuh</creator><creator>Chen, Ke-Min</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-2778-3098</orcidid></search><sort><creationdate>20201001</creationdate><title>Angiostrongylus cantonensis infection induces MMP-9 and causes tight junction protein disruption associated with Purkinje cell degeneration</title><author>Lai, Shih-Chan ; Lu, Cheng-You ; Shyu, Ling-Yuh ; Chen, Ke-Min</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357y-d31fccaae29b54c9773dd1a97216ec4a230c26721e0b6ec640fc06529e0b66c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Angiostrongylus cantonensis</topic><topic>Angiostrongylus cantonensis - physiology</topic><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Central nervous system</topic><topic>Degeneration</topic><topic>Disease Models, Animal</topic><topic>Gelatinase B</topic><topic>Health aspects</topic><topic>Helminthology - Original Paper</topic><topic>Immunofluorescence</topic><topic>Immunology</topic><topic>Infections</topic><topic>Larva - physiology</topic><topic>Leukocytes (eosinophilic)</topic><topic>Localization</topic><topic>Matrix metalloproteinase</topic><topic>Matrix Metalloproteinase 9 - metabolism</topic><topic>Medical Microbiology</topic><topic>Meningitis</topic><topic>Meningoencephalitis</topic><topic>Metalloproteinase</topic><topic>Mice</topic><topic>Microbiology</topic><topic>Permeability</topic><topic>Physiological aspects</topic><topic>Proteins</topic><topic>Purkinje cells</topic><topic>Purkinje Cells - metabolism</topic><topic>Purkinje Cells - parasitology</topic><topic>Purkinje Cells - pathology</topic><topic>Strongylida Infections - metabolism</topic><topic>Strongylida Infections - parasitology</topic><topic>Strongylida Infections - pathology</topic><topic>Tight Junction Proteins - metabolism</topic><topic>Zonula occludens-1 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lai, Shih-Chan</creatorcontrib><creatorcontrib>Lu, Cheng-You</creatorcontrib><creatorcontrib>Shyu, Ling-Yuh</creatorcontrib><creatorcontrib>Chen, Ke-Min</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Parasitology research (1987)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lai, Shih-Chan</au><au>Lu, Cheng-You</au><au>Shyu, Ling-Yuh</au><au>Chen, Ke-Min</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Angiostrongylus cantonensis infection induces MMP-9 and causes tight junction protein disruption associated with Purkinje cell degeneration</atitle><jtitle>Parasitology research (1987)</jtitle><stitle>Parasitol Res</stitle><addtitle>Parasitol Res</addtitle><date>2020-10-01</date><risdate>2020</risdate><volume>119</volume><issue>10</issue><spage>3433</spage><epage>3441</epage><pages>3433-3441</pages><issn>0932-0113</issn><eissn>1432-1955</eissn><abstract>Angiostrongylus cantonensis
causes a human central nervous system (CNS) infection characterized by eosinophilic meningitis or meningoencephalitis. Individuals infected with
A. cantonensis
exhibit unbalanced walking. The mechanism of extensive neurological impairments of hosts caused by
A. cantonensis
larvae remains unclear. Tight junction proteins (e.g., claudin-5 and zonula occludens-1) are the most important regulators of paracellular permeability and cellular adhesion. In a previous study, we found that increased matrix metalloproteinase-9 (MMP-9) activity may be associated with blood–CNS barrier disruption and/or the degeneration of Purkinje cells in eosinophilic meningitis caused by
A. cantonensis
. In the present study, the co-localization of MMP-9 and tight junction proteins on the degeneration of Purkinje cells was measured via confocal laser scanning immunofluorescence microscopy. The statistical evidence indicated that MMP-9 correlated between tight junction protein disruption and Purkinje cell degeneration at 20 days post-infection with
A. cantonensis
. In conclusion, Purkinje cell degeneration is highly correlated with tight junction protein disruption via the MMP-9 activation pathway.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>32789733</pmid><doi>10.1007/s00436-020-06840-y</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-2778-3098</orcidid></addata></record> |
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| ispartof | Parasitology research (1987), 2020-10, Vol.119 (10), p.3433-3441 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Angiostrongylus cantonensis Angiostrongylus cantonensis - physiology Animals Biomedical and Life Sciences Biomedicine Central nervous system Degeneration Disease Models, Animal Gelatinase B Health aspects Helminthology - Original Paper Immunofluorescence Immunology Infections Larva - physiology Leukocytes (eosinophilic) Localization Matrix metalloproteinase Matrix Metalloproteinase 9 - metabolism Medical Microbiology Meningitis Meningoencephalitis Metalloproteinase Mice Microbiology Permeability Physiological aspects Proteins Purkinje cells Purkinje Cells - metabolism Purkinje Cells - parasitology Purkinje Cells - pathology Strongylida Infections - metabolism Strongylida Infections - parasitology Strongylida Infections - pathology Tight Junction Proteins - metabolism Zonula occludens-1 protein |
| title | Angiostrongylus cantonensis infection induces MMP-9 and causes tight junction protein disruption associated with Purkinje cell degeneration |
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