{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T07:53:41Z","timestamp":1768809221213,"version":"3.49.0"},"reference-count":44,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2013,7,29]],"date-time":"2013-07-29T00:00:00Z","timestamp":1375056000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Neuropathology"],"published-print":{"date-parts":[[2014,2]]},"abstract":"<jats:p><jats:styled-content style=\"fixed-case\">FIG4<\/jats:styled-content> is a phosphatase that regulates intracellular vesicle trafficking along the endosomal\u2010lysosomal pathway. Mutations of <jats:italic><jats:styled-content style=\"fixed-case\">FIG4<\/jats:styled-content><\/jats:italic> lead to the development of <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>harcot<jats:styled-content style=\"fixed-case\">\u2010M<\/jats:styled-content>arie\u2010<jats:styled-content style=\"fixed-case\">T<\/jats:styled-content>ooth disease type <jats:styled-content style=\"fixed-case\">4J<\/jats:styled-content> and amyotrophic lateral sclerosis (<jats:styled-content style=\"fixed-case\">ALS<\/jats:styled-content>). Moreover, <jats:styled-content style=\"fixed-case\">ALS<\/jats:styled-content>\u2010associated proteins (transactivation response <jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content> protein 43 (<jats:styled-content style=\"fixed-case\">TDP<\/jats:styled-content>\u201043), fused in sarcoma (<jats:styled-content style=\"fixed-case\">FUS<\/jats:styled-content>), optineurin, ubiquilin\u20102, charged mutivesicular body protein 2b (<jats:styled-content style=\"fixed-case\">CHMP2B<\/jats:styled-content>) and valosin\u2010containing protein) are involved in inclusion body formation in several neurodegenerative diseases. Using immunohistochemistry, we examined the brains and spinal cords of patients with various neurodegenerative diseases, including sporadic <jats:styled-content style=\"fixed-case\">TDP<\/jats:styled-content>\u201043 proteinopathy (<jats:styled-content style=\"fixed-case\">ALS<\/jats:styled-content> and frontotemporal lobar degeneration). <jats:styled-content style=\"fixed-case\">TDP<\/jats:styled-content>\u201043 proteinopathy demonstrated no <jats:styled-content style=\"fixed-case\">FIG4<\/jats:styled-content> immunoreactivity in neuronal inclusions. However, <jats:styled-content style=\"fixed-case\">FIG4<\/jats:styled-content> immunoreactivity was present in <jats:styled-content style=\"fixed-case\">P<\/jats:styled-content>ick bodies in <jats:styled-content style=\"fixed-case\">P<\/jats:styled-content>ick's disease, <jats:styled-content style=\"fixed-case\">L<\/jats:styled-content>ewy bodies in <jats:styled-content style=\"fixed-case\">P<\/jats:styled-content>arkinson's disease and dementia with <jats:styled-content style=\"fixed-case\">L<\/jats:styled-content>ewy bodies, neuronal nuclear inclusions in polyglutamine and intranuclear inclusion body diseases, and <jats:styled-content style=\"fixed-case\">M<\/jats:styled-content>arinesco and <jats:styled-content style=\"fixed-case\">H<\/jats:styled-content>irano bodies in aged control subjects. These findings suggest that <jats:styled-content style=\"fixed-case\">FIG4<\/jats:styled-content> is not incorporated in <jats:styled-content style=\"fixed-case\">TDP<\/jats:styled-content>\u201043 inclusions and that it may have a common role in the formation or degradation of neuronal cytoplasmic and nuclear inclusions in several neurodegenerative diseases.<\/jats:p>","DOI":"10.1111\/neup.12056","type":"journal-article","created":{"date-parts":[[2013,7,29]],"date-time":"2013-07-29T10:36:53Z","timestamp":1375094213000},"page":"19-26","source":"Crossref","is-referenced-by-count":27,"title":["<scp>ALS<\/scp>\u2010associated protein <scp>FIG4<\/scp> is localized in <scp>P<\/scp>ick and <scp>L<\/scp>ewy bodies, and also neuronal nuclear inclusions, in polyglutamine and intranuclear inclusion body diseases"],"prefix":"10.1111","volume":"34","author":[{"given":"Tomoya","family":"Kon","sequence":"first","affiliation":[{"name":"Department of Neuropathology Hirosaki University Graduate School 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