{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,7]],"date-time":"2026-01-07T07:47:21Z","timestamp":1767772041295},"reference-count":35,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2015,5,18]],"date-time":"2015-05-18T00:00:00Z","timestamp":1431907200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Neuroscience Research"],"published-print":{"date-parts":[[2015,9]]},"abstract":"<jats:p>Neurons have well\u2010developed membrane microdomains called \u201crafts\u201d that are recovered as a detergent\u2010resistant membrane microdomain fraction (DRM). Neuronal tissue\u2010enriched acidic protein of 22 kDa (NAP\u201022) is one of the major protein components of neuronal DRM. To determine the cellular function of NAP\u201022, interacting proteins were screened with an immunoprecipitation assay, and calcineurin (CaN) was detected. Further studies with NAP\u201022 prepared from DRM and CaN expressed in bacteria showed the binding of these proteins and a dose\u2010dependent inhibitory effect of the NAP\u201022 fraction on the phosphatase activity of CaN. On the other hand, NAP\u201022 expressed in bacteria showed low binding to CaN and a weak inhibitory effect on phosphatase activity. To solve this discrepancy, identification of a nonprotein component that modulates CaN activity in the DRM\u2010derived NAP\u201022 fraction was attempted. After lyophilization, a lipid fraction was extracted with chloroform\/methanol. The lipid fraction showed an inhibitory effect on CaN without NAP\u201022, and further fractionation of the extract with thin\u2010layer chromatography showed the presence of several lipid bands having an inhibitory effect on CaN. The mobility of these bands coincided with that of authentic ganglioside (GM1a, GD1a, GD1b, and GT1b), and authentic ganglioside showed an inhibitory effect on CaN. Treatment of lipid with endoglycoceramidase, which degrades ganglioside to glycochain and ceramide, caused a diminution of the inhibitory effect. These results show that DRM\u2010derived NAP\u201022 binds several lipids, including ganglioside, and that ganglioside inhibits the phosphatase activity of CaN. \u00a9 2015 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/jnr.23599","type":"journal-article","created":{"date-parts":[[2015,5,18]],"date-time":"2015-05-18T07:08:14Z","timestamp":1431932894000},"page":"1462-1470","source":"Crossref","is-referenced-by-count":10,"title":["Ganglioside contained in the neuronal tissue\u2010enriched acidic protein of 22 kDa (NAP\u201022) fraction prepared from the detergent\u2010resistant membrane microdomain of rat brain inhibits the phosphatase activity of calcineurin"],"prefix":"10.1002","volume":"93","author":[{"given":"Yuumi","family":"Kobayashi","sequence":"first","affiliation":[{"name":"Department of Biology Graduate School of Science Kobe University Kobe Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ronan","family":"da Silva","sequence":"additional","affiliation":[{"name":"Department of Biology Graduate School of Science Kobe University Kobe Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Haruko","family":"Kumanogoh","sequence":"additional","affiliation":[{"name":"Division of Biochemistry and Cellular Biology National Institute of Neuroscience National Center of Neurology and Psychiatry Kodaira Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shinji","family":"Miyata","sequence":"additional","affiliation":[{"name":"Bioscience and Biotechnology Center Nagoya University Nagoya Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chihiro","family":"Sato","sequence":"additional","affiliation":[{"name":"Bioscience and Biotechnology Center Nagoya University Nagoya Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ken","family":"Kitajima","sequence":"additional","affiliation":[{"name":"Bioscience and Biotechnology Center Nagoya University Nagoya Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shun","family":"Nakamura","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Life Science Tokyo University of Agriculture and Technology Koganei Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mistuhiro","family":"Morita","sequence":"additional","affiliation":[{"name":"Department of Biology Graduate School of Science Kobe University Kobe Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fumio","family":"Hayashi","sequence":"additional","affiliation":[{"name":"Department of Biology Graduate School of Science Kobe University Kobe Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shohei","family":"Maekawa","sequence":"additional","affiliation":[{"name":"Department of Biology Graduate School of Science Kobe University Kobe Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2015,5,18]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.abb.2006.08.012"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1471-4159.1990.tb13288.x"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/3.1.57"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkn955"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0812101106"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1006\/prep.1997.0807"},{"key":"e_1_2_8_8_1","doi-asserted-by":"crossref","first-page":"9831","DOI":"10.1016\/S0021-9258(19)50169-7","article-title":"Calmodulin, a ganglioside\u2010binding protein. 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