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Misfolding and accumulation of endogenous A\u03b2 can lead to neural cell apoptosis through endoplasmic reticulum (<jats:styled-content style=\"fixed-case\">ER<\/jats:styled-content>) stress. Added exogenous A\u03b2 can also result in <jats:styled-content style=\"fixed-case\">ER<\/jats:styled-content> stress, leading to neurotoxicity and apoptosis, which is identical to that caused by the endogenous peptide. We have speculated that the endocytic transport of A\u03b2 causes <jats:styled-content style=\"fixed-case\">ER<\/jats:styled-content> stress and have previously shown that the oxysterol, in particular, 7\u2010ketocholesterol (7\u2010keto) induces more surface interaction between A\u03b2\u201042 and Jurkat cells than cholesterol. However, the interaction was not enough to induce intracellular transfer of the peptide. In this study, we investigated the effect of another oxysterol, 25\u2010hydroxycholesterol (25\u2010OH) on the membrane raft\u2010dependent transport of A\u03b2\u201042 in Jurkat cells. Interestingly, intracellular transfer of A\u03b2\u201042 was observed in the presence of 25\u2010<jats:styled-content style=\"fixed-case\">OH<\/jats:styled-content> only after the inclusion of cholera toxin B subunit (CT\u2010B), a marker used to detect the raft domain. We speculated that 25\u2010<jats:styled-content style=\"fixed-case\">OH<\/jats:styled-content> can induce intracellular movement of A\u03b2 peptides. Furthermore, <jats:styled-content style=\"fixed-case\">CT<\/jats:styled-content>\u2010B together with <jats:styled-content style=\"fixed-case\">GM<\/jats:styled-content>1 provided negative curvature, which resulted in the intracellular transport of A\u03b2\u201042. Notably, we used a protofibrillar species of A\u03b2\u201042 in this study. We have shown that the transport was microtubule\u2010dependent since it could not be observed in depolymerized microtubules. These results demonstrate that oxysterols and glycosyl chains are important factors affecting intracellular transport. These compounds are also associated with aging and advanced glycation are risk factors for <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content>. Thus, this study should further understanding of the pathology of <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content>.<\/jats:p>","DOI":"10.1002\/2211-5463.12234","type":"journal-article","created":{"date-parts":[[2017,4,26]],"date-time":"2017-04-26T08:10:20Z","timestamp":1493194220000},"page":"865-876","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Glycosyl chains and 25\u2010hydroxycholesterol contribute to the intracellular transport of amyloid beta (A\u03b2\u201042) in Jurkat T cells"],"prefix":"10.1002","volume":"7","author":[{"given":"Neha","family":"Sharma","sequence":"first","affiliation":[{"name":"School of Materials Science Japan Advanced Institute of Science and Technology (JAIST) Ishikawa Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"KeangOK","family":"Baek","sequence":"additional","affiliation":[{"name":"School of Materials Science Japan Advanced Institute 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