{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T23:01:57Z","timestamp":1773270117308,"version":"3.50.1"},"reference-count":60,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2022,12,5]],"date-time":"2022-12-05T00:00:00Z","timestamp":1670198400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/100012835","name":"Toho University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012835","id-type":"DOI","asserted-by":"publisher"}]},{"name":"JSPS KAKENHI","award":["JP21K06861"],"award-info":[{"award-number":["JP21K06861"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,3,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>\u03b1-Synuclein is a protein linked to various synuclein-associated diseases (\u2018synucleinopathies\u2019), including Parkinson\u2019s disease, dementia with Lewy Bodies and multiple system atrophy, and is highly expressed in the central nervous system and in erythrocytes. Moreover, \u03b1-synuclein-containing erythrocyte-derived extracellular vesicles may be involved in the pathogenesis of synucleinopathies and their progression across the blood\u2013brain barrier. Several post-translational modifications of \u03b1-synuclein have been reported in brain inclusions, including S129 phosphorylation, but fewer have been found in erythrocytes. In this study, we analysed the post-translational modifications of erythrocyte \u03b1-synuclein using liquid chromatography\u2013mass spectrometry. We found that all lysine residues in the \u03b1-synuclein protein could be modified by acetylation, glycation, ubiquitination or SUMOylation but that phosphorylation, nitration and acylation were uncommon minor post-translational modifications in erythrocytes. Since the post-translational modification of lysine residues has been implicated in both membrane association and protein clearance, our findings provide new insight into how synucleinopathies may progress and suggest possible therapeutic strategies designed to target \u03b1-synuclein.<\/jats:p>","DOI":"10.1093\/jb\/mvac100","type":"journal-article","created":{"date-parts":[[2022,12,5]],"date-time":"2022-12-05T20:07:38Z","timestamp":1670270858000},"page":"177-184","source":"Crossref","is-referenced-by-count":10,"title":["Post-translational modification of lysine residues in erythrocyte \u03b1-synuclein"],"prefix":"10.1093","volume":"173","author":[{"given":"Ryosuke","family":"Amagai","sequence":"first","affiliation":[{"name":"Toho University Laboratory of Biochemistry, Department of Biology, Faculty of Science, , 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sakura","family":"Yoshioka","sequence":"additional","affiliation":[{"name":"Toho University Laboratory of Biochemistry, Department of Biology, Faculty of Science, , 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Riki","family":"Otomo","sequence":"additional","affiliation":[{"name":"Toho University Laboratory of Biochemistry, Department of Biology, Faculty of Science, , 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hidekazu","family":"Nagano","sequence":"additional","affiliation":[{"name":"Chiba University Graduate School of Medicine Department of Molecular Diagnosis, , Chiba, Chiba 260-8670, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naoko","family":"Hashimoto","sequence":"additional","affiliation":[{"name":"Chiba University Graduate School of Medicine Department of Molecular Diagnosis, , Chiba, Chiba 260-8670, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ryuji","family":"Sakakibara","sequence":"additional","affiliation":[{"name":"Toho University Division of Neurology, Department of Internal Medicine, Sakura Medical Center, , Sakura, Chiba 285-8741, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9761-1750","authenticated-orcid":false,"given":"Tomoaki","family":"Tanaka","sequence":"additional","affiliation":[{"name":"Chiba University Graduate School of Medicine Department of Molecular Diagnosis, , Chiba, Chiba 260-8670, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0026-7453","authenticated-orcid":false,"given":"Ayako","family":"Okado-Matsumoto","sequence":"additional","affiliation":[{"name":"Toho University Laboratory of Biochemistry, Department of Biology, Faculty of Science, , 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2022,12,5]]},"reference":[{"key":"2023030810061860400_","doi-asserted-by":"crossref","first-page":"134316","DOI":"10.1016\/j.neulet.2019.134316","article-title":"\u03b1-Synuclein pathology in Parkinson\u2019s disease and related \u03b1-synucleinopathies","volume":"709","author":"Henderson","year":"2019","journal-title":"Neurosci. 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